ID G1KBH7_ANOCA Unreviewed; 1179 AA.
AC G1KBH7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Thrombospondin 2 {ECO:0000313|Ensembl:ENSACAP00000002993.3};
GN Name=THBS2 {ECO:0000313|Ensembl:ENSACAP00000002993.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000002993.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000002993.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000002993.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000002993.3}
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 RefSeq; XP_008122806.1; XM_008124599.2.
DR AlphaFoldDB; G1KBH7; -.
DR STRING; 28377.ENSACAP00000002993; -.
DR Ensembl; ENSACAT00000003070.4; ENSACAP00000002993.3; ENSACAG00000002861.4.
DR GeneID; 100563584; -.
DR KEGG; acs:100563584; -.
DR CTD; 7058; -.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR GeneTree; ENSGT00940000157846; -.
DR HOGENOM; CLU_009257_0_0_1; -.
DR InParanoid; G1KBH7; -.
DR OrthoDB; 5345349at2759; -.
DR TreeFam; TF324917; -.
DR Proteomes; UP000001646; Chromosome 1.
DR Bgee; ENSACAG00000002861; Expressed in gonad and 3 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0031091; C:platelet alpha granule; IEA:Ensembl.
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 GO; GO:0016525; P:negative regulation of angiogenesis; IBA:GO_Central.
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; 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; 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:UP000001646};
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..1179
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003412910"
FT DOMAIN 325..382
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 556..596
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 655..697
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 736..771
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 795..830
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 892..927
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 928..963
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 967..1179
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 738..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..758
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1179 AA; 131380 MW; 0D74AF86AAFF77AD CRC64;
MLHRSWLLWL TILLTLWISS EAQDEDGGDE TTYDLMQISN INRKTIGAKA FRGNISGVPA
YRFIRFDHIP PLNSEKLKQI VKLIQQNEGF ILTATFRQDR DSRGTIIALE GPGISQRQFE
IISNGRDNTL ELSYWVDGSR KGYPLEDVDL ADLQWKNITI QVLGENYSLY VGCDLIDSLS
LEEPFYENLK AEKSRMYVVK GSTRENHFRG LIQNIHLIFG TSVEDVLRNK GCQKSQSAEV
NTINESTEIL HLTPSVMTEY IGDNTEKKPE FCDRSCEELG SMFTELTGLR IVVNGLTEKL
EKVSEVNEKI VSELLGPNKT LKNQSACWQD GREFVNNSHW VVDSCTKCHC QNSKTVCNKI
TCPPVHCVSP AFIDGECCPV CSHSDDSEEG WSPWSEWTEC SVTCGSGTQQ RGRSCDVTSN
TCRGPSIQTR TCSLGKCDNR IRQDGGWSHW SPWSSCSVTC GVGNITRIRL CNSPIPQMGG
KGCKGSGRET KECEGPPCPV NGRWSPWSPW SACTVTCGGG IHERSRLCNS PEPQYGGKPC
VGDVIQRDMC NKQDCPIDGC LSNPCFPGAD CNSYPDGSWS CGACPAGYLG NGTFCEDLNE
CAVVPDVCFK LNQNHRCVNT NPGFHCLPCP PRYKGTQPYG VGLEAARAEK QVCEPANPCK
DKTHNCHRSA ECIYLGHFSD PMYKCECRTG YAGDGFICGE DSDLDGWPNN NLVCAANATY
HCMKDNCPLL PNSGQEDFDK DGKGDACDED DDNDGVEDDK DNCPLLFNPR QFDYDKDEVG
DRCDNCPYVH NPAQIDTDNN GEGDACAVDI DGDDVFNARD NCPYVYNTDQ IDTDGDGVGD
QCDNCPLVHN PEQTDVDNDL VGDQCDNNED IDEDGHQNNK DNCPYISNAN QADHDKDGKG
DACDPDDDND GIPDDRDNCR LTFNPDQKDS DGDGRGDICK DDFDNDKVPD IYDVCPENDA
ISETDFRKFQ MVPLDPKGTT QIDPNWVIRH QGKELVQTAN SDPGIAVGYD EFSSVDFSGT
FYVNTDRDDD YAGFVFAYQS SSRFYVLMWK QVTQTYWEDK PTRAYGYSGV SLKVVNSTTG
TGEHLRNALW HTGNTAGQVR TLWHDPKNIG WKDYTAYRWH LIHRPKTGLI KVLVYEGKQI
MADSGAIYDK TYAGGRLGLF VFSQEMVYFS DLKYECRDA
//
