ID A0A3Q3NEG3_9LABR Unreviewed; 604 AA.
AC A0A3Q3NEG3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Thrombospondin 2b {ECO:0000313|Ensembl:ENSLBEP00000032670.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000032670.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000032670.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the thrombospondin family.
CC {ECO:0000256|ARBA:ARBA00009456}.
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DR AlphaFoldDB; A0A3Q3NEG3; -.
DR Ensembl; ENSLBET00000034129.1; ENSLBEP00000032670.1; ENSLBEG00000024586.1.
DR GeneTree; ENSGT00940000157846; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
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; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 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; IPR018097; EGF_Ca-bd_CS.
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; IPR028974; TSP_type-3_rpt.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR PANTHER; PTHR10199:SF10; THROMBOSPONDIN-2; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF02412; TSP_3; 7.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51234; TSP3; 4.
DR PROSITE; PS51236; TSP_CTER; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT REPEAT 156..191
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 215..250
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 312..347
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 348..383
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 387..601
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 152..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..178
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 67129 MW; 090A57D40911976D CRC64;
KCSSHSDGSW ECGHCPLGLQ GNGTHCEDED ECEVEDVCVT QCVNTDPGFY CLPCPPRYKG
SQPYGLGLQE AQKIKQVCVC EPYNPCKDNT HTCHRFADCL YLGLASEVLY KCVCAVGFAG
DGFLCGEDSD LDGWPNKRLT CKQNDNCPML PNSGQEDLDQ DGQGDACDPD DDNDDITDER
DNCPLVYNPR QFDSDRDGVG DRCDNCPFES NPLQTDTDGN GEGDACSIDI DGDDVLNDRD
NCPLVYNTDQ RDTDLDGVGD QCDNCPLLHN PLQRDSDSDL VGDMCDNNED IDEDGLQNSL
DNCPYIANSN QADHDNDGKG DACDHDDDND GIPDDRDNCR LVPNKDQLDS DGDGSGDACF
DDFDNDSIPD ALDPCPLNQD IGSTDFRKYQ VVLLDPKGTT QSDPLWVIRS QGTELLQTAN
SDPGIALGYD KFSSVDFSVT FYVNTNRDDD YAGIVFAYQS SRRFYVVMWK QVSQAYWEKK
PFKAFGTAGV SIKLVNSTTG PGEYLRNSLW HTGNTRHQVR TLWHDPNKIG WKDYTAYRMH
LIHRPKTGFI RVVVYEGRNI LSDSGAVYDH TLAGGRLGLF VFSQEHVLFS DLRYECRGKT
TCFS
//