ID H3DJ86_TETNG Unreviewed; 1174 AA.
AC H3DJ86;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Thrombospondin 1 {ECO:0000313|Ensembl:ENSTNIP00000020582.1};
GN Name=THBS1 {ECO:0000313|Ensembl:ENSTNIP00000020582.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000020582.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000020582.1}
RP IDENTIFICATION.
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 AlphaFoldDB; H3DJ86; -.
DR STRING; 99883.ENSTNIP00000020582; -.
DR Ensembl; ENSTNIT00000020814.1; ENSTNIP00000020582.1; ENSTNIG00000017441.1.
DR GeneTree; ENSGT00940000155832; -.
DR HOGENOM; CLU_009257_0_0_1; -.
DR InParanoid; H3DJ86; -.
DR OMA; LTNKGCK; -.
DR TreeFam; TF324917; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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:SF120; THROMBOSPONDIN-1; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF00090; TSP_1; 3.
DR Pfam; PF02412; TSP_3; 6.
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; 3.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50092; TSP1; 3.
DR PROSITE; PS51234; TSP3; 4.
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:UP000007303};
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..1174
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003583335"
FT DOMAIN 319..376
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 551..591
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 650..694
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 731..766
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 790..825
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 887..922
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 923..958
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 962..1174
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 726..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 129618 MW; C5E17AB31700E0E0 CRC64;
KMMLCGIFLL LMLWGCEGAR LAGSPDDNSV YDLFDLARVS KRQNGVTLVK GADPYSPAYK
VLNADLIPSV PDSSFRDILD SILAERGFLL IINLKQFRKS RGSILTIEKN DGSGSIFEIV
SNGRANTLEV LYSTANHQQV VTIEDTDLAT GHWKNITLFV QDDRVKLYVG CEEVNEAEMD
FPIHKVLTQE LADVATLRIA KGAVRDKFTG VLQNVRFVFG TSLDEILRNK GCQNGAVLTD
VMTLENPVNG SSPAVQTDHP GHKAKDVQPG QVCGLSCEDI AGIFKELRGL GVVVRKLSID
LRKVSEESML LKNETKQSGI CIHNGIVYQD KNEWTVDSCT ECTCQNSATV CRKISCPLVP
CANATVPDGE CCPRCGSSMV SAQGGWSPWS AWTQCSVTCG RGVQQRGRSC DRINSNCEGT
SVQTRDCYPQ ECDKRFKQDG AWSHWSPWSS CSVTCGEGVI TRIRLCNSPT PQMGGMDCQG
EGRQTEICRK SPCPIDGGWG PWSPWDTCTL TCGKGIQTRK RLCSDPAPRF GGKDCVGEAK
MSQVCNKQDC PIDGCLSNPC FPGAMCTSFP DGSFRCGKCP LGYTGDGLTC KDIDECKEVP
DACYVHNGVH LCENTEPGYN CLPCPARFSG PQPFGRGVEQ ATAKKQVCEP RNPCRDGSHD
CHKNANCIYL GVYSESMFRC ECKPGYAGNG HICGEDSDLD GWPNHNLVCV ENATYHCSKD
NCPSLPNSGQ EDHDKDGLGD ECDTDDDNDR IPDDRDNCPR LYNPAQYDAD RDDVGDLCDN
CVFEANTDQT DTDSNGEGDA CAVDIDGDGI LNEDDNCPYV YNVDQRDTDR DGVGDHCDNC
PLEHNPDQID SDSDRVGDKC DNNQDIDEDG HQNNLDNCPY IPNANQADHD KDGKGDACDH
DDDNDGIPDD KDNCRLAFNP DQTDSDGDGR GDICKDDFDQ DSVLDIYDVC PENFAISETD
FRRFQMVPLD PTGTSQIDPN WVVRHQGKEL VQTVNCDPGI AVGYDEFSAV DFSGTFFINT
DRDDDYAGFV FGYQSSSRFY TVMWKQITQT YWSTTPTRAQ GYSGLSIKVV NSTTGPGEHL
RNALWHTGDT AGQVRTLWHD PKKIGWKDFT AYRWHLTHRP KTGLIRVVMY EGKRIMADSG
NIYDKTYAGG RLGLYVFSQE MVYFSDLKYE CRGK
//
