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Conserved domains on  [gi|27545211|ref|NP_775333|]
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thrombospondin-4-B precursor [Danio rerio]

Protein Classification

TSP_3 and TSP_C domain-containing protein (domain architecture ID 10430102)

protein containing domains LamG, EGF_CA, TSP_3, and TSP_C

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TSP_C pfam05735
Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and ...
734-931 4.75e-139

Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and related proteins.


:

Pssm-ID: 310385  Cd Length: 198  Bit Score: 417.02  E-value: 4.75e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545211   734 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFSGVDFEGTFHVNTVTDDDYAGFIFGYQDSSSFYVVMWKQTEQTYWQAT 813
Cdd:pfam05735   1 QIDPVWVITNQGAEIVQTLNSDPGLAIGNDSFGGVDFEGTFFVNTDSDDDYAGFVFGYQSNRKFYVVMWKQVNQTYWQST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545211   814 PFRAVAEPGIQLKAVKSKTGPGEHLRNSLWHTGDTNDQVRLLWKDPRNVGWKDKVSYRWYLQHRPQVGYIRVRFYEGTEL 893
Cdd:pfam05735  81 PFRAVAIKGIQLKLVDSTTGPGEYLRNALWHTGDTTNQVKLLWKDPNKIGWKDRTAYRWHLQHRPSIGLIRVRVYEGDTL 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 27545211   894 VADSGVTIDTTMRGGRLGVFCFSQENIIWSNLKYRCND 931
Cdd:pfam05735 161 IADSGNLYDTTLKGGRLGVFCFSQENVIWSNLKYRCND 198
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
38-194 9.23e-21

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


The actual alignment was detected with superfamily member smart00210:

Pssm-ID: 328935  Cd Length: 184  Bit Score: 92.81  E-value: 9.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545211     38 DLLHGGLAEqgvtELYILTTFRIQPGTGNTIFSLYNpRDNSKYFEFSVFGKANKAILRYLRRDGRMSAVTFNKLNLADGE 117
Cdd:smart00210  44 DLFPSGLPE----DFSLLTTFRQTPKSRGVLFAIYD-AQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLPLADGQ 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545211    118 KHRLLFHLKGLEvghpggfphsqgalpvpgVELHLDCRLVETlRDLPAVFNGLNNHQAVELKTMQ----GKAQEGLEELK 193
Cdd:smart00210 119 WHKLALSVSGSS------------------ATLYVDCNEIDS-RPLDRPGQPPIDTDGIEVRGAQaadrKPFQGDLQQLK 179

                   .
gi 27545211    194 L 194
Cdd:smart00210 180 I 180
TSPcc super family cl13107
Coiled coil region of thrombospondin; This domain family contains coiled coil region of ...
222-265 2.13e-20

Coiled coil region of thrombospondin; This domain family contains coiled coil region of subgroup B of thrombospondins, comprising TSP-3, TSP-4, and TSP-5, that assemble as pentamers. This region is located adjacent to the N-terminal domain (NTD) of thrombospondin (TSP), that mediates co-translational oligomerization via formation of a left-handed super-helix which binds hydrophilic signaling molecules such as vitamin D3 and vitamin A. Pentameric TSPs are stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end. TSP-5 is also known as cartilage oligomeric matrix protein (COMP). TSPs comprise a conserved family of extracellular, oligomeric, multidomain, calcium-binding glycoproteins. In mammals, they have several complex tissue-specific roles, including activities in wound healing and angiogenesis, connective tissue organization, vessel wall biology, and synaptogenesis, all mechanistically derived from interactions with cell surfaces, cytokines, growth factors, or components of the extracellular matrix (ECM) that together regulate many aspects of cell phenotype. In invertebrates, TSPs may have ancient functions such as bridging activities in cell-cell and cell-ECM interactions. Most protostomes and inferred basal metazoa encode a single TSP with the general domain organization of subgroup B TSPs and with a pentamerizing coiled coil.


The actual alignment was detected with superfamily member cd16080:

Pssm-ID: 300590  Cd Length: 44  Bit Score: 87.59  E-value: 2.13e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 27545211 222 NTKQLTTQMLELTKVINELKDVLIQQVKETSFLRNTISECQACG 265
Cdd:cd16080   1 VGRQLLGQMTQLNQVLGEVKDLLRQQVKETSFLRNTIAECQACG 44
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
485-520 7.21e-09

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


:

Pssm-ID: 308167  Cd Length: 36  Bit Score: 54.30  E-value: 7.21e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 27545211   485 EDADGDGKGDACDPDADGDGILNEQDNCWLTPNINQ 520
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPYNANIDQ 36
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
682-715 4.68e-06

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


:

Pssm-ID: 308167  Cd Length: 36  Bit Score: 46.21  E-value: 4.68e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 27545211   682 DDNNDGVGDICESDFDQDKVIDRIDNCPENAEIT 715
Cdd:pfam02412   2 DSDSDGVGDACDNDFDNDGVPDLLDNCPYNANID 35
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
312-346 3.05e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.78  E-value: 3.05e-05
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 27545211 312 DVDECQ-FNPCFPGVRCVNMAPGFRCEaCPLGFTGK 346
Cdd:cd00054   1 DIDECAsGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
604-640 1.13e-04

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


:

Pssm-ID: 308167  Cd Length: 36  Bit Score: 41.97  E-value: 1.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 27545211   604 DIDNDLVGDSCDtnQDSDGDGHQDSKDNCPMVINSSQ 640
Cdd:pfam02412   2 DSDSDGVGDACD--NDFDNDGVPDLLDNCPYNANIDQ 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
365-402 2.23e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 2.23e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 27545211 365 DIDECKgpDNGGCTANSICVNSVGSYQCgRCKTGFTGD 402
Cdd:cd00054   1 DIDECA--SGNPCQNGGTCVNTVGSYRC-SCPPGYTGR 35
 
Name Accession Description Interval E-value
TSP_C pfam05735
Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and ...
734-931 4.75e-139

Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and related proteins.


Pssm-ID: 310385  Cd Length: 198  Bit Score: 417.02  E-value: 4.75e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545211   734 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFSGVDFEGTFHVNTVTDDDYAGFIFGYQDSSSFYVVMWKQTEQTYWQAT 813
Cdd:pfam05735   1 QIDPVWVITNQGAEIVQTLNSDPGLAIGNDSFGGVDFEGTFFVNTDSDDDYAGFVFGYQSNRKFYVVMWKQVNQTYWQST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545211   814 PFRAVAEPGIQLKAVKSKTGPGEHLRNSLWHTGDTNDQVRLLWKDPRNVGWKDKVSYRWYLQHRPQVGYIRVRFYEGTEL 893
Cdd:pfam05735  81 PFRAVAIKGIQLKLVDSTTGPGEYLRNALWHTGDTTNQVKLLWKDPNKIGWKDRTAYRWHLQHRPSIGLIRVRVYEGDTL 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 27545211   894 VADSGVTIDTTMRGGRLGVFCFSQENIIWSNLKYRCND 931
Cdd:pfam05735 161 IADSGNLYDTTLKGGRLGVFCFSQENVIWSNLKYRCND 198
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
38-194 9.23e-21

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 92.81  E-value: 9.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545211     38 DLLHGGLAEqgvtELYILTTFRIQPGTGNTIFSLYNpRDNSKYFEFSVFGKANKAILRYLRRDGRMSAVTFNKLNLADGE 117
Cdd:smart00210  44 DLFPSGLPE----DFSLLTTFRQTPKSRGVLFAIYD-AQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLPLADGQ 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545211    118 KHRLLFHLKGLEvghpggfphsqgalpvpgVELHLDCRLVETlRDLPAVFNGLNNHQAVELKTMQ----GKAQEGLEELK 193
Cdd:smart00210 119 WHKLALSVSGSS------------------ATLYVDCNEIDS-RPLDRPGQPPIDTDGIEVRGAQaadrKPFQGDLQQLK 179

                   .
gi 27545211    194 L 194
Cdd:smart00210 180 I 180
TSP-4cc cd16080
Coiled coil region of thrombospondin-4 (TSP-4); This family contains the N-terminal coiled ...
222-265 2.13e-20

Coiled coil region of thrombospondin-4 (TSP-4); This family contains the N-terminal coiled coil region of TSP-4, which is abundantly expressed in tendon and muscle, as well as in neural and osteogenic tissues, and has also been detected in brain capillaries. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-4 regulates the composition of the deposition of extracellular matrix (ECM) in tendon and skeletal muscle. The absence of TSP-4 alters the organization, composition and physiological functions of these tissues. TSP-4 deficiency causes incorrect modification of heparan-sulfate (HS), resulting in decreased activity of lipoprotein lipase (LpL) and loss of beta-glycan; HS is involved in a wide variety of cellular functions, LpL is an endothelial enzyme responsible for the uptake and hydrolysis of lipoproteins, and beta-glycan has inhibiting effect on TGF-beta signaling in skeletal muscle. The human gene THBS4 that encodes for TSP-4 contains a single nucleotide polymorphism (SNP), which is expressed at high frequency in Caucasians and associated with a significantly increased risk of premature myocardial infarction. TSP-4 also binds stromal interaction molecule 1 (STIM1), a transmembrane protein that functions in the endoplasmic reticulum (ER), and regulates calcium channel activity. Studies show that TSP-4 may act as an organizer of adhesive and axon outgrowth-promoting molecules in the ECM to optimize retinal ganglion cell responses. TSP-4 is also involved in the post-translational modification of collagen and may assist in collagen fibril assembly.


Pssm-ID: 293926  Cd Length: 44  Bit Score: 87.59  E-value: 2.13e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 27545211 222 NTKQLTTQMLELTKVINELKDVLIQQVKETSFLRNTISECQACG 265
Cdd:cd16080   1 VGRQLLGQMTQLNQVLGEVKDLLRQQVKETSFLRNTIAECQACG 44
COMP pfam11598
Cartilage oligomeric matrix protein; This family of proteins represents the five-stranded ...
222-265 6.48e-16

Cartilage oligomeric matrix protein; This family of proteins represents the five-stranded coiled-coil domain of cartilage oligomeric matrix protein (COMP). This region has a binding site between two internal rings formed by Leu37 and Thr40


Pssm-ID: 288452  Cd Length: 45  Bit Score: 74.74  E-value: 6.48e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 27545211   222 NTKQLTTQMLELTKVINELKDVLIQQVKETSFLRNTISECQACG 265
Cdd:pfam11598   2 CAEQLARQLTELNQLLQELREEMRQQVKEISFLRNTIEECQACG 45
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
485-520 7.21e-09

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


Pssm-ID: 308167  Cd Length: 36  Bit Score: 54.30  E-value: 7.21e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 27545211   485 EDADGDGKGDACDPDADGDGILNEQDNCWLTPNINQ 520
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPYNANIDQ 36
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
682-715 4.68e-06

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


Pssm-ID: 308167  Cd Length: 36  Bit Score: 46.21  E-value: 4.68e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 27545211   682 DDNNDGVGDICESDFDQDKVIDRIDNCPENAEIT 715
Cdd:pfam02412   2 DSDSDGVGDACDNDFDNDGVPDLLDNCPYNANID 35
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
312-346 3.05e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.78  E-value: 3.05e-05
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 27545211 312 DVDECQ-FNPCFPGVRCVNMAPGFRCEaCPLGFTGK 346
Cdd:cd00054   1 DIDECAsGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
604-640 1.13e-04

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


Pssm-ID: 308167  Cd Length: 36  Bit Score: 41.97  E-value: 1.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 27545211   604 DIDNDLVGDSCDtnQDSDGDGHQDSKDNCPMVINSSQ 640
Cdd:pfam02412   2 DSDSDGVGDACD--NDFDNDGVPDLLDNCPYNANIDQ 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
312-344 1.67e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 41.46  E-value: 1.67e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 27545211    312 DVDECQ-FNPCFPGVRCVNMAPGFRCEaCPLGFT 344
Cdd:smart00179   1 DIDECAsGNPCQNGGTCVNTVGSYRCE-CPPGYT 33
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
365-402 2.23e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 2.23e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 27545211 365 DIDECKgpDNGGCTANSICVNSVGSYQCgRCKTGFTGD 402
Cdd:cd00054   1 DIDECA--SGNPCQNGGTCVNTVGSYRC-SCPPGYTGR 35
EGF_CA smart00179
Calcium-binding EGF-like domain;
365-400 5.72e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 39.92  E-value: 5.72e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 27545211    365 DIDECKgpDNGGCTANSICVNSVGSYQCgRCKTGFT 400
Cdd:smart00179   1 DIDECA--SGNPCQNGGTCVNTVGSYRC-ECPPGYT 33
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
373-402 1.95e-03

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 315598  Cd Length: 36  Bit Score: 38.27  E-value: 1.95e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 27545211   373 DNGGCTANSICVNSVGSYQCgRCKTGFTGD 402
Cdd:pfam12947   4 NNGGCHPNATCTNTDGSFTC-TCNDGYTGD 32
 
Name Accession Description Interval E-value
TSP_C pfam05735
Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and ...
734-931 4.75e-139

Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and related proteins.


Pssm-ID: 310385  Cd Length: 198  Bit Score: 417.02  E-value: 4.75e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545211   734 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFSGVDFEGTFHVNTVTDDDYAGFIFGYQDSSSFYVVMWKQTEQTYWQAT 813
Cdd:pfam05735   1 QIDPVWVITNQGAEIVQTLNSDPGLAIGNDSFGGVDFEGTFFVNTDSDDDYAGFVFGYQSNRKFYVVMWKQVNQTYWQST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545211   814 PFRAVAEPGIQLKAVKSKTGPGEHLRNSLWHTGDTNDQVRLLWKDPRNVGWKDKVSYRWYLQHRPQVGYIRVRFYEGTEL 893
Cdd:pfam05735  81 PFRAVAIKGIQLKLVDSTTGPGEYLRNALWHTGDTTNQVKLLWKDPNKIGWKDRTAYRWHLQHRPSIGLIRVRVYEGDTL 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 27545211   894 VADSGVTIDTTMRGGRLGVFCFSQENIIWSNLKYRCND 931
Cdd:pfam05735 161 IADSGNLYDTTLKGGRLGVFCFSQENVIWSNLKYRCND 198
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
38-194 9.23e-21

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 92.81  E-value: 9.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545211     38 DLLHGGLAEqgvtELYILTTFRIQPGTGNTIFSLYNpRDNSKYFEFSVFGKANKAILRYLRRDGRMSAVTFNKLNLADGE 117
Cdd:smart00210  44 DLFPSGLPE----DFSLLTTFRQTPKSRGVLFAIYD-AQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLPLADGQ 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27545211    118 KHRLLFHLKGLEvghpggfphsqgalpvpgVELHLDCRLVETlRDLPAVFNGLNNHQAVELKTMQ----GKAQEGLEELK 193
Cdd:smart00210 119 WHKLALSVSGSS------------------ATLYVDCNEIDS-RPLDRPGQPPIDTDGIEVRGAQaadrKPFQGDLQQLK 179

                   .
gi 27545211    194 L 194
Cdd:smart00210 180 I 180
TSP-4cc cd16080
Coiled coil region of thrombospondin-4 (TSP-4); This family contains the N-terminal coiled ...
222-265 2.13e-20

Coiled coil region of thrombospondin-4 (TSP-4); This family contains the N-terminal coiled coil region of TSP-4, which is abundantly expressed in tendon and muscle, as well as in neural and osteogenic tissues, and has also been detected in brain capillaries. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-4 regulates the composition of the deposition of extracellular matrix (ECM) in tendon and skeletal muscle. The absence of TSP-4 alters the organization, composition and physiological functions of these tissues. TSP-4 deficiency causes incorrect modification of heparan-sulfate (HS), resulting in decreased activity of lipoprotein lipase (LpL) and loss of beta-glycan; HS is involved in a wide variety of cellular functions, LpL is an endothelial enzyme responsible for the uptake and hydrolysis of lipoproteins, and beta-glycan has inhibiting effect on TGF-beta signaling in skeletal muscle. The human gene THBS4 that encodes for TSP-4 contains a single nucleotide polymorphism (SNP), which is expressed at high frequency in Caucasians and associated with a significantly increased risk of premature myocardial infarction. TSP-4 also binds stromal interaction molecule 1 (STIM1), a transmembrane protein that functions in the endoplasmic reticulum (ER), and regulates calcium channel activity. Studies show that TSP-4 may act as an organizer of adhesive and axon outgrowth-promoting molecules in the ECM to optimize retinal ganglion cell responses. TSP-4 is also involved in the post-translational modification of collagen and may assist in collagen fibril assembly.


Pssm-ID: 293926  Cd Length: 44  Bit Score: 87.59  E-value: 2.13e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 27545211 222 NTKQLTTQMLELTKVINELKDVLIQQVKETSFLRNTISECQACG 265
Cdd:cd16080   1 VGRQLLGQMTQLNQVLGEVKDLLRQQVKETSFLRNTIAECQACG 44
COMP pfam11598
Cartilage oligomeric matrix protein; This family of proteins represents the five-stranded ...
222-265 6.48e-16

Cartilage oligomeric matrix protein; This family of proteins represents the five-stranded coiled-coil domain of cartilage oligomeric matrix protein (COMP). This region has a binding site between two internal rings formed by Leu37 and Thr40


Pssm-ID: 288452  Cd Length: 45  Bit Score: 74.74  E-value: 6.48e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 27545211   222 NTKQLTTQMLELTKVINELKDVLIQQVKETSFLRNTISECQACG 265
Cdd:pfam11598   2 CAEQLARQLTELNQLLQELREEMRQQVKEISFLRNTIEECQACG 45
TSPcc cd16076
Coiled coil region of thrombospondin; This domain family contains coiled coil region of ...
225-264 3.90e-11

Coiled coil region of thrombospondin; This domain family contains coiled coil region of subgroup B of thrombospondins, comprising TSP-3, TSP-4, and TSP-5, that assemble as pentamers. This region is located adjacent to the N-terminal domain (NTD) of thrombospondin (TSP), that mediates co-translational oligomerization via formation of a left-handed super-helix which binds hydrophilic signaling molecules such as vitamin D3 and vitamin A. Pentameric TSPs are stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end. TSP-5 is also known as cartilage oligomeric matrix protein (COMP). TSPs comprise a conserved family of extracellular, oligomeric, multidomain, calcium-binding glycoproteins. In mammals, they have several complex tissue-specific roles, including activities in wound healing and angiogenesis, connective tissue organization, vessel wall biology, and synaptogenesis, all mechanistically derived from interactions with cell surfaces, cytokines, growth factors, or components of the extracellular matrix (ECM) that together regulate many aspects of cell phenotype. In invertebrates, TSPs may have ancient functions such as bridging activities in cell-cell and cell-ECM interactions. Most protostomes and inferred basal metazoa encode a single TSP with the general domain organization of subgroup B TSPs and with a pentamerizing coiled coil.


Pssm-ID: 293923  Cd Length: 40  Bit Score: 60.91  E-value: 3.90e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 27545211 225 QLTTQMLELTKVINELKDVLIQQVKETSFLRNTISECQAC 264
Cdd:cd16076   1 QLARQLTELNQMLQELREEMRQQVKETAFLRNTIMECQAC 40
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
485-520 7.21e-09

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


Pssm-ID: 308167  Cd Length: 36  Bit Score: 54.30  E-value: 7.21e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 27545211   485 EDADGDGKGDACDPDADGDGILNEQDNCWLTPNINQ 520
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPYNANIDQ 36
TSP-5cc cd16077
Coiled coil region of thrombospondin-5 (TSP-5); This family contains the N-terminal coiled ...
225-264 5.18e-08

Coiled coil region of thrombospondin-5 (TSP-5); This family contains the N-terminal coiled coil region of TSP-5, also known as cartilage oligomeric matrix protein (COMP). It forms a pentameric left-handed coiled coil (COMPcc) with a channel that is a unique carrier for lipophilic compounds. It is known to bind hydrophilic signaling molecules such as vitamin D3 and vitamin A, making it a possible targeted drug delivery system. TSP-5/COMP is expressed in all types of cartilage as well as in the vitreous of the eye, tendons, vascular smooth muscle cells, and heart. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-5 is essential for modulating the phenotypic transition of vascular smooth muscle cells and vascular remodeling. Mutations in TSP-5 result in two different inherited chondrodysplasias and osteoarthritic phenotypes: pseudoachondroplasia and multiple epithelial dysplasia. Deficiency of TSP-5 causes dilated cardiomyopathy (DCM), a common cause of congestive heart failure. Early increase in serum TSP-5 is associated with joint damage progression in patients with rheumatoid arthritis, thus representing a novel indicator of an activated destructive process in the joint.


Pssm-ID: 293924  Cd Length: 43  Bit Score: 52.14  E-value: 5.18e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 27545211 225 QLTTQMLELTKVINELKDVLIQQVKETSFLRNTISECQAC 264
Cdd:cd16077   4 QMLSEMQETNQALAEVKELLKQQVKEITFLKNTVMECDAC 43
TSP-3cc cd16079
Coiled coil region of thrombospondin-3 (TSP-3); This family contains the N-terminal coiled ...
222-264 7.98e-08

Coiled coil region of thrombospondin-3 (TSP-3); This family contains the N-terminal coiled coil region of TSP-3, which is highly expressed in osteosarcomas and associated with metastasis. TSP-3, along with TSP-5 and type IX collagen, is also expressed in the growth plate and all operate in concert and participate in growth plate organization that directly modulates linear growth. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-3 knockout mice have been shown to display accelerated endochondral ossification and increased trabecular bone in the femoral head.


Pssm-ID: 293925  Cd Length: 43  Bit Score: 51.50  E-value: 7.98e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 27545211 222 NTKQLTTQMLELTKVINELKDVLIQQVKETSFLRNTISECQAC 264
Cdd:cd16079   1 HTKALITQLTLFNQILGELREDIRDQVKEMSLIRNTIMECQVC 43
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
682-715 4.68e-06

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


Pssm-ID: 308167  Cd Length: 36  Bit Score: 46.21  E-value: 4.68e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 27545211   682 DDNNDGVGDICESDFDQDKVIDRIDNCPENAEIT 715
Cdd:pfam02412   2 DSDSDGVGDACDNDFDNDGVPDLLDNCPYNANID 35
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
312-346 3.05e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.78  E-value: 3.05e-05
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 27545211 312 DVDECQ-FNPCFPGVRCVNMAPGFRCEaCPLGFTGK 346
Cdd:cd00054   1 DIDECAsGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35
TSP_3 pfam02412
Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which ...
604-640 1.13e-04

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.


Pssm-ID: 308167  Cd Length: 36  Bit Score: 41.97  E-value: 1.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 27545211   604 DIDNDLVGDSCDtnQDSDGDGHQDSKDNCPMVINSSQ 640
Cdd:pfam02412   2 DSDSDGVGDACD--NDFDNDGVPDLLDNCPYNANIDQ 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
312-344 1.67e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 41.46  E-value: 1.67e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 27545211    312 DVDECQ-FNPCFPGVRCVNMAPGFRCEaCPLGFT 344
Cdd:smart00179   1 DIDECAsGNPCQNGGTCVNTVGSYRCE-CPPGYT 33
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
365-402 2.23e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 41.08  E-value: 2.23e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 27545211 365 DIDECKgpDNGGCTANSICVNSVGSYQCgRCKTGFTGD 402
Cdd:cd00054   1 DIDECA--SGNPCQNGGTCVNTVGSYRC-SCPPGYTGR 35
EGF_CA smart00179
Calcium-binding EGF-like domain;
365-400 5.72e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 39.92  E-value: 5.72e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 27545211    365 DIDECKgpDNGGCTANSICVNSVGSYQCgRCKTGFT 400
Cdd:smart00179   1 DIDECA--SGNPCQNGGTCVNTVGSYRC-ECPPGYT 33
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
373-402 1.95e-03

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 315598  Cd Length: 36  Bit Score: 38.27  E-value: 1.95e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 27545211   373 DNGGCTANSICVNSVGSYQCgRCKTGFTGD 402
Cdd:pfam12947   4 NNGGCHPNATCTNTDGSFTC-TCNDGYTGD 32
 
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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