ID A0A3Q3FIW9_9LABR Unreviewed; 960 AA.
AC A0A3Q3FIW9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Thrombospondin-4-B-like {ECO:0000313|Ensembl:ENSLBEP00000019454.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000019454.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000019454.1}
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; A0A3Q3FIW9; -.
DR Ensembl; ENSLBET00000020508.1; ENSLBEP00000019454.1; ENSLBEG00000014918.1.
DR GeneTree; ENSGT00940000155227; -.
DR Proteomes; UP000261660; 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; -; 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; 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; 5.
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; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..960
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018687501"
FT DOMAIN 329..366
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 503..538
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 562..597
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 659..694
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 695..730
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 734..948
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 593..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..680
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 105206 MW; AB1B01E3327B15EA CRC64;
MDVWARAVAL SLLLQQLVLT VTAQGIVYDL LVSPDCLPDL LQGSLKNKGR DEAFLLSSFR
LQNKAPTSLF SVINPQDNTK YLELSVQAKL SKVILRYQKT DGRFGTTSFN HPSLADGQDH
HVMLHASGLQ HGTPRLHIYI DCRLTHTLDD LPAVFGSIPP GSNKVALWTL QTSGQDELTD
LKLVIEDTID NVATLQDCSM EHTQSRTSAR EALQLLGIQG GQVLQDQTTM QELKSMLAEM
KQLLNQQIKE TNFLRNTITE CLPCGLRGNP TNTGPAPTPG QFVMQPQPLT QCPLGTCFKQ
NMCIPTDSGG FQCAPCPDGY TGDGVHCDDV DECQFGPCFP GVKCVNTAPG FRCGQCPLGY
TGPEINGVGV AYAKTNKQVC EDIDECLGPP DNGGCTANSH CHNTMGSFRC GDCRTGFTGD
QVSGCRGTRL CPNGLPNPCD ANAECVVERD GSISCMCGVG WAGNGYVCGK DTDIDAYPDS
KLACRDNNCK EDNCVFVPNS GQEDADRDGM GDACDDDADS DGIINIDDNC WLVPNVDQKN
SDKDLHGDAC DNCITLDNPY QRDTDKDGLG DECDDDMDGD GLKNILDNCQ RVPNVDQKDR
DKDGVGDACD SCPDMINPNQ SDSDDDLVGD TCDDNIDSDG DGHQNTKDNC PTVINSSQLD
TDKDGMGDDC DDDDDNDGIL DEVDNCRLVP NPDQRDSDNN NVGDACEGDF DKDDVIDIID
HCPENAEVTL TDFRAYQTVV LDPEGDSQID PNWVVLNQGM EIVQTMNSDP GLAVGYTAFS
GVDFEGTFHV NTVTDDDYAG FIFGYQDSSS FYVVMWKQTE QTYWQAAPFR AVADPGIQLK
AVKSKTGPGE YLRNSLWHTG DTQDQVRLLW RDPRNVGWKD KVSYRWFLQH RPQVGYIRAR
FFEGSDLVAD TGAIIDTSMR GGRLGVFCFS QENIIWSNLK YRCNDTIPFD YEDLSAQNTE
//
