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Conserved domains on  [gi|47086187|ref|NP_998089|]
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insulin-like growth factor-binding protein 7 precursor [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
138-227 9.08e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 316449  Cd Length: 76  Bit Score: 57.12  E-value: 9.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187   138 PEIVTPPGEVWNITGSQVFLSCEAIGVPTPVLTWRkvsggsekpvplpgdKDNLAVQTRGGPEKHQVTGWVLISPLTKAE 217
Cdd:pfam13927   2 PVITVSPSSVVVLEGESVTLTCEATGGPPPTITWY---------------KNGKPGPTSSRISLSGSNSTLTISNVTRED 66
                          90
                  ....*....|
gi 47086187   218 DGSYECHASN 227
Cdd:pfam13927  67 SGTYTCVASN 76
IGFBP pfam00219
Insulin-like growth factor binding protein;
23-77 5.90e-10

Insulin-like growth factor binding protein;


:

Pssm-ID: 306685  Cd Length: 53  Bit Score: 54.24  E-value: 5.90e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 47086187    23 GSCDRTQCaPLPAQGCSSGTLRDSCGCCELCAAAEGEFCGGRGvsaRRCGSGLEC 77
Cdd:pfam00219   3 PPCDPERC-PPPPPGCPAGLVLDGCGCCPVCARQEGEPCGVYT---PPCDKGLRC 53
 
Name Accession Description Interval E-value
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
138-227 9.08e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 57.12  E-value: 9.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187   138 PEIVTPPGEVWNITGSQVFLSCEAIGVPTPVLTWRkvsggsekpvplpgdKDNLAVQTRGGPEKHQVTGWVLISPLTKAE 217
Cdd:pfam13927   2 PVITVSPSSVVVLEGESVTLTCEATGGPPPTITWY---------------KNGKPGPTSSRISLSGSNSTLTISNVTRED 66
                          90
                  ....*....|
gi 47086187   218 DGSYECHASN 227
Cdd:pfam13927  67 SGTYTCVASN 76
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: ...
155-240 3.16e-10

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: 55.51  E-value: 3.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 155 VFLSCEAIGVPTPVLTWRKVSGgsekpvPLPGDkdnlavqtRGGPEKHQVTgwVLISPLTKAEDGSYECHASNTQGEASA 234
Cdd:cd05731   1 LLLECIAEGLPTPDIRWIKLGG------ELPKG--------RTKFENFNKT--LKIENVSEADSGEYQCTASNTMGSARH 64

                ....*.
gi 47086187 235 VGSIHV 240
Cdd:cd05731  65 TISVTV 70
IGFBP pfam00219
Insulin-like growth factor binding protein;
23-77 5.90e-10

Insulin-like growth factor binding protein;


Pssm-ID: 306685  Cd Length: 53  Bit Score: 54.24  E-value: 5.90e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 47086187    23 GSCDRTQCaPLPAQGCSSGTLRDSCGCCELCAAAEGEFCGGRGvsaRRCGSGLEC 77
Cdd:pfam00219   3 PPCDPERC-PPPPPGCPAGLVLDGCGCCPVCARQEGEPCGVYT---PPCDKGLRC 53
IB smart00121
Insulin growth factor-binding protein homologues; High affinity binding partners of ...
22-80 8.44e-10

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


Pssm-ID: 197525  Cd Length: 75  Bit Score: 54.39  E-value: 8.44e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 47086187     22 CGSCDRTQCAPLPAqGCSSGTLRDSCGCCELCAAAEGEFCggrGVSARRCGSGLECVKP 80
Cdd:smart00121   3 CPPCDPARCPPCPP-GCAELVRLDGCGCCPVCARQEGEPC---GVYTPRCAPGLRCQPP 57
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
152-240 5.23e-07

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 47.11  E-value: 5.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187    152 GSQVFLSCEAIGVPTPVLTWRKvsggsekpvplpGDKDNLAVQTRGGPEKHQVTGWVLISPLTKAEDGSYECHASNTQGE 231
Cdd:smart00410   9 GESVTLSCEASGSPPPEVTWYK------------QGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGS 76

                   ....*....
gi 47086187    232 ASAVGSIHV 240
Cdd:smart00410  77 ASSGTTLTV 85
 
Name Accession Description Interval E-value
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
138-227 9.08e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 57.12  E-value: 9.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187   138 PEIVTPPGEVWNITGSQVFLSCEAIGVPTPVLTWRkvsggsekpvplpgdKDNLAVQTRGGPEKHQVTGWVLISPLTKAE 217
Cdd:pfam13927   2 PVITVSPSSVVVLEGESVTLTCEATGGPPPTITWY---------------KNGKPGPTSSRISLSGSNSTLTISNVTRED 66
                          90
                  ....*....|
gi 47086187   218 DGSYECHASN 227
Cdd:pfam13927  67 SGTYTCVASN 76
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: ...
155-240 3.16e-10

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: 55.51  E-value: 3.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 155 VFLSCEAIGVPTPVLTWRKVSGgsekpvPLPGDkdnlavqtRGGPEKHQVTgwVLISPLTKAEDGSYECHASNTQGEASA 234
Cdd:cd05731   1 LLLECIAEGLPTPDIRWIKLGG------ELPKG--------RTKFENFNKT--LKIENVSEADSGEYQCTASNTMGSARH 64

                ....*.
gi 47086187 235 VGSIHV 240
Cdd:cd05731  65 TISVTV 70
IGFBP pfam00219
Insulin-like growth factor binding protein;
23-77 5.90e-10

Insulin-like growth factor binding protein;


Pssm-ID: 306685  Cd Length: 53  Bit Score: 54.24  E-value: 5.90e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 47086187    23 GSCDRTQCaPLPAQGCSSGTLRDSCGCCELCAAAEGEFCGGRGvsaRRCGSGLEC 77
Cdd:pfam00219   3 PPCDPERC-PPPPPGCPAGLVLDGCGCCPVCARQEGEPCGVYT---PPCDKGLRC 53
IB smart00121
Insulin growth factor-binding protein homologues; High affinity binding partners of ...
22-80 8.44e-10

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


Pssm-ID: 197525  Cd Length: 75  Bit Score: 54.39  E-value: 8.44e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 47086187     22 CGSCDRTQCAPLPAqGCSSGTLRDSCGCCELCAAAEGEFCggrGVSARRCGSGLECVKP 80
Cdd:smart00121   3 CPPCDPARCPPCPP-GCAELVRLDGCGCCPVCARQEGEPC---GVYTPRCAPGLRCQPP 57
Ig3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third Ig domain of ...
140-240 3.88e-09

Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third 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 act ivity 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: 319277  Cd Length: 88  Bit Score: 52.93  E-value: 3.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 140 IVTPPGEVWNITGSQVFLSCEAIGVPTPVLTWRKVSGgseKPVPlpgdkdnLAVQTRGGPekhqvtgwVLISPLTKAED- 218
Cdd:cd04968   4 KVRFPADTYALKGQTVTLECFALGNPVPQIKWRKVDG---SPSS-------QWTTSTSEP--------VLEIPNVQFEDe 65
                        90       100
                ....*....|....*....|..
gi 47086187 219 GSYECHASNTQGEASAVGSIHV 240
Cdd:cd04968  66 GTYECEAENSRGKDTVQGRIIV 87
I-set pfam07679
Immunoglobulin I-set domain;
138-240 3.74e-08

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 50.33  E-value: 3.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187   138 PEIVTPPGEVWNITGSQVFLSCEAIGVPTPVLTWRKvsGGSekpvPLPGDkDNLAVQTRGGpeKHQVTgwvlISPLTKAE 217
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK--DGQ----PLRSS-DRFKVTYEGG--TYTLT----ISNVQPDD 67
                          90       100
                  ....*....|....*....|...
gi 47086187   218 DGSYECHASNTQGEASAVGSIHV 240
Cdd:pfam07679  68 SGKYTCVATNSAGEAEASAELTV 90
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
155-234 1.31e-07

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: 48.39  E-value: 1.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 155 VFLSCEAIGVPTPVLTWRKvsggsekpvplpgDKDNLAVQTRGGPEKHQVTGWVLISPLTKAEDGSYECHASNTQGEASA 234
Cdd:cd00096   1 VTLTCSASGNPPPTITWLK-------------NGKPLPSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASA 67
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
152-240 5.23e-07

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 47.11  E-value: 5.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187    152 GSQVFLSCEAIGVPTPVLTWRKvsggsekpvplpGDKDNLAVQTRGGPEKHQVTGWVLISPLTKAEDGSYECHASNTQGE 231
Cdd:smart00410   9 GESVTLSCEASGSPPPEVTWYK------------QGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGS 76

                   ....*....
gi 47086187    232 ASAVGSIHV 240
Cdd:smart00410  77 ASSGTTLTV 85
IG smart00409
Immunoglobulin;
152-240 5.23e-07

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 47.11  E-value: 5.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187    152 GSQVFLSCEAIGVPTPVLTWRKvsggsekpvplpGDKDNLAVQTRGGPEKHQVTGWVLISPLTKAEDGSYECHASNTQGE 231
Cdd:smart00409   9 GESVTLSCEASGSPPPEVTWYK------------QGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGS 76

                   ....*....
gi 47086187    232 ASAVGSIHV 240
Cdd:smart00409  77 ASSGTTLTV 85
Ig3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third Ig domain of the ...
138-240 1.24e-06

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: 45.78  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 138 PEIVTPPGEVWNITGSQVFLSCEAIGVPTPVLTWRKVSggseKPVPLPGDkdnlaVQTRGGPEKhqvtgwvlISPLTKAE 217
Cdd:cd05851   2 ADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRKIL----EPMPATAE-----ISMSGAVLK--------IFNIQPED 64
                        90       100
                ....*....|....*....|...
gi 47086187 218 DGSYECHASNTQGEASAVGSIHV 240
Cdd:cd05851  65 EGTYECEAENIKGKDKHQARVYV 87
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
152-230 2.39e-06

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar domains; Ig_Perlecan_like: the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar domains. Perlecan consists of five domains. Domain I has three putative heparan sulfate attachment sites; domain II has four LDL receptor-like repeats, and one Ig-like repeat; domain III resembles the short arm of laminin chains; domain IV has multiple Ig-like repeats (21 repeats in human perlecan); and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 44.79  E-value: 2.39e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47086187 152 GSQVFLSCEAIGVPTPVLTWRKVSGgsekPVPlpgDKDNLAVQTRGGpekhqvTGWVLISPLTKAEDGSYECHASNTQG 230
Cdd:cd05743   1 GETVEFTCVATGVPTPIINWRLNWG----HVP---DSARVSITSEGG------YGTLTIRDVKESDQGAYTCEAINTRG 66
Ig2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
152-240 1.69e-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: 42.51  E-value: 1.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 152 GSQVFLSCEAIGVPTPVLTWRKvsggsekpvplpgDKDNLAVQTRGGPEKHQvtgWVL-ISPLTKAEDGSYECHASNTQG 230
Cdd:cd05856   9 GSSVRLKCVASGNPRPDITWLK-------------DNKPLTPTEIGESRKKK---WTLsLKNLKPEDSGKYTCHVSNRAG 72
                        90
                ....*....|
gi 47086187 231 EASAVGSIHV 240
Cdd:cd05856  73 EINATYKVDV 82
Ig2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain ...
144-231 2.08e-05

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: 42.38  E-value: 2.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 144 PGEVWNITGSQVFLSCEA-IGVPTPVLTWRKvsggSEKPVplpgDKDNLAVQTRGGpekhqvtGWVLISPLTKAEDGSYE 222
Cdd:cd05724   3 PSDTQVAVGEMAVLECSPpRGHPEPTVSWRK----DGQPL----NLDNERVRIVDD-------GNLLIAEARKSDEGTYK 67

                ....*....
gi 47086187 223 CHASNTQGE 231
Cdd:cd05724  68 CVATNMVGE 76
Ig3_NCAM-1_like cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); ...
151-240 3.50e-05

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig3_NCAM-1_like: domain similar to the third 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.


Pssm-ID: 143207  Cd Length: 95  Bit Score: 41.84  E-value: 3.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 151 TGSQVFLSCEAIGVPTPVLTWRkvsggsekpvplpgdKDNLAVQTrgGPEKHQVT---GWVLISPLTKAEDGSYECHASN 227
Cdd:cd05730  17 LGQSVTLACDADGFPEPTMTWT---------------KDGEPIES--GEEKYSFNedgSEMTILDVDKLDEAEYTCIAEN 79
                        90
                ....*....|...
gi 47086187 228 TQGEASAVGSIHV 240
Cdd:cd05730  80 KAGEQEAEIHLKV 92
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM: ...
155-240 3.74e-05

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: 41.45  E-value: 3.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 155 VFLSCEAIGVPTPVLTWRKVSGgsekpvPLPGDkdnlavqtRGGPEKHQvtGWVLISPLTKAEDGSYECHASNTQGEASA 234
Cdd:cd05876   1 LVLECIAEGLPTPEVHWDRIDG------PLSPN--------RTKKLNNN--KTLQLDNVLESDDGEYVCTAENSEGSARH 64

                ....*.
gi 47086187 235 VGSIHV 240
Cdd:cd05876  65 HYTVTV 70
IGc2 smart00408
Immunoglobulin C-2 Type;
152-230 8.77e-05

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 40.08  E-value: 8.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187    152 GSQVFLSCEAIGVPTPVLTWRkvsggsekpvplpgdKDNLAVQTRGgpeKHQVTGWVL-ISPLTKAEDGSYECHASNTQG 230
Cdd:smart00408   2 GQSVTLTCPAEGNPVPNITWL---------------KDGKPLPESN---RFVASGSTLtIKSVSLEDSGLYTCVAENSAG 63
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
152-241 1.56e-04

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: 39.75  E-value: 1.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 152 GSQVFLSCEAIGVPTPVLTWRkVSGgseKPV-PLPGDKDNLavqtrggpekhqVTGWVLI-SPLTKAEDGSYECHASNTQ 229
Cdd:cd04978   1 GETGELICEAEGNPQPTITWR-LNG---VPIePAPEDMRRT------------VDGRTLIfSNLQPNDTAVYQCNASNVH 64
                        90
                ....*....|..
gi 47086187 230 GEASAVGSIHVV 241
Cdd:cd04978  65 GYLLANAFLHVL 76
Ig1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; Ig1_Contactin: First Ig domain of contactins. ...
137-230 1.89e-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: 39.51  E-value: 1.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 137 GPEIVTPPGEVWNITGS---QVFLSCEAIGVPTPVLTWRKvsGGSEKPVpLPGDKDNLavqtrggpekhqVTGWVLISPL 213
Cdd:cd04967   1 GPVFEEQPDDTIFPEESdeeKVALNCRARANPPPTYRWKM--NGTEIKL-EPDSRYSL------------VGGNLVISNP 65
                        90
                ....*....|....*...
gi 47086187 214 TKAED-GSYECHASNTQG 230
Cdd:cd04967  66 SKAKDaGHYQCLATNTVG 83
Ig2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor and similar ...
152-234 1.93e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor and similar proteins; Ig2_FGFR_like: domain similar to the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, -2, -3, -4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor_like-1(FGFRL1). 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: 319297  Cd Length: 85  Bit Score: 39.51  E-value: 1.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 152 GSQVFLSCEAIGVPTPVLTWRKvsggsekpvplpgDKDNLAVQTRGGPEKHQVTGWVLISPLTKAED-GSYECHASNTQG 230
Cdd:cd05729   9 NTKVRLECGARGNPTPNITWLK-------------DGKQKWKINVIRPTRVEEKGWVLIIRRAIPRDtGKYTCIVSNQYG 75

                ....
gi 47086187 231 EASA 234
Cdd:cd05729  76 TINH 79
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third ...
152-240 2.10e-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: 39.15  E-value: 2.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 152 GSQVFLSCEAIGVPTPVLTWRKvsGGSekpvPLPGDKdnlavqtrggpeKHQV--TGWVLISPLTKAEDGSYECHASNTQ 229
Cdd:cd05745   2 GQTVDFLCEAQGYPQPVIAWTK--GGS----QLSVDR------------RHLVlsSGTLRISRVALHDQGQYECQAVNIV 63
                        90
                ....*....|.
gi 47086187 230 GEASAVGSIHV 240
Cdd:cd05745  64 GSQRTVAQLTV 74
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig4_L1-CAM_like: ...
152-241 1.25e-03

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig4_L1-CAM_like: fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 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.


Pssm-ID: 143275  Cd Length: 76  Bit Score: 37.17  E-value: 1.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 152 GSQVFLSCEAIGVPTPVLTWRkVSGgsekpVPLPG-DKDnlavqtrggPEKHQVTGWVLISPLTKAEDGSYECHASNTQG 230
Cdd:cd05867   1 GETARLDCQVEGIPTPNITWS-ING-----APIEGtDPD---------PRRHVSSGALILTDVQPSDTAVYQCEARNRHG 65
                        90
                ....*....|.
gi 47086187 231 EASAVGSIHVV 241
Cdd:cd05867  66 NLLANAHVHVV 76
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth ...
155-233 1.51e-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: 36.78  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 155 VFLSCEAIGVPTPVLTWrkvsggsekpvplpgDKDNLAVQTRGgpeKHQVT--GWVLISPLTKAEDGSYECHASNTQGEA 232
Cdd:cd05746   1 VQIPCSAQGDPEPTITW---------------NKDGVQVTESG---KFHISpeGYLAIRDVGVADQGRYECVARNTIGYA 62

                .
gi 47086187 233 S 233
Cdd:cd05746  63 S 63
Ig_hNeurofascin_like cd05875
Immunoglobulin (Ig)-like domain of human neurofascin (NF); Ig_hNeurofascin_like: domain ...
155-232 4.10e-03

Immunoglobulin (Ig)-like domain of human neurofascin (NF); Ig_hNeurofascin_like: domain similar to the first immunoglobulin (Ig)-like domain of human neurofascin (NF). NF 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 a cytoplasmic domain. NF has many alternatively spliced isoforms having different temporal expression patterns during development. NF participates in axon subcellular targeting and synapse formation, however little is known of the functions of the different isoforms.


Pssm-ID: 143283  Cd Length: 77  Bit Score: 35.34  E-value: 4.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 155 VFLSCEAIGVPTPVLTWRKVSG----GSEKPVPLPGDKDNLAVQTRGGPEKHQVtgwvlispltkaeDGSYECHASNTQG 230
Cdd:cd05875   1 IIIECEAKGNPVPTFQWTRNGKffnvAKDPRVSMRRRSGTLVIDFSGGGRPEDY-------------EGEYQCFARNNLG 67

                ..
gi 47086187 231 EA 232
Cdd:cd05875  68 TA 69
Ig1_Robo cd07693
First immunoglobulin (Ig)-like domain in Robo (roundabout) receptors and similar proteins; ...
138-241 4.82e-03

First immunoglobulin (Ig)-like domain in Robo (roundabout) receptors and similar proteins; Ig1_Robo: domain similar to the first 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: 143317  Cd Length: 100  Bit Score: 35.60  E-value: 4.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 138 PEIVTPPGEVWNITGSQVFLSCEAIGVPTPVLTWRKvsGGSekpvPLPGDKDNLAVQTRGGPEKHQVTGWVLISPLTKAE 217
Cdd:cd07693   2 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLK--NGQ----PLETDKDDPRSHRIVLPSGSLFFLRVVHGRKGRSD 75
                        90       100
                ....*....|....*....|....*
gi 47086187 218 DGSYECHASNTQGEA-SAVGSIHVV 241
Cdd:cd07693  76 EGVYVCVAHNSLGEAvSRNASLEVA 100
Ig_NCAM-1_like cd05732
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar ...
152-230 8.69e-03

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: 34.81  E-value: 8.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086187 152 GSQVFLSCEAIGVPTPVLTWRKVSGG-SEKPVPLPGDkdnlaVQTRGGPEKHQVTgwvlISPLTKAEDGSYECHASNTQG 230
Cdd:cd05732  16 LEQITLTCEAEGDPIPEITWRRATRNfSEGDKSLDGR-----IVVRGHARVSSLT----LKDVQLTDAGRYDCEASNRIG 86
 
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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