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Database: UniProt
Entry: A0A3Q2VA56_HAPBU
LinkDB: A0A3Q2VA56_HAPBU
Original site: A0A3Q2VA56_HAPBU 
ID   A0A3Q2VA56_HAPBU        Unreviewed;      1185 AA.
AC   A0A3Q2VA56;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Thrombospondin 2 {ECO:0000313|Ensembl:ENSHBUP00000007609.1};
GN   Name=THBS2 {ECO:0000313|Ensembl:ENSHBUP00000007609.1};
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:ENSHBUP00000007609.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000007609.1}
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   RefSeq; XP_005915524.1; XM_005915462.2.
DR   RefSeq; XP_005915525.1; XM_005915463.2.
DR   AlphaFoldDB; A0A3Q2VA56; -.
DR   STRING; 8153.ENSHBUP00000007609; -.
DR   Ensembl; ENSHBUT00000003351.1; ENSHBUP00000007609.1; ENSHBUG00000009211.1.
DR   GeneID; 102305848; -.
DR   CTD; 100535241; -.
DR   GeneTree; ENSGT00940000157846; -.
DR   OrthoDB; 5345349at2759; -.
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; 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:UP000264840};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1185
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018640314"
FT   DOMAIN          323..380
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          652..694
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..1178
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51236"
FT   REGION          730..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          855..939
FT                   /note="Disordered"
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        910..939
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1185 AA;  131761 MW;  314931595B2E9D42 CRC64;
     MILRRSLFLL LLSFNYLQAL TEDGEQEDET SFDLFEISDI TRRTLGAKQF RGQNLDAPAY
     RFIRFDHLPP VSPPILKQML HQIQNNEGFV FVASIRQDRS SRGTLIGLEG PDGRRQFEIV
     SNGRANTLDL VYWADGSQNV VSFEDVDLSD SQWKNITLHV HGENANLFVG CSLIDSFILD
     EPFYEHLKAE GSRMYVAKGS IRENHFRGLL QSVRFIFDTS IEDILLSRDC EITKQDDANI
     VSESGEIVDV SPSITTNVIG QKTDDVGAEM CERSCEELST MFQELKGLRI VVSNLIDGLQ
     KVTEENSVMK DALGRMKNSS EKNMCWQDGR LFDDKEDWVV DSCTKCTCQE SKIVCHQITC
     PPVACASPSF IDGECCPACL PMDSDDGWSP WSEWTECTVT CGIGTQQRGR SCDATSNPCT
     GPSIQTRKCS LGKCDSRVRQ DGGWSLWSPW SSCSVTCGEG QITRIRHCNA PVPQLGGRDC
     EGSGRETQGC TAKPCPIDGG WGPWSPWATC SATCGGGHKS RSRECNSPEP QYGGKKCFGE
     AVDRDSCNKN DCPIDGCLSN PCFAGVDCSS SADGSWECGP CPAGFRGNGT HCEDINECDM
     VSDVCYKVNG MQRCVNTDPG FHCLPCPKRY KGTQPFGMGV EAAKKNKQVC EPENPCKDRT
     HNCHKYAECI YISHFSDPMY KCECRTGYAG DGFICGEDSD LDGWPNQNLV CGANATYHCK
     KDNCPSLPNS GQEDFDRDGQ GDACDKDDDN DGILDERDNC PLLYNPRQFD FDKDEVGDRC
     DNCPYEHNPA QIDTDHNGEG DACAVDIDGD GILNENDNCP YVYNTDQKDT DMDGVGDQCD
     NCPLLHNPDQ TDLDNDLVGD QCDNSQDIDE DGHQNNLDNC PYVANSNQAD HDKDGKGDAC
     DYDDDNDGIP DDRDNCRLTP NEDQEDSDGD GRGDACKDDF DNDSIPDILD VCPENNAISV
     TDFRKFQMVH LDPKGTTQID PNWVVRHQGK ELVQTANSDP GIAVGFDEFS AVDFSGTMYV
     NTDRDDDYAG FVFGYQSSGR FYVVMWKQIT QTYWEDKPSK AFGISGVSLK VVNSTTGTGE
     YLRNALWHTG NTPGQVRTLW HDPKNIGWKD YTAYRWHLIH RPKTGFIRVV VYEGKQIMAD
     SGPIYDKTFA GGRLGLFVFS QELVFFSDLK YECRDKPELP TVLTR
//
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