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Database: UniProt
Entry: A0A3B3V852_9TELE
LinkDB: A0A3B3V852_9TELE
Original site: A0A3B3V852_9TELE 
ID   A0A3B3V852_9TELE        Unreviewed;       714 AA.
AC   A0A3B3V852;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Thrombospondin-4-B-like {ECO:0000313|Ensembl:ENSPLAP00000021106.1};
OS   Poecilia latipinna (sailfin molly).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000021106.1, ECO:0000313|Proteomes:UP000261500};
RN   [1] {ECO:0000313|Ensembl:ENSPLAP00000021106.1}
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   AlphaFoldDB; A0A3B3V852; -.
DR   STRING; 48699.ENSPLAP00000021106; -.
DR   Ensembl; ENSPLAT00000011823.1; ENSPLAP00000021106.1; ENSPLAG00000004623.1.
DR   GeneTree; ENSGT00940000155227; -.
DR   Proteomes; UP000261500; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 2.
DR   Gene3D; 1.20.5.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
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; 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   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   SUPFAM; SSF58006; Assembly domain of cartilage oligomeric matrix protein; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
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; 2.
DR   PROSITE; PS51234; TSP3; 4.
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   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}.
FT   DOMAIN          86..123
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          184..226
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          260..295
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          319..354
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          416..451
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          452..487
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   DOMAIN          491..705
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51236"
FT   REGION          346..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..437
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..460
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   714 AA;  78149 MW;  E0444BA8DCC6EF09 CRC64;
     ELKSMLSEMR ELLHKQIKET NFLRNTIAEC LACGPSPEQV VIPSHLTGCP PGTCFRQNMC
     ISSESGGFQC APCPDGYTGD GVHCDDVDEC SFNPCFPGVR CVNTAPGFRC EKCPVGYMGP
     EINGVGVSYA KSHKQVCEDL DECLGPPENG GCTPNSLCYN TIGSFRCGEC RAGFTGDQLT
     GCHGTRLCPN GQPNPCDVNG ECIVERDGSI SCVCGIGWAG NGYECGKDTD IDAYPDNNLV
     CRDNNCNQDN CVFVPNSGQE DADRDGSGDA CDDDADNDGI INIDDNCWLV PNVDQKNSDK
     DIHGDACDNC KTIQNPSQRD TDKDGLGDEC DDDMDGDGLK NVLDNCQRVP NPDQADRDND
     GVGDACDSCP DVANPNQSDS DDDLVGDTCD DNIDSDGDGH QNTKDNCPTV INSSQLDTDK
     DGMGDECDDD DDNDGIPDSE DNCRLVPNSD QKDSDMDKVG DACEGDFDKD NVIDIIDHCP
     ENAEVTLTDF RAYQTVVLDP EGDSQIDPNW VVLNQGMEIV QTMNSDPGLA VGYKAFSGVD
     FEGTFHVNTV TDDDYAGFIF GYQDSSSFYV VMWKQTEQTY WQAAPFRAVA EPGIQLKVVK
     SKTGPGEYMR NSLWHTGNTT DQVRLLWKDP RNVGWKDKVS YRWFLQHRPQ VGYIRARFYE
     GSKLVADTGV IIDTSMRGGR LGVFCFSQEN IIWSNLKYRC NDPERCRAAL SGRC
//
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