ID A0A3B3R6K6_9TELE Unreviewed; 1146 AA.
AC A0A3B3R6K6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Thrombospondin 2b {ECO:0000313|Ensembl:ENSPKIP00000013555.1};
GN Name=THBS2 {ECO:0000313|Ensembl:ENSPKIP00000013555.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000013555.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000013555.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3B3R6K6; -.
DR STRING; 1676925.ENSPKIP00000013555; -.
DR Ensembl; ENSPKIT00000037979.1; ENSPKIP00000013555.1; ENSPKIG00000000928.1.
DR GeneTree; ENSGT00940000157846; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
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; IPR001881; EGF-like_Ca-bd_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; 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; 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; 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|ARBA:ARBA00022536};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1146
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017340357"
FT DOMAIN 302..359
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT REPEAT 693..728
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 752..787
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 849..884
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 885..920
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 924..1138
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 687..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1146 AA; 126814 MW; 8DDAB6E8A32EFE9F CRC64;
FHWTFLIVEV LGLLVTGYEE VEDQTLFDLL EASHITRKTA GIKLFRGLDA DTPAYRFISV
EHLPSVRAAA LQRLLRQVQN NEGFVLTATL RQDRGSRGTL LAIEGPGGRR QLEIVSNGRT
NTLDLVYWAD GSQNVVSFED VDLADSQWKN VTLHVYGEAA TLYVGCILVD GFILDMPFYE
HLRAEGSKMF VAKGSVRESH FRVRANVVSE SVELDEADPG IAGNAIAPKE DATTPAGTPA
GSDLMCERSC EELHSLFQEL QGLRVVVGNL IDGLQKVVRS QPGHNNQLWA KTLAKIKTSS
EQICWQDGRQ FEDKEEWVVD SCTKCTCQDG KVVCRQIMCP AVACANPTFS DGECCPACLP
NDGDDGWSPW SEWTECSVTC GSGTQQRGRS CDDSSNACAG PSIQTRRCSL SRCESRVRQD
GGWSLWSPWS SCSVTCGEGQ VTRIRHCNAP MPQRGGKDCQ GTGRETQSCQ ADPCPIDGGW
GPWSPWATCS ATCGGGLKSR SRECNSPPPQ HGGRGCMGEP SDNEVCNRQD CPIDGCLSNP
CFAGVECHTG ADGFWECGPC PLGFRGNGTF CEDVNECDMV SDLCYKVIGT ERCINTEPGF
HCLPCPPRYK GTQPYGLGVE AAKNSKQVCI ALTYTCLHPG HNSTHLPQII TPSLLLLYCL
EYNSLRRPPP LTHFGLSIKF QDNCPHLPNS GQEDFDNDGQ GDACDSDDDN DDIVDERDNC
PLHYNPHQFD YDKDDVGDQC DNCPYEHNPA QRDTDNNGEG DACSIDIDGD EILNEQDNCP
YFYNTDQKDT DLDGVGDQCD NCPLVHNPGQ ADKDNDLVGD QCDNNQDIDE DGYQNNMDNC
PYIPNANQAD HDKDGRGDAC DHDDDNDGIP DDRDNCRLVP NPDQLDSDGD GRGDACKDDF
DNDSIPDILD ACPENDAISV TDFRKFQMVH LDPKGTTQID PNWVVRNQGK ELVQTANSDP
GIAVGFDVFN AVDFSGTFYV NTDRDDDYAG FVFGYQSSRR FYVVMWKQIT QTYWEEKPSK
AFGISGVSLK VVNSTTGTGE SLRNALWHTG NTKQQVRTLW HDPNNIGWKD YTAYRWHLIH
RPKTGFIRVV VYEGKQIMAD SGPIYDRTFA GGRLGLFVFS QELVFFSDLK YECRDVFVLK
LDISCI
//
