ID U3I892_ANAPP Unreviewed; 1127 AA.
AC U3I892;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Thrombospondin 1 {ECO:0000313|Ensembl:ENSAPLP00000003463.2};
GN Name=THBS1 {ECO:0000313|Ensembl:ENSAPLP00000003463.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000003463.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000003463.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000003463.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; U3I892; -.
DR Ensembl; ENSAPLT00000004064.2; ENSAPLP00000003463.2; ENSAPLG00000003908.2.
DR GeneTree; ENSGT00940000155832; -.
DR HOGENOM; CLU_009257_0_0_1; -.
DR Proteomes; UP000016666; Chromosome 5.
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; 2.
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; 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; 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; 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 4: Predicted;
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|PROSITE-ProRule:PRU00076};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1127
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019729108"
FT DOMAIN 324..381
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 555..595
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 603..647
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 684..719
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 743..778
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 840..875
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 876..911
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 915..1127
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 681..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 124317 MW; 6BC07E15A722040B CRC64;
MGPAALLVLV LLLLRGGSEA RRTAESRADD NSVFDLFELI GFIRKGAGRR APGVHLVKGP
ESSSPAYRIE DASRIPAVPD AKFQDLLDAI HAEKGFILLA TLRQAKKSRG TLLAVEQKDG
SGHVFSLVSN GKAGTLDLSL SGDGKQQLVS VEDALLATGH WKNITLFVQE DRAQLYVGCE
KMENAELDIP IQNIFTRDLA SSARLRIAKG GVNDNFQGLL QNVRFVFGTT LETILRNKGC
SSSTSAIITL DNPMNGSSPA IRTNYIGHKT KDIQAVCGFS CDELTNMFVE LQGLRSMVTT
LQDRVRKVTE ENELIAKVVQ ITPGVCIHNG IMHKNKEEWT IDSCTECTCQ NSATICRKVS
CPLMPCSNAT VPDGECCPRC WPSDYADDGW SPWSEWTSCS VTCGNGIQQR GRSCDSLNNR
CEGSSVQTRT CHLQECDKRF KQDGGWSHWS PWSSCSVTCG TGMITRIRLC NSPVPQLNGK
PCEGEARETK SCQKDPCPIN GNWGPWSPWD ACTVTCGGGL QKRSRLCNNP EPQYGGKTCV
GEAKGTQVCN KQDCPIDGCL SNPCFAGTTC TSSPDGSWKC GACPAGYHGD GIHCEDIDEV
CKPRNPCTDG THDCNKNAKC NYLGHFSDPM YRCECKPGYA GNGIICGEDT DLDGWPNENL
VCVANATYHC KKDNCPNLPN SGQEDYDKDG IGDACDNDDD DDGIPDDRDN CPFIYNPQQY
DYDRDDVGDR CDNCPYNHNP DQIDTDNNGE GDACAVDIDG DGVLNERDNC QYVYNVDQRD
TDLDGVGDQC DNCPLEHNPD QEDTDSDRIG DECDNNQDID EDGHQNNLDN CPYVPNANQA
DHDKDGKGDA CDHDDDNDGI PDDKDNCRLV ANPDQADSDG DGRGDACKDD FDQDSVPDID
DICPENVDIS ETDFRRFQMI PLDPKGTSQN DPNWVVRHQG KELVQTVNCD PGLAVGFDEF
NAVDFSGTFF INTERDDDYA GFVFGYQSSS RFYVVMWKQI TQSYWDSTPT KAQGYSGLSI
KVVNSTTGPG EHLRNALWHT GNTPGQVRTL WHDPRHIGWK DFTAYRWRLS HRPKTGYIRV
VMYEGKKIMA DSGPIYDKTY AGGRLGLFVF SQEMVFFSDL KYECRDP
//
