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Conserved domains on  [gi|226958445|ref|NP_032074|]
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insulin-like growth factor-binding protein 7 isoform 2 precursor [Mus musculus]

Protein Classification

IB and Ig domain-containing protein (domain architecture ID 12189917)

protein containing domains IB, KAZAL_FS, and Ig

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IB smart00121
Insulin growth factor-binding protein homologues; High affinity binding partners of ...
32-90 3.07e-13

Insulin growth factor-binding protein homologues; High affinity binding partners of insulin-like growth factors.


:

Pssm-ID: 197525  Cd Length: 75  Bit Score: 64.02  E-value: 3.07e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 226958445    32 CGPCVPASCPALPrLGCPLGETRDACGCCPVCARGEGEPCGggaAGRGHCAPGMECVKS 90
Cdd:smart00121   3 CPPCDPARCPPCP-PGCAELVRLDGCGCCPVCARQEGEPCG---VYTPRCAPGLRCQPP 57
I-set super family cl28434
Immunoglobulin I-set domain;
160-265 1.90e-11

Immunoglobulin I-set domain;


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 333254  Cd Length: 90  Bit Score: 59.58  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445  160 PSIVTPPKDIWNVTGAKVFLSCEVIGIPTPVLIWNKvkrdhsgvQRTELLPGDRenLAIQTRGGpeKHEVTgwvlVSPLS 239
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK--------DGQPLRSSDR--FKVTYEGG--TYTLT----ISNVQ 64
                          90       100
                  ....*....|....*....|....*.
gi 226958445  240 KEDAGEYECHASNSQGQASAAAKITV 265
Cdd:pfam07679  65 PDDSGKYTCVATNSAGEAEASAELTV 90
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
111-156 7.52e-05

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 40.36  E-value: 7.52e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 226958445   111 CVCKSRY-PVCGSNGITYPSGCQLRAASLraesRGEKAITQVSKGTC 156
Cdd:smart00280   4 EACPREYdPVCGSDGVTYSNECHLCKAAC----ESGKSIEVKHDGPC 46
 
Name Accession Description Interval E-value
IB smart00121
Insulin growth factor-binding protein homologues; High affinity binding partners of ...
32-90 3.07e-13

Insulin growth factor-binding protein homologues; High affinity binding partners of insulin-like growth factors.


Pssm-ID: 197525  Cd Length: 75  Bit Score: 64.02  E-value: 3.07e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 226958445    32 CGPCVPASCPALPrLGCPLGETRDACGCCPVCARGEGEPCGggaAGRGHCAPGMECVKS 90
Cdd:smart00121   3 CPPCDPARCPPCP-PGCAELVRLDGCGCCPVCARQEGEPCG---VYTPRCAPGLRCQPP 57
IGFBP pfam00219
Insulin-like growth factor binding protein;
33-87 2.37e-12

Insulin-like growth factor binding protein;


Pssm-ID: 306685  Cd Length: 53  Bit Score: 61.17  E-value: 2.37e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 226958445   33 GPCVPASCPALPRlGCPLGETRDACGCCPVCARGEGEPCGGGAagrGHCAPGMEC 87
Cdd:pfam00219   3 PPCDPERCPPPPP-GCPAGLVLDGCGCCPVCARQEGEPCGVYT---PPCDKGLRC 53
I-set pfam07679
Immunoglobulin I-set domain;
160-265 1.90e-11

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 59.58  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445  160 PSIVTPPKDIWNVTGAKVFLSCEVIGIPTPVLIWNKvkrdhsgvQRTELLPGDRenLAIQTRGGpeKHEVTgwvlVSPLS 239
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK--------DGQPLRSSDR--FKVTYEGG--TYTLT----ISNVQ 64
                          90       100
                  ....*....|....*....|....*.
gi 226958445  240 KEDAGEYECHASNSQGQASAAAKITV 265
Cdd:pfam07679  65 PDDSGKYTCVATNSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
174-265 1.65e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653  Cd Length: 85  Bit Score: 54.43  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445   174 GAKVFLSCEVIGIPTPVLIWNKVKRdhsgvqrTELLPGDRenlaIQTRGGPEKHEVTgwvlVSPLSKEDAGEYECHASNS 253
Cdd:smart00410   9 GESVTLSCEASGSPPPEVTWYKQGG-------KLLAESGR----FSVSRSGSTSTLT----ISNVTPEDSGTYTCAATNS 73
                           90
                   ....*....|..
gi 226958445   254 QGQASAAAKITV 265
Cdd:smart00410  74 SGSASSGTTLTV 85
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
177-262 3.54e-09

Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 319273  Cd Length: 70  Bit Score: 53.01  E-value: 3.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 177 VFLSCEVIGIPTPVLIWNKvkrdhsgvqrtellpgDRENLAIQTRGGPEKHEVTGWVLVSPLSKEDAGEYECHASNSQGQ 256
Cdd:cd00096    1 VTLTCSASGNPPPTITWLK----------------NGKPLPSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGS 64

                 ....*.
gi 226958445 257 ASAAAK 262
Cdd:cd00096   65 ASASVT 70
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
111-156 7.52e-05

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 40.36  E-value: 7.52e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 226958445   111 CVCKSRY-PVCGSNGITYPSGCQLRAASLraesRGEKAITQVSKGTC 156
Cdd:smart00280   4 EACPREYdPVCGSDGVTYSNECHLCKAAC----ESGKSIEVKHDGPC 46
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
113-156 3.00e-04

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052  Cd Length: 41  Bit Score: 38.79  E-value: 3.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 226958445 113 CKSRY-PVCGSNGITYPSGCQLRaaslRAESRGEKAITQVSKGTC 156
Cdd:cd00104    1 CPKEYdPVCGSDGKTYSNECHLG----CAACRSGRSITVAHNGPC 41
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
118-156 1.04e-03

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 311539  Cd Length: 42  Bit Score: 37.23  E-value: 1.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 226958445  118 PVCGSNGITYPSGCQLRAASLRAESRgekaITQVSKGTC 156
Cdd:pfam07648   8 PVCGSDGKTYGNKCALCCANCLLGEK----LKVKYEGSC 42
 
Name Accession Description Interval E-value
IB smart00121
Insulin growth factor-binding protein homologues; High affinity binding partners of ...
32-90 3.07e-13

Insulin growth factor-binding protein homologues; High affinity binding partners of insulin-like growth factors.


Pssm-ID: 197525  Cd Length: 75  Bit Score: 64.02  E-value: 3.07e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 226958445    32 CGPCVPASCPALPrLGCPLGETRDACGCCPVCARGEGEPCGggaAGRGHCAPGMECVKS 90
Cdd:smart00121   3 CPPCDPARCPPCP-PGCAELVRLDGCGCCPVCARQEGEPCG---VYTPRCAPGLRCQPP 57
IGFBP pfam00219
Insulin-like growth factor binding protein;
33-87 2.37e-12

Insulin-like growth factor binding protein;


Pssm-ID: 306685  Cd Length: 53  Bit Score: 61.17  E-value: 2.37e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 226958445   33 GPCVPASCPALPRlGCPLGETRDACGCCPVCARGEGEPCGGGAagrGHCAPGMEC 87
Cdd:pfam00219   3 PPCDPERCPPPPP-GCPAGLVLDGCGCCPVCARQEGEPCGVYT---PPCDKGLRC 53
I-set pfam07679
Immunoglobulin I-set domain;
160-265 1.90e-11

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 59.58  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445  160 PSIVTPPKDIWNVTGAKVFLSCEVIGIPTPVLIWNKvkrdhsgvQRTELLPGDRenLAIQTRGGpeKHEVTgwvlVSPLS 239
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK--------DGQPLRSSDR--FKVTYEGG--TYTLT----ISNVQ 64
                          90       100
                  ....*....|....*....|....*.
gi 226958445  240 KEDAGEYECHASNSQGQASAAAKITV 265
Cdd:pfam07679  65 PDDSGKYTCVATNSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
174-265 1.65e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653  Cd Length: 85  Bit Score: 54.43  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445   174 GAKVFLSCEVIGIPTPVLIWNKVKRdhsgvqrTELLPGDRenlaIQTRGGPEKHEVTgwvlVSPLSKEDAGEYECHASNS 253
Cdd:smart00410   9 GESVTLSCEASGSPPPEVTWYKQGG-------KLLAESGR----FSVSRSGSTSTLT----ISNVTPEDSGTYTCAATNS 73
                           90
                   ....*....|..
gi 226958445   254 QGQASAAAKITV 265
Cdd:smart00410  74 SGSASSGTTLTV 85
IG smart00409
Immunoglobulin;
174-265 1.65e-09

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 54.43  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445   174 GAKVFLSCEVIGIPTPVLIWNKVKRdhsgvqrTELLPGDRenlaIQTRGGPEKHEVTgwvlVSPLSKEDAGEYECHASNS 253
Cdd:smart00409   9 GESVTLSCEASGSPPPEVTWYKQGG-------KLLAESGR----FSVSRSGSTSTLT----ISNVTPEDSGTYTCAATNS 73
                           90
                   ....*....|..
gi 226958445   254 QGQASAAAKITV 265
Cdd:smart00409  74 SGSASSGTTLTV 85
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
177-262 3.54e-09

Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 319273  Cd Length: 70  Bit Score: 53.01  E-value: 3.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 177 VFLSCEVIGIPTPVLIWNKvkrdhsgvqrtellpgDRENLAIQTRGGPEKHEVTGWVLVSPLSKEDAGEYECHASNSQGQ 256
Cdd:cd00096    1 VTLTCSASGNPPPTITWLK----------------NGKPLPSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGS 64

                 ....*.
gi 226958445 257 ASAAAK 262
Cdd:cd00096   65 ASASVT 70
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
160-252 5.17e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 52.89  E-value: 5.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445  160 PSIVTPPKDIWNVTGAKVFLSCEVIGIPTPVLIWNKvkrdhsgvqrtellpgdrENLAIQTRGGPEKHEVTGWVLVSPLS 239
Cdd:pfam13927   2 PVITVSPSSVVVLEGESVTLTCEATGGPPPTITWYK------------------NGKPGPTSSRISLSGSNSTLTISNVT 63
                          90
                  ....*....|...
gi 226958445  240 KEDAGEYECHASN 252
Cdd:pfam13927  64 REDSGTYTCVASN 76
Ig3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third Ig domain of the ...
160-265 4.76e-07

Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third Ig domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 47.32  E-value: 4.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 160 PSIVTPPKDIWNVTGAKVFLSCEVIGIPTPVLIWNKVkrdhsgvqrTELLPGDREnlaIQTRGGPEKhevtgwvlVSPLS 239
Cdd:cd05851    2 ADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRKI---------LEPMPATAE---ISMSGAVLK--------IFNIQ 61
                         90       100
                 ....*....|....*....|....*.
gi 226958445 240 KEDAGEYECHASNSQGQASAAAKITV 265
Cdd:cd05851   62 PEDEGTYECEAENIKGKDKHQARVYV 87
Ig_Palladin_C cd05893
C-terminal immunoglobulin (Ig)-like domain of palladin; Ig_Palladin_C: C-terminal ...
177-265 2.18e-05

C-terminal immunoglobulin (Ig)-like domain of palladin; Ig_Palladin_C: C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (DIP, mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions.


Pssm-ID: 143301  Cd Length: 75  Bit Score: 42.35  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 177 VFLSCEVIGIPTPVLIWNKvkRDHSGVQRTELLPGDRENlaiqtrggpekhevTGWV--LVSPLSKEDAGEYECHASNSQ 254
Cdd:cd05893    1 VRLECRVSGVPHPQIFWKK--ENESLTHNTDRVSMHQDN--------------CGYIclLIQGATKEDAGWYTVSAKNEA 64
                         90
                 ....*....|.
gi 226958445 255 GQASAAAKITV 265
Cdd:cd05893   65 GIVSCTARLDV 75
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: ...
177-265 2.76e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: domain similar to the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 319298  Cd Length: 71  Bit Score: 42.03  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 177 VFLSCEVIGIPTPVLIWNKVKRDhsgvqrtelLPGDREnlaiqtrggpeKHEVTGWVL-VSPLSKEDAGEYECHASNSQG 255
Cdd:cd05731    1 LLLECIAEGLPTPDIRWIKLGGE---------LPKGRT-----------KFENFNKTLkIENVSEADSGEYQCTASNTMG 60
                         90
                 ....*....|
gi 226958445 256 QASAAAKITV 265
Cdd:cd05731   61 SARHTISVTV 70
Ig2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
174-265 2.85e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); Ig2_FGFRL1-like: second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 143264  Cd Length: 82  Bit Score: 42.13  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 174 GAKVFLSCEVIGIPTPVLIWNKvkrdhsgvqrtellpgDRENLAIQTRGGPEKHEvtgWVL-VSPLSKEDAGEYECHASN 252
Cdd:cd05856    9 GSSVRLKCVASGNPRPDITWLK----------------DNKPLTPTEIGESRKKK---WTLsLKNLKPEDSGKYTCHVSN 69
                         90
                 ....*....|...
gi 226958445 253 SQGQASAAAKITV 265
Cdd:cd05856   70 RAGEINATYKVDV 82
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
111-156 7.52e-05

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 40.36  E-value: 7.52e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 226958445   111 CVCKSRY-PVCGSNGITYPSGCQLRAASLraesRGEKAITQVSKGTC 156
Cdd:smart00280   4 EACPREYdPVCGSDGVTYSNECHLCKAAC----ESGKSIEVKHDGPC 46
Ig_NCAM-1 cd05869
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: ...
176-265 8.21e-05

Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: immunoglobulin (Ig)-like domain similar to the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143277  Cd Length: 97  Bit Score: 41.12  E-value: 8.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 176 KVFLSCEVIGIPTPVLIWNKVKRDHSGVQRTelLPGdreNLAIQTrggpekHEVTGWVLVSPLSKEDAGEYECHASNSQG 255
Cdd:cd05869   19 QITLTCEASGDPIPSITWRTSTRNISSEEKT--LDG---HIVVRS------HARVSSLTLKYIQYTDAGEYLCTASNTIG 87
                         90
                 ....*....|
gi 226958445 256 QASAAAKITV 265
Cdd:cd05869   88 QDSQSMYLEV 97
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third ...
174-265 1.23e-04

Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death, and protection of the organism against non-self.


Pssm-ID: 143222  Cd Length: 74  Bit Score: 40.31  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 174 GAKVFLSCEVIGIPTPVLIWNKvkrdhSGVQrtelLPGDRENLAIQTrggpekhevtGWVLVSPLSKEDAGEYECHASNS 253
Cdd:cd05745    2 GQTVDFLCEAQGYPQPVIAWTK-----GGSQ----LSVDRRHLVLSS----------GTLRISRVALHDQGQYECQAVNI 62
                         90
                 ....*....|..
gi 226958445 254 QGQASAAAKITV 265
Cdd:cd05745   63 VGSQRTVAQLTV 74
Ig2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain ...
166-265 1.34e-04

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain similar to the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 143201  Cd Length: 86  Bit Score: 40.07  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 166 PKDIWNVTGAKVFLSCEV-IGIPTPVLIWNKvkrdhSGVqrtellPGDRENLAIQTRGGpekhevtGWVLVSPLSKEDAG 244
Cdd:cd05724    3 PSDTQVAVGEMAVLECSPpRGHPEPTVSWRK-----DGQ------PLNLDNERVRIVDD-------GNLLIAEARKSDEG 64
                         90       100
                 ....*....|....*....|..
gi 226958445 245 EYECHASNSQG-QASAAAKITV 265
Cdd:cd05724   65 TYKCVATNMVGeRESAAARLSV 86
Ig1_Neogenin cd05722
First immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig1_Neogenin: first ...
161-265 2.75e-04

First immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig1_Neogenin: first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC, which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain.


Pssm-ID: 143199  Cd Length: 95  Bit Score: 39.38  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 161 SIVTPPKDIWNVTGAKVFLSCEVIGIPTPVLIWnkvKRDHSGVQ-----RTELLPGDreNLAIQTrggpekhevtgwVLV 235
Cdd:cd05722    1 WFLSEPSDIVAVRGGPVVLNCSAEGEPPPKIEW---KKDGVLLNlvsdeRRQQLPNG--SLLITS------------VVH 63
                         90       100       110
                 ....*....|....*....|....*....|..
gi 226958445 236 SPLSKEDAGEYECHASN-SQGQ-ASAAAKITV 265
Cdd:cd05722   64 SKHNKPDEGFYQCVAQNdSLGSiVSRTARLTV 95
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
113-156 3.00e-04

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052  Cd Length: 41  Bit Score: 38.79  E-value: 3.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 226958445 113 CKSRY-PVCGSNGITYPSGCQLRaaslRAESRGEKAITQVSKGTC 156
Cdd:cd00104    1 CPKEYdPVCGSDGKTYSNECHLG----CAACRSGRSITVAHNGPC 41
Ig_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; Ig_Myotilin_like_C: ...
177-265 3.10e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; Ig_Myotilin_like_C: immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners: all three bind to alpha-actinin; in addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP).


Pssm-ID: 319304  Cd Length: 75  Bit Score: 39.13  E-value: 3.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 177 VFLSCEVIGIPTPVLIWNKvkrdhsgvqrtellpgDRENLAIQTRGGPEKHEVTGWV--LVSPLSKEDAGEYECHASNSQ 254
Cdd:cd05744    1 VKLECQVLAIPPPQIFWKK----------------ENEMLQFNTDRISLYQDNHGRIclLIKDVTKEDAGWYTVSAKNEA 64
                         90
                 ....*....|.
gi 226958445 255 GQASAAAKITV 265
Cdd:cd05744   65 GITSCNARLDV 75
Ig1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; Ig1_Contactin: First Ig domain of contactins. ...
159-255 3.36e-04

First immunoglobulin (Ig) domain of contactin; Ig1_Contactin: First Ig domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 319276  Cd Length: 91  Bit Score: 39.12  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 159 GPSIVTPPKDIWNVTGA---KVFLSCEVIGIPTPVLIWnkvKRDHSGVqrtELLPGDRENLAiqtrGGpekhevtGWVLV 235
Cdd:cd04967    1 GPVFEEQPDDTIFPEESdeeKVALNCRARANPPPTYRW---KMNGTEI---KLEPDSRYSLV----GG-------NLVIS 63
                         90       100
                 ....*....|....*....|
gi 226958445 236 SPLSKEDAGEYECHASNSQG 255
Cdd:cd04967   64 NPSKAKDAGHYQCLATNTVG 83
IGc2 smart00408
Immunoglobulin C-2 Type;
174-255 3.39e-04

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 38.93  E-value: 3.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445   174 GAKVFLSCEVIGIPTPVLIWNKvkrdhsgvqrtellpgdrENLAIQTRGgpeKHEVTGWVL-VSPLSKEDAGEYECHASN 252
Cdd:smart00408   2 GQSVTLTCPAEGNPVPNITWLK------------------DGKPLPESN---RFVASGSTLtIKSVSLEDSGLYTCVAEN 60

                   ...
gi 226958445   253 SQG 255
Cdd:smart00408  61 SAG 63
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; ...
166-265 6.82e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; Ig4_Contactin-2-like: fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (aliases TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205  Cd Length: 85  Bit Score: 37.96  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 166 PKDIWNVTGAKVFLSCEVIGIPTPVLIWnkvkrdhsgVQRTELLPGDREnlaIQTRGGPekhevtgwVLVSPLSKEDAGE 245
Cdd:cd05728    6 ISDTEADIGSSLRWECKASGNPRPAYRW---------LKNGQPLASENR---IEVEAGD--------LRITKLSLSDSGM 65
                         90       100
                 ....*....|....*....|
gi 226958445 246 YECHASNSQGQASAAAKITV 265
Cdd:cd05728   66 YQCVAENKHGTIYASAELAV 85
Ig_NCAM-1_like cd05732
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar ...
172-260 6.92e-04

Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar proteins; Ig_NCAM-1 like: domain similar to the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE).


Pssm-ID: 143209  Cd Length: 96  Bit Score: 38.28  E-value: 6.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 172 VTGAKVFLSCEVIGIPTPVLIWNKVKRDHSGVQRTelLPGDrenlaIQTRGgpeKHEVTGWVLVSpLSKEDAGEYECHAS 251
Cdd:cd05732   14 VELEQITLTCEAEGDPIPEITWRRATRNFSEGDKS--LDGR-----IVVRG---HARVSSLTLKD-VQLTDAGRYDCEAS 82

                 ....*....
gi 226958445 252 NSQGQASAA 260
Cdd:cd05732   83 NRIGGDQQS 91
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
179-266 1.03e-03

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); Ig4_L1-NrCAM_like: fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 319284  Cd Length: 76  Bit Score: 37.44  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 179 LSCEVIGIPTPVLIW--NKVKrdhsgvqrTELLPGDRENLaiqtrggpekheVTGWVLV-SPLSKEDAGEYECHASNSQG 255
Cdd:cd04978    6 LICEAEGNPQPTITWrlNGVP--------IEPAPEDMRRT------------VDGRTLIfSNLQPNDTAVYQCNASNVHG 65
                         90
                 ....*....|.
gi 226958445 256 QASAAAKITVV 266
Cdd:cd04978   66 YLLANAFLHVL 76
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
118-156 1.04e-03

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 311539  Cd Length: 42  Bit Score: 37.23  E-value: 1.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 226958445  118 PVCGSNGITYPSGCQLRAASLRAESRgekaITQVSKGTC 156
Cdd:pfam07648   8 PVCGSDGKTYGNKCALCCANCLLGEK----LKVKYEGSC 42
Ig1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; Ig1_Contactin-5: First Ig domain of the ...
159-255 1.12e-03

First immunoglobulin (Ig) domain of contactin-5; Ig1_Contactin-5: First Ig domain of the neural cell adhesion molecule contactin-5. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains, anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. In rats, a lack of contactin-5 (NB-2) results in an impairment of the neuronal activity in the auditory system. Contactin-5 is expressed specifically in the postnatal nervous system, peaking at about 3 weeks postnatal. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala; lower levels of expression have been detected in the corpus callosum, caudate nucleus, and spinal cord.


Pssm-ID: 143256  Cd Length: 94  Bit Score: 37.61  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 159 GPSIVTPPKDIWNVTGA---KVFLSCEVIGIPTPVLIW--NKVKRDHSGVQRTELLPGdreNLAIQtrggpekhevtgwv 233
Cdd:cd05848    1 GPVFVQEPDDAIFPTDSdekKVILNCEARGNPVPTYRWlrNGTEIDTESDYRYSLIDG---NLIIS-------------- 63
                         90       100
                 ....*....|....*....|..
gi 226958445 234 lvSPLSKEDAGEYECHASNSQG 255
Cdd:cd05848   64 --NPSEVKDSGRYQCLATNSIG 83
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth ...
177-264 1.39e-03

Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells, which have undergone programmed cell death, and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 37.16  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 177 VFLSCEVIGIPTPVLIWNKvkrdhSGVQRTEllpgdrenlaiqtrggPEKHEVT--GWVLVSPLSKEDAGEYECHASNSQ 254
Cdd:cd05746    1 VQIPCSAQGDPEPTITWNK-----DGVQVTE----------------SGKFHISpeGYLAIRDVGVADQGRYECVARNTI 59
                         90
                 ....*....|
gi 226958445 255 GQASAAAKIT 264
Cdd:cd05746   60 GYASVSMVLS 69
Ig4_Neogenin cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth ...
177-265 2.29e-03

Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC, which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain.


Pssm-ID: 212460  Cd Length: 71  Bit Score: 36.48  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 177 VFLSCEVIGIPTPVLIWNKvkrdhsgvQRTELLPGDRENLAiqtrggpEKHEVTgwvlVSPLSKEDAGEYECHASNSQGQ 256
Cdd:cd05723    2 IVFECEVTGKPTPTVKWVK--------NGDMVIPSDYFKIV-------KEHNLQ----VLGLVKSDEGFYQCIAENDVGN 62

                 ....*....
gi 226958445 257 ASAAAKITV 265
Cdd:cd05723   63 VQAGAQLII 71
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar domains; Ig_Titin_like: immunoglobulin ...
183-265 3.72e-03

Immunoglobulin (Ig)-like domain of titin and similar domains; Ig_Titin_like: immunoglobulin (Ig)-like domain found in titin-like proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin, and similar to titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle, which also have repeated Ig-like and FN-III domains.


Pssm-ID: 319305  Cd Length: 74  Bit Score: 35.66  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 183 VIGIPTPVLIWNKVKRDhsgvqrteLLPGDRENLaiqtrggpEKHEVTGWVLVSPLSKEDAGEYECHASNSQGQASAAAK 262
Cdd:cd05748    8 ISGRPTPTVTWSKDGQP--------LKLSGRVQI--------ETTATSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATVN 71

                 ...
gi 226958445 263 ITV 265
Cdd:cd05748   72 VKV 74
Ig_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; Ig_Myotilin_C: C-terminal ...
179-265 3.83e-03

C-terminal immunoglobulin (Ig)-like domain of myotilin; Ig_Myotilin_C: C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle, and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin and actin. Mutations in myotilin lead to muscle disorders.


Pssm-ID: 143300  Cd Length: 75  Bit Score: 35.69  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 179 LSCEVIGIPTPVLIWnkvKRDHSGVQRTEllpgDRENLAiqtrggpekHEVTGWV--LVSPLSKEDAGEYECHASNSQGQ 256
Cdd:cd05892    3 LECQISAIPPPKIFW---KRNNEMVQYNT----DRISLY---------QDNSGRVtlLIKNVNKKDAGWYTVSAVNEAGV 66

                 ....*....
gi 226958445 257 ASAAAKITV 265
Cdd:cd05892   67 ATCHARLDV 75
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM: ...
177-265 8.99e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM: third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 143284  Cd Length: 71  Bit Score: 34.52  E-value: 8.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958445 177 VFLSCEVIGIPTPVLIWNKVKrdhsgvqrTELLPgdrenlaiqTRGGPEKHevTGWVLVSPLSKEDAGEYECHASNSQGQ 256
Cdd:cd05876    1 LVLECIAEGLPTPEVHWDRID--------GPLSP---------NRTKKLNN--NKTLQLDNVLESDDGEYVCTAENSEGS 61

                 ....*....
gi 226958445 257 ASAAAKITV 265
Cdd:cd05876   62 ARHHYTVTV 70
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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