ID W5NHC5_LEPOC Unreviewed; 1177 AA.
AC W5NHC5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Thrombospondin 2 {ECO:0000313|Ensembl:ENSLOCP00000020034.1};
GN Name=THBS2 {ECO:0000313|Ensembl:ENSLOCP00000020034.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000020034.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000020034.1}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AHAT01001667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006638832.1; XM_006638769.2.
DR AlphaFoldDB; W5NHC5; -.
DR Ensembl; ENSLOCT00000020067.1; ENSLOCP00000020034.1; ENSLOCG00000016241.1.
DR GeneID; 102686166; -.
DR KEGG; loc:102686166; -.
DR CTD; 100535241; -.
DR GeneTree; ENSGT00940000157846; -.
DR HOGENOM; CLU_009257_0_0_1; -.
DR OrthoDB; 5345349at2759; -.
DR Proteomes; UP000018468; Linkage group LG16.
DR Bgee; ENSLOCG00000016241; Expressed in zone of skin and 13 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:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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:SF10; THROMBOSPONDIN-2; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF00090; TSP_1; 3.
DR Pfam; PF02412; TSP_3; 6.
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; 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; 1.
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:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1177
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004867752"
FT DOMAIN 324..381
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 653..697
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 734..769
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 793..828
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 890..925
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 926..961
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 965..1177
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 849..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1177 AA; 131505 MW; 3C8A280C2A2A9AAC CRC64;
MILRRRLLWL PVLFIICASS KAQDDEVEDN SVFDLFEISK ITRKTLGAKQ FRGQDPNSPA
YRFIRFDHLP HVNPAVLRQI LQQMQNNEGF VFLATIRQDR GSRGTLLALE GPGSTQRQFE
IVSNGKADTL DLVYWVDGSQ NVVSFEDVEL SDSQWKNITL HVHGENANLY IGCTLFDSFI
LDEPFYEHLR ADGSRMYVAK GSIRENHFRG LLQNVRFIFD TSVEDILRNK GCEISKPEEV
NAVSESTEIV DVSPAITTNF IGQKTDQAAD FCDRSCEEFS TMFQELKGLR VVVSNLIDGL
QKVTEENGIM RNILDKMENP SEQDMCWQDG RLFEDKEDWI VDSCTKCTCK ESKVVCNQIT
CPAVSCASPS FIEGECCPVC LPKDSEDGWS PWSEWTECTV TCGTGTQQRG RSCDATNNPC
VGPSIQTRRC SLGKCDSRFR QDGGWSLWSP WSSCSVTCGE GMVTRIRHCN APMPQLGGKN
CEGSGRETQR CEAEPCPIDG GWGPWSPWAT CSATCGKGLR GRTRVCNSPQ PQYGGKKCMG
DPNGNESCND HACPIDGCLS NPCFAGVECN SSPDGSWECG PCPVGFRGNG TFCEDLNECD
LVSDVCFKVN NVQRCINTDP GFHCLPCPPR YKGTQPFGMG IEAAKKNKQV CEPENPCKDK
THSCHKYAEC IYLSHFSDPM YKCECKIGYA GDGIICGEDS DLDGWPNQNL VCGANATYHC
NKDNCPNLPN SGQEDFDKDG QGDACDKDDD NDSIVDERDN CPLLYNPRQF DYDKDDVGDR
CDNCPYEHNP AQIDTDNNGE GDACAIDIDG DEILNEHDNC PYVYNTDQKD TDLDKVGDQC
DNCPLVHNPD QADTDNDLVG DKCDNNQDID EDGHQNNLDN CPYIANANQA DHDKDGKGDA
CDHDDDNDGV PDDRDNCRLV PNRDQLDSDG DGRGDACKDD FDNDNIPDIF DVCPENFDIS
VTDFRKFQMV HLDPKGTTQI DPNWVVRHQG KELVQTANSD PGIAVGYDEF NAVDFSGTFY
VNTDRDDDYA GFVFGYQSSG RFYVVMWKQI TQTYWEEKPS MAYGISGVSL KVVNSTTGTG
ENLRNALWHT GNTPGQVRTL WHDPKNIGWK DYTAYRWHLI HRPKTGFIRV VVYEGKQIMA
DSGPIYDKTF AGGRLGLFVF SQELVFFSDL KYECRDN
//
