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Database: UniProt
Entry: A0A0Q3QBR9_AMAAE
LinkDB: A0A0Q3QBR9_AMAAE
Original site: A0A0Q3QBR9_AMAAE 
ID   A0A0Q3QBR9_AMAAE        Unreviewed;      1176 AA.
AC   A0A0Q3QBR9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Thrombospondin-1 {ECO:0000313|EMBL:KQK85612.1};
GN   ORFNames=AAES_38879 {ECO:0000313|EMBL:KQK85612.1};
OS   Amazona aestiva (Blue-fronted Amazon parrot).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX   NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK85612.1, ECO:0000313|Proteomes:UP000051836};
RN   [1] {ECO:0000313|EMBL:KQK85612.1, ECO:0000313|Proteomes:UP000051836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FVVF132 {ECO:0000313|EMBL:KQK85612.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQK85612.1}.
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DR   EMBL; LMAW01000736; KQK85612.1; -; Genomic_DNA.
DR   STRING; 12930.A0A0Q3QBR9; -.
DR   Proteomes; UP000051836; 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:UP000051836};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1176
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006206773"
FT   DOMAIN          322..379
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          553..593
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          652..696
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          733..768
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          792..827
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          889..924
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          925..960
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   DOMAIN          964..1176
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51236"
FT   REGION          730..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          780..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..755
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..874
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        889..903
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        927..944
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1176 AA;  129722 MW;  DA8B5B83C1B9CF20 CRC64;
     MGPTAALCLL LLLSGSEARR TAESRSDDNS VFDLFELIGL IRKGAGRRAP GVHLVKGPES
     SSPAYRIEDA SRIPPVPDSK FQDLLDAIHT EKGFILLATL RQAKKSRGTL LSVEQKDGSG
     HVFSLVSNGK AGTLDLSLXG DGKQQIVSVE DALLATGHWK NITLFVQEDR AQLYVGCEKM
     ENAELDIPIQ NIFTRDLASS ARLRIAKGGV NDNFQGLLQN VRFVFGTTLE TILRNKGCSS
     STSAIITLDN PINGSSPAIR TNYIGHKTKD IQAVCGFSCD ELTNMFVELQ GLRSMVTTLQ
     DRVRKVTEEN ELIAKVVQIT PGVCIHNGIL HKNKEEWTID SCTECTCQNS ATICRKVSCP
     LMPCSNATVP DGECCPRCWP SDYADDGWSP WSEWTSCSVT CGNGIQQRGR SCDSLNNRXE
     GSSVQTRTCH LQECDKRFKQ DGGWSHWSPW SSCSVTCGTG IITRIRLCNS PVPQLNGKPC
     EGEARENKPC QKDPCPINGN WGPWSPWDAC TVTCGGGLQK RSRLCNNPEP QYGGKTCVGE
     ARGTQVCNKQ DCPIDGCLSN PCFAGTTCTS SPDGSWKCGA CPPGYHGDGI HCQDIDECKE
     VPDACFVFNG VHRCENTEPG YNCLPCPPRF TGTQPFGRSV EDAMANKQVC KPRNPCTDGT
     HDCNKNAKCN YLGHFSDPMY RCECKPGYAG NGIICGEDTD LDGWPNENLV CVANATYHCK
     KDNCPDLPNS GQXDYDKDGV GDACDNDDDD DGIPDDRDNC PFIYNPQQYD YDRDDVGDRC
     DNCPYNHNPD QTDTDNNGEG DACAVDIDGD GVLNEMDNCQ YVYNVDQRDT DLDGVGDQCD
     NCPLEHNPDQ EDADSDRIGD QCDNNQDIDE DGHQNNLDNC PYVPNANQAD HDKDGKGDAC
     DHDDDNDGIP DDKDNCRLVA NPDQADSDGD GRGDACKXDF DQDSVPDIDD ICPENVDISE
     TDFRKFQMIP LDPKGTSQND PNWVVRHQGK ELVQTVNCDP GLAVGFDEFN AVDFSGTFFI
     NTERDDDYAG FVFGYQSSSR FYVVMWKQIT QSYWDSTPTK AQGYSGLSIK VVNSTTGPGE
     HLRNALWHTG NTPGQVRTLW HDPRHIGWKD FTAYRWRLSH RPKTGYIRVV MYEGKKIMAD
     SGPIYDKTYA GGRLGLFVFS QEMVFFSDLK YECRDP
//
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