ID A0A2Y9ILB8_ENHLU Unreviewed; 956 AA.
AC A0A2Y9ILB8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=LOW QUALITY PROTEIN: thrombospondin-3 {ECO:0000313|RefSeq:XP_022346820.1};
GN Name=LOC111139020 {ECO:0000313|RefSeq:XP_022346820.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022346820.1};
RN [1] {ECO:0000313|RefSeq:XP_022346820.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022346820.1};
RG RefSeq;
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 RefSeq; XP_022346820.1; XM_022491112.1.
DR AlphaFoldDB; A0A2Y9ILB8; -.
DR STRING; 391180.A0A2Y9ILB8; -.
DR KEGG; elk:111139020; -.
DR OrthoDB; 5345349at2759; -.
DR Proteomes; UP000248482; Unplaced.
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:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd16079; TSP-3cc; 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; 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; IPR028507; TSP3_coiled-coil.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR048287; TSPN-like_N.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR PANTHER; PTHR10199:SF89; THROMBOSPONDIN-3; 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; 2.
DR SMART; SM00210; TSPN; 1.
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; 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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..956
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016078926"
FT DOMAIN 316..354
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 492..527
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 551..586
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 610..647
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 688..723
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 727..941
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 518..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..667
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 103842 MW; B27F169DAB691DB5 CRC64;
METQKLRGAL ALLLLCTLAS ASQDLQVIDL LTVGESRQMT AVAEKIRAAL LTAADIYLLS
TFRLPPKQGG VLFGLYSRQD NTRWLEASVV GKINKVLVRY QREDGRVHAV HLQQAGLADG
RTHTALLRLR GPARPSPALQ LYVDCKLGDQ HSGLPALAPI PPAEVDGLEV RTGQKAYLRM
QGFVESMKMI LGGSMARVGA LSECPFQGDE SIHSAVTSAL HSILGEQTKA LVTQLTLFNQ
ILVELRDDIR DQVKEMSLIR NAIMECQVCG FHEQRSHCSP NPCFRGVDCM EVYEDPGYRC
GPCPPGLQGN GTHCADIDEC AHADPCFPGA SCINTVPGFH CEACPRGYKG TRVSGVGIDY
ARASKQVCND VDECNDGNNG GCDPNSICTN TVGSFKCGPC RLGFLGNQSQ GCLPARTCHS
PAHSPCHVHA HCLFERNGAV SCACNVGWAG NGNVCGTDTD IDGYPDQALP CMDNNKHCKQ
DNCLLTPNSG QEDADNDGVG DQCDDDADGD GIKNVEDNCR LFPNKDQQNS DTDSFGDACD
NCPNVPNNDQ KDTDSNGEGD ACDNDVDGDG IPNGLDNCPK VPNPLQTDRD EDGVGDACDS
CPEMSNPTQT DADSDLVGDV CDTNEDSDGD GHQDTKDNCP ELPNSSQLDS DNDGLGDECD
GDDDNDGIPD YVPPGPDNCR LVPNPNQKDS DGNGVGDVCE DDFDNDAVAD PLDVCPESAE
VTLTDFRAYQ TVVLDPEGDA QIDPNWVVLN QGMEIVQTMN SDPGLAVGYT AFNGVDFEGT
FHVNTVTDDD YAGFLFSYQD SGRFYVVMWK QTEQTYWQAT PFRAVAQPGL QLKAVTSVSG
PGEHLRNALW HTGHTPDQVR LLWTDPRNVG WRDKTSYRWQ LLHRPQVGYI RVKLYEGPQL
VADSGVVIDT AMRGGRLGVF CFSQENIIWS NLQYRCNDTV PEDFEPFRRQ LLQGRV
//
