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Database: UniProt
Entry: A0A087VJG1_BALRE
LinkDB: A0A087VJG1_BALRE
Original site: A0A087VJG1_BALRE 
ID   A0A087VJG1_BALRE        Unreviewed;      1111 AA.
AC   A0A087VJG1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Thrombospondin-1 {ECO:0000313|EMBL:KFO12753.1};
DE   Flags: Fragment;
GN   ORFNames=N312_01584 {ECO:0000313|EMBL:KFO12753.1};
OS   Balearica regulorum gibbericeps (East African grey crowned-crane).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX   NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO12753.1, ECO:0000313|Proteomes:UP000053309};
RN   [1] {ECO:0000313|EMBL:KFO12753.1, ECO:0000313|Proteomes:UP000053309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO12753.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL495693; KFO12753.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087VJG1; -.
DR   Proteomes; UP000053309; Unassembled WGS sequence.
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:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 6.20.200.20; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
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; IPR024731; EGF_dom.
DR   InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR   InterPro; IPR017897; Thrombospondin_3_rpt.
DR   InterPro; IPR008859; Thrombospondin_C.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   InterPro; IPR028974; TSP_type-3_rpt.
DR   InterPro; IPR048287; TSPN-like_N.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR   PANTHER; PTHR10199:SF78; THROMBOSPONDIN-1; 1.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF00090; TSP_1; 3.
DR   Pfam; PF02412; TSP_3; 7.
DR   Pfam; PF05735; TSP_C; 1.
DR   Pfam; PF00093; VWC; 1.
DR   PRINTS; PR01705; TSP1REPEAT.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00209; TSP1; 3.
DR   SMART; SM00210; TSPN; 1.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS50092; TSP1; 3.
DR   PROSITE; PS51234; TSP3; 4.
DR   PROSITE; PS51236; TSP_CTER; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 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}; Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053309};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          305..362
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          536..576
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          635..679
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          716..751
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          775..810
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          872..907
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          908..943
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   DOMAIN          947..1111
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51236"
FT   REGION          713..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        827..857
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        872..886
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..925
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO12753.1"
FT   NON_TER         1111
FT                   /evidence="ECO:0000313|EMBL:KFO12753.1"
SQ   SEQUENCE   1111 AA;  122525 MW;  798BAF3D2A10A987 CRC64;
     SDLSAESRSD DNSVFDLFEL IGFIRKGAGR RAPGVHLVKG PESSSPAYRI EDASRIPAVP
     DSKFQDLLDA IHAEKGFILL ATLRQAKKSR GTLLSVEQKD GSGHVFSLVS NGKAGTLDLS
     LSGDGKQQLV SVEDALLATG HWKNITLFVQ EDRAQLYVGC EKMENAELDI PIQNIFTRDL
     ASSARLRIAK GGVNDNFQGL LQNVRFVFGT TLETILRNKG CSSSTSAIIT LDNPINGSSP
     AIRTNYIGHK TKDIQAVCGF SCDELTNMFV ELQGLRSMVT TLQDRVRKVT EENELIAKVV
     QITPGVCIHN GILHKNKEEW TIDSCTECTC QNSATICRKV SCPLMPCSNA TVPDGECCPR
     CWPSDYADDG WSPWSEWTSC SVTCGNGIQQ RGRSCDSLNN RCEGSSVQTR TCHLQECDKR
     FKQDGGWSHW SPWSSCSVTC GTGIITRIRL CNSPVPQLNG KPCEGEAREN KPCQKDPCPI
     NGNWGPWSPW DACTVTCGGG LQKRSRLCNN PEPQYGGKTC VGEARGTQVC NKQDCPIDGC
     LSNPCFAGTT CTSSPDGSWK CGACPAGYHG DGVHCQDIDE CKEVPDACFV FNGVHRCENT
     EPGYNCLPCP PRFTGTQPFG RSVEDAMANK QVCKPRNPCT DGTHDCNKNA KCNYLGHFSD
     PMYRCECKPG YAGNGIICGE DTDLDGWPNE NLVCVANATY HCKKDNCPNL PNSGQEDYDK
     DGIGDACDND DDDDGIPDDR DNCPFIYNPQ QYDYDRDDVG DRCDNCPYNH NPDQTDTDNN
     GEGDACAVDI DGDGVLNERD NCQYVYNVDQ RDTDLDGVGD QCDNCPLEHN PDQEDTDSDR
     IGDQCDNNQD IDEDGHQNNL DNCPYVPNAN QADHDKDGKG DACDHDDDND GMPDDKDNCR
     LVANPDQADS DGDGRGDACK DDFDQDSVPD IDDICPENVD ISETDFRRFQ MIPLDPKGTS
     QNDPNWVVRH QGKELVQTVN CDPGLAVGFD EFNAVDFSGT FFINTERDDD YAGFVFGYQS
     SSRFYVVMWK QITQSYWDST PTKAQGYSGL SIKVVNSTTG PGEHLRNALW HTGNTPGQVR
     TLWHDPRHIG WKDFTAYRWR LSHRPKTGYI R
//
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