ID A0A3Q2WVQ9_HAPBU Unreviewed; 1159 AA.
AC A0A3Q2WVQ9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Thrombospondin 2 {ECO:0000313|Ensembl:ENSHBUP00000026449.1};
GN Name=THBS2 {ECO:0000313|Ensembl:ENSHBUP00000026449.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000026449.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000026449.1}
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 AlphaFoldDB; A0A3Q2WVQ9; -.
DR Ensembl; ENSHBUT00000003323.1; ENSHBUP00000026449.1; ENSHBUG00000009211.1.
DR GeneTree; ENSGT00940000157846; -.
DR Proteomes; UP000264840; Unplaced.
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; PS50026; EGF_3; 1.
DR PROSITE; PS50092; TSP1; 3.
DR PROSITE; PS51234; TSP3; 4.
DR PROSITE; PS51236; TSP_CTER; 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:UP000264840};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 302..375
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 629..671
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 710..745
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 769..804
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 866..901
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 902..937
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 941..1155
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 707..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1159 AA; 128873 MW; C32A9EB042A4DE12 CRC64;
MLDSLQLLAF QAMTEDETSF DLFEISDITR RTLGAKQFRG QNLDAPAYRF IRFDHLPPVS
PPILKQMLHQ IQNNEGFVFV ASIRQDRSSR GTLIGLEGPD GRRQFEIVSN GRANTLDLVY
WADGSQNVVS FEDVDLSDSQ WKNITLHVHG ENANLFVGCS LIDSFILDEP FYEHLKAEGS
RMYVAKGSIR ENHFRGLLQS VRFIFDTSIE DILLSRDCEI TKQDDANIVS ESGEIVDVSP
SITTNVIGQK TDDVGAEMCE RSCEELSTMF QELKGLRIVV SNLIDGLQKV LMCFLWEPPK
KNMCWQDGRL FDDKEDWVVD SCTKCTCQES KIVCHQITCP PVACASPSFI DGECCPASMD
SDDGWSPWSE WTECTVTCGI GTQQRGRSCD ATSNPCTGPS IQTRKCSLGK CDSRVRQDGG
WSLWSPWSSC SVTCGEGQIT RIRHCNAPVP QLGGRDCEGS GRETQGCTAK PCPIDGGWGP
WSPWATCSAT CGGGHKSRSR ECNSPEPQYG GKKCFGEAVD RDSCNKNDCP IDGCLSNPCF
AGVDCSSSAD GSWECGPCPA GFRGNGTHCE DINECDMVSD VCYKVNGMQR CVNTDPGFHC
LPCPKRYKGT QPFGMGVEAA KKNKQVCEPE NPCKDRTHNC HKYAECIYIS HFSDPMYKCE
CRTGYAGDGF ICGEDSDLDG WPNQNLVCGA NATYHCKKDN CPSLPNSGQE DFDRDGQGDA
CDKDDDNDGI LDERDNCPLL YNPRQFDFDK DEVGDRCDNC PYEHNPAQID TDHNGEGDAC
AVDIDGDGIL NENDNCPYVY NTDQKDTDMD GVGDQCDNCP LLHNPDQTDL DNDLVGDQCD
NSQDIDEDGH QNNLDNCPYV ANSNQADHDK DGKGDACDYD DDNDGIPDDR DNCRLTPNED
QEDSDGDGRG DACKDDFDND SIPDILDVCP ENNAISVTDF RKFQMVHLDP KGTTQIDPNW
VVRHQGKELV QTANSDPGIA VGFDEFSAVD FSGTMYVNTD RDDDYAGFVF GYQSSGRFYV
VMWKQITQTY WEDKPSKAFG ISGVSLKVVN STTGTGEYLR NALWHTGNTP GQVRTLWHDP
KNIGWKDYTA YRWHLIHRPK TGFIRVVVYE GKQIMADSGP IYDKTFAGGR LGLFVFSQEL
VFFSDLKYEC RGKHNYLKL
//