ID A0A3B4DEK1_PYGNA Unreviewed; 977 AA.
AC A0A3B4DEK1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Thrombospondin 4 {ECO:0000313|Ensembl:ENSPNAP00000021888.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000021888.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000021888.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_017546571.1; XM_017691082.1.
DR AlphaFoldDB; A0A3B4DEK1; -.
DR STRING; 42514.ENSPNAP00000021888; -.
DR Ensembl; ENSPNAT00000033627.1; ENSPNAP00000021888.1; ENSPNAG00000004896.1.
DR GeneID; 108423646; -.
DR CTD; 563429; -.
DR GeneTree; ENSGT00940000155227; -.
DR OMA; SHCYNTV; -.
DR OrthoDB; 5345349at2759; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd16076; TSPcc; 1.
DR Gene3D; 1.20.5.10; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.10.25.10; Laminin; 4.
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; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR024665; TSP/COMP_coiled-coil.
DR InterPro; IPR046970; TSP/COMP_coiled-coil_sf.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR048287; TSPN-like_N.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR PANTHER; PTHR10199:SF116; THROMBOSPONDIN-4 PRECURSOR; 1.
DR Pfam; PF11598; COMP; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02412; TSP_3; 6.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF58006; Assembly domain of cartilage oligomeric matrix protein; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51234; TSP3; 3.
DR PROSITE; PS51236; TSP_CTER; 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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..977
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017284612"
FT DOMAIN 300..337
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 443..485
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 519..554
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 578..613
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 675..710
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 750..964
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 398..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 217..244
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 405..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 977 AA; 106220 MW; 24042E326F08844B CRC64;
MVAWARILFC LFALSSTVNA QGIVYDFLVS PDCLPDLLQG GLKTKNVNDV FILTTFQLHN
KAPTRVFRIY NPANNSDYFD FTMHGKLNKV SLRYLKSNGK MGTANFIKVP LADGRPHNVM
LHFSGLTHGT PSMALYVDCR LVEIVEDLPV AFKTLPSGPN RVALKTMPTT AQDSLSDLKL
VLDESIENVA ELQDCTLQQG ESLQLLGLTS KLEAGPMFEL VRMMQELKEK MDQQIRETAN
MRKIIMECVP CDGPKGKTDM PAKCAPGVCF QQSMCVATEQ GFECTPCPEG YTGDGVHCDD
VNECQFNPCS SGVRCINTAP GFRCESCPRG YTGDVVQGVG ITYAQAHKQV CTDIDECQSS
DNRGCTPYSY CINTVGSFHC GECKPGFTGD QVSGCRPSGL GSDPGTGPGS GSDTGPGSGS
GTGPGSGSGT GQGSGSTASA ALSSRQCGNA QTNPCDINAE CIVERDGSIS CVCNIGWAGN
GYVCGKDTDI DAYPDRKLQC QDATCKKDNC MSVPNSGQED ADRDGKGDAC DEDADNDGIL
NEKDNCWLNR NVDQKNSDDD LHGDSCDNCV NVNNPDQRDT DQDGLGDACD DDMDGDGLKN
ILDNCQTVPN PDQLDRDNDG VGDACDSCPE VPNPTQSDVD DDLVGDTCDT NIDSDGDGHQ
NTKDNCPTII NSSQLDTDKD GHGDECDDDD DNDGIPDDKD NCRLVPNKDQ ADENNDGVGD
ACAGDFDRDQ VIDRIDTCPE NAQVTLTDFR AYQTVVLDPE GEAQIDPNWV VLNQGMEIVQ
TMNSDPGLAV GYTAFNGVDF EGTFHVNTVT DDDYAGFIFG YQDSSSFYVV MWKQTEQTYW
QAVPFRAVAE PGIQLKAVKS KTGPGEFLRN SLWHTGDTKD QVRLLWKDPR NVGWKDKVSY
RWNLQHRPQV GYIKVRFYEG TSLVADSGVV IDTSMRGGRL GVFCFSQENI IWSNLKYRCN
DTIPADYEEY SAQHISS
//
