ID H0VRT7_CAVPO Unreviewed; 1163 AA.
AC H0VRT7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Thrombospondin 1 {ECO:0000313|Ensembl:ENSCPOP00000013317.3};
GN Name=THBS1 {ECO:0000313|Ensembl:ENSCPOP00000013317.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000013317.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000013317.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000013317.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the thrombospondin family.
CC {ECO:0000256|ARBA:ARBA00009456}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AAKN02015860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0VRT7; -.
DR STRING; 10141.ENSCPOP00000013317; -.
DR Ensembl; ENSCPOT00000014924.3; ENSCPOP00000013317.3; ENSCPOG00000014779.4.
DR VEuPathDB; HostDB:ENSCPOG00000014779; -.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR GeneTree; ENSGT00940000155832; -.
DR HOGENOM; CLU_009257_0_0_1; -.
DR InParanoid; H0VRT7; -.
DR OMA; AVPDDKF; -.
DR TreeFam; TF324917; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000014779; Expressed in ovary and 10 other cell types or tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR GO; GO:0005577; C:fibrinogen complex; IEA:Ensembl.
DR GO; GO:0031091; C:platelet alpha granule; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070052; F:collagen V binding; IEA:Ensembl.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:Ensembl.
DR GO; GO:0070051; F:fibrinogen binding; IEA:Ensembl.
DR GO; GO:0017134; F:fibroblast growth factor binding; IEA:Ensembl.
DR GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0043236; F:laminin binding; IEA:Ensembl.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0001786; F:phosphatidylserine binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0002544; P:chronic inflammatory response; IEA:Ensembl.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:Ensembl.
DR GO; GO:0002581; P:negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0002605; P:negative regulation of dendritic cell antigen processing and presentation; IEA:Ensembl.
DR GO; GO:2001027; P:negative regulation of endothelial cell chemotaxis; IEA:Ensembl.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; IEA:Ensembl.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IEA:Ensembl.
DR GO; GO:0010748; P:negative regulation of long-chain fatty acid import across plasma membrane; IEA:Ensembl.
DR GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; IEA:Ensembl.
DR GO; GO:0010757; P:negative regulation of plasminogen activation; IEA:Ensembl.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IEA:Ensembl.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IEA:Ensembl.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0002040; P:sprouting angiogenesis; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 6.20.200.20; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR Gene3D; 4.10.1080.10; TSP type-3 repeat; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR PANTHER; PTHR10199:SF78; THROMBOSPONDIN-1; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF00090; TSP_1; 3.
DR Pfam; PF02412; TSP_3; 5.
DR Pfam; PF05735; TSP_C; 1.
DR Pfam; PF00093; VWC; 1.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00209; TSP1; 3.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 2.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50092; TSP1; 3.
DR PROSITE; PS51234; TSP3; 3.
DR PROSITE; PS51236; TSP_CTER; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00634}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1163
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012745564"
FT DOMAIN 317..374
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 647..691
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 771..806
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 868..903
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 904..939
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 943..1157
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 824..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1163 AA; 129024 MW; 24CB4648433EE4DA CRC64;
MGLAWGLSVL FLVHVCGTNR IPESGGDNSV FDIFELTGAT RKGSGRRLVK GPDPSSPAFR
IENANLIPPV PDDKFQDLVD AVRAEKGFLL LASLRQLKKT RGTLLAVERK DQSGQIFSVV
SNGKAGTLDL SLSAQGKQQV VSVEEALLAT GQWKSITLFV QEDRAQLYID CEKMENAELD
VPIQNIFTRD LANIARLRIA KGDVNGNFQG VLQNVRFVFG TTPEDILRNK GCSSSATNVL
LTLNNNVVNG SSPAIRTNYI GHKTKDLQAI CGISCEELSS MFLELRGLRT IVTTLQDSIR
KVTEENKELA NELRRPPLCY HNGVQYRNNE EWTVDSCTEC HCQNSVTICK KVSCPIMPCS
NATVPDGECC PRCWPSDSAD DGWSPWSEWT ACSVTCGNGI QQRGRSCDSL NNRCEGSSVQ
TRTCHIQECD KRFKQDGGWS HWSPWSSCSV TCGDGVITRI RLCNSPSPQM NGKPCEGEAR
ETKPCKRDAC PINGGWGPWS LWDICSVTCG GGVQKRSRLC NNPMPQFGGK DCIGDVTETQ
VCNTQECPID GCLSNPCFAG TKCTSYPDGS WKCGACPAGY SGNGIQCKDV DECREVPDAC
FNHNGEHRCK NTDPGYNCLP CPPRFTGTQP FGRGVEHATA NKQVCKPRNP CTDGTHNCNK
NAKCNYLGHY SDPMYRCECK PGYAGNGIIC GEDTDLDGWP NEDLLCVANA TYHCKKDNCP
NLPNSGQEDY DKGWNWDNCP FHYNPAQYDY DRDDVGDRCD NCPYNHNPDQ ADTDNNGEGD
ACAADIDGDG ILNERDNCQY VYNVDQRDTD MDGVGDQCDN CPLEHNPDQL DSDSDRIGDT
CDNNQDIDED GHQNNLDNCP YVPNANQADH DKDGKGDACD HDDDNDGIPD DRDNCRLVPN
PDQKDSDGDG RGDACKDDFD HDNVPDIDDI CPENVDISET DFRRFQMIPL DPKGTSQNDP
NWVVRHQGKE LVQTVNCDPG LAIGFDEFNA VDFSGTFFIN TERDDDYAGF VFGYQSSSRF
YVVMWKQVTQ SYWDTNPTRA QGYSGLSVKV VNSTTGPGEH LRNALWHTGN TPGQVRTLWH
DPRHIGWKDF TAYRWRLSHR PKTGFIRVVM YEGKKIMADS GPIYDKTYAG GRLGLFVFSQ
EMVFFSDLKY ECRGRSNIAL NMQ
//
