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Database: UniProt
Entry: A0A3Q2D7T7_CYPVA
LinkDB: A0A3Q2D7T7_CYPVA
Original site: A0A3Q2D7T7_CYPVA 
ID   A0A3Q2D7T7_CYPVA        Unreviewed;      1176 AA.
AC   A0A3Q2D7T7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Thrombospondin-1-like {ECO:0000313|Ensembl:ENSCVAP00000014618.1};
GN   Name=THBS1 {ECO:0000313|Ensembl:ENSCVAP00000014618.1};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000014618.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000014618.1}
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; A0A3Q2D7T7; -.
DR   STRING; 28743.ENSCVAP00000014618; -.
DR   Ensembl; ENSCVAT00000031191.1; ENSCVAP00000014618.1; ENSCVAG00000017402.1.
DR   GeneTree; ENSGT00940000155832; -.
DR   Proteomes; UP000265020; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF78; THROMBOSPONDIN-1; 1.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF00090; TSP_1; 3.
DR   Pfam; PF02412; TSP_3; 7.
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   Coiled coil {ECO:0000256|SAM:Coils};
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          321..378
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          553..593
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          652..696
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          733..768
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          792..827
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          889..924
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          925..960
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   DOMAIN          964..1176
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51236"
FT   REGION          730..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          288..315
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        739..754
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..874
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        889..903
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1176 AA;  130963 MW;  0A87AB5B3464E881 CRC64;
     MLWTCEGARV AGELKIFIYQ IISFFFFFFS NISNILELTY YSPAESREDN SVFDLFELIR
     VPSKNHGVSL VKGDDPYSPA YRILNPDLIP PVPESAFRDL VDSVQAERGF LLLLNFKQFK
     RTRGSLLTVE KRDGSGVVFE IISNGKANTL DIVYSTEKKQ QVVSIEEVDL ATGHWKNITL
     FVQEDRAQLF AGCEEVNTAE MDAPIQNILT QGTPAGARLR VGKGAVKDKF MGVLQNVRFV
     FGTTLDAILR NKGCQKGNVI YTRVDLNIYL QMVCGFSCED LISMFKELKG LGVVVKELST
     ELRQLTNENK LIRTHMGIHS GICFHNGIKH NNKDEWTVDD CTECTCQNSA TVCRKISCPL
     IPCANATVPD GECCPRCGTP SDYAEDGWSP WSEWTHCSVS CGRGIQQRGR SCDRINNVCE
     GTSVQTRDCY LQECDKRFKQ DGNWSHWSPW SSCSVTCGAG VITRIRLCNS PTPQLGGRDC
     VGEGRQTEKC KMSPCPINGN WGPWSPWGTC TLTCGGGVQT RKRLCNDPAP KHGGKECVGD
     AIDKQMCNKK ACPIDGCLSN PCFSGAKCSS FPDGSWKCGK CPIGYTGNGI RCKDVDECKE
     VPDACFEFNG VHRCENTEPG YNCLPCPPRY SGPQPFGKGV EQAAANKQVC TPQNPCLDGS
     HDCNKNARCN YLGHFSDPMF RCECKPGYAG NGHICGEDTD LDGWPNADLV CVENATYHCK
     KDNCPNLPNS GQEDYDKDGI GDACDDDDDN DGIPDDRDNC PFVYNPRQYD YDRDDVGDRC
     DNCPYNSNPD QTDTDNNGEG DACAVDIDGD GILNEKDNCP YIYNVDQRDT DLDGVGDMCD
     NCPLENNPDQ VDSDDDRVGD KCDSNQDIDE DGHQNNLDNC PYIPNANQAD HDKDGKGDAC
     DHDDDNDGIP DDKDNCRLAF NPDQLDSDGD GRGDACKDDF DQDNVPDIYD VCPENFDISE
     TDFRKFQMVP LDPKGTSQID PNWVVRHQGK ELVQTVNCDP GIAVGYHEFN SVDFSGTFFI
     NTERDDDYAG FVFGYQSSSR FYVVMWKQIT QTYWSSKPTK AQGYSGLSIK VVNSTTGPGE
     HLRNALWHTG NTAGQVRTLW HDPKNVGWKD FTAYRWHLIH RPRTGLIRVV MYEGKKIMAD
     SGSIYDKTYA GGRLGLFVFS QEMVYFSDLK YECRGR
//
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