ID A0A1L8F5B7_XENLA Unreviewed; 956 AA.
AC A0A1L8F5B7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Thrombospondin-3 isoform X1 {ECO:0000313|RefSeq:XP_018089130.1};
GN Name=thbs3.S {ECO:0000313|RefSeq:XP_018089130.1,
GN ECO:0000313|Xenbase:XB-GENE-17330634};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018089130.1};
RN [1] {ECO:0000313|RefSeq:XP_018089130.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018089130.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018089130.1};
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_018089130.1; XM_018233641.2.
DR AlphaFoldDB; A0A1L8F5B7; -.
DR STRING; 8355.A0A1L8F5B7; -.
DR PaxDb; 8355-A0A1L8F5B7; -.
DR GeneID; 108700446; -.
DR KEGG; xla:108700446; -.
DR AGR; Xenbase:XB-GENE-17330634; -.
DR CTD; 108700446; -.
DR Xenbase; XB-GENE-17330634; thbs3.S.
DR OMA; XVKLYEG; -.
DR OrthoDB; 5345349at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 108700446; Expressed in internal ear and 10 other cell types or tissues.
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; 6.
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; 2.
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; 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 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:UP000186698};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..956
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035204162"
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 688..723
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REGION 514..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 105633 MW; 9E7D4C56DBBCFA57 CRC64;
MGGHLLLLLL CCFFCWTQAS RQHSKHIIDL LTVSESRHMS GVVEKIRSEL LVVNDLYFLS
TFRLPPKAGG VLFGLYSKKD NTKWLEASIV GKINRVLVRY MREDSKLHAV SLQNANLSDG
NIHTMILRVS GFWGDTLSLE LYVDCKQVDT SLGLPEMMII PQFEVESGDI RSGHKAFLRM
QGSVESMKLI LGGSLSRVGA LSECPFHEDE SIHNTVNGVV NSILGEHTKA LITQMTLFNK
VLAELRKDIR DQVKEMSLIR NTIMECQVCG FHEHRSRCNP NPCFPGVDCM EAYEYPGYRC
GPCPPGSQGN GTYCADIDEC SHVNPCFSGS KCINTSPGFR CEHCPRGYKG NMVSGVGVDY
AKASKQVCKD IDECNDGNNG GCDVNSICTN TVGSFRCGPC KPGFVGNQTV RCIPKRSCAS
PAFNPCHVNG HCVFERNGDI TCACNIGWAG NGYTCGRDTD LDGYPDEPMP CIDNNKHCRQ
DNCRLTPNSG QEDADNDGIG DQCDEDADGD GIKNVEDNCR LVPNKDQQNS DTDSFGDACD
NCPNVPNNDQ KDTDANGEGD TCDNDIDGDG IPNMLDNCPK VPNHLQTDRD LDGVGDACDS
CPETSNPTQT DADSDLVGDM CDTNQDRDGD GHQDTKDNCP DIPNSSQLDS DNDGKGDECD
QDDDNDGIPD YIPPGPDNCR LIHNPNQKDS DGDGVGDVCE EDFDNDTVID LLDVCPESAE
VTLTDFRAYQ TVILDPEGDA QIDPNWVVLN QGMEIVQTMN SDPGLAVGYT AFNGVDFEGT
FHVNTVTDDD YAGFIFSYQD SSSFYVVMWK QTEQTYWQAT PFRAVAEPGL QLKAVKSTTG
PGEQLRNALW NTGHTQDQVR LLWKDPRNVG WKDKTSYRWQ LMHRPQVGYI RVKLYEGVDL
VADSGVIIDT NMRGGRLGVF CFSQENIIWS NLHYRCNDTI PEDFEPYRRL LQDGKD
//
