ID G3PRG5_GASAC Unreviewed; 644 AA.
AC G3PRG5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Growth arrest-specific 6 {ECO:0008006|Google:ProtNLM};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000020200.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000020200.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000020200.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000256|ARBA:ARBA00008850}.
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; G3PRG5; -.
DR Ensembl; ENSGACT00000020239.1; ENSGACP00000020200.1; ENSGACG00000015310.1.
DR GeneTree; ENSGT00940000154035; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000015310; Expressed in zone of skin and 12 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 4.10.740.10; Coagulation Factor IX; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR24040:SF14; GROWTH ARREST-SPECIFIC PROTEIN 6; 1.
DR PANTHER; PTHR24040; LAMININ G-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57630; GLA-domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Gamma-carboxyglutamic acid {ECO:0000256|ARBA:ARBA00022479};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 37..83
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 105..143
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 145..184
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 284..458
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 465..637
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 114..131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 133..142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 610..637
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 644 AA; 71528 MW; 5C4913C32EA8C280 CRC64;
IRICGTKIAR KCICLTFCCY VSLSPEEAKQ FLSRPRRANQ VFEETKQGHL ERECVEEKCS
KEEAREVFEN DPETDYFYPK YLACMEKFGD AEKKKQDLIT CVHNIPDQCS PSPCNARGTV
RCEDKKGDFL CHCFTGWAGA RCDKDVDECS KRNGGCDHEC NNTMGSYRCS CHQGYVLVER
HMCDDVDECD NPGVCGTARC ENKKGGFGCS CDVGYVYDNE TKSCVDVDEC GADVCAEQCL
NTLGSFRCFC DGRQGMKLGR DLRSCKTITP CMSPSLRRNS RSLYLGRMFS GVPVVRLRFR
RRVQTGFSAE FDFRSYDAEG VIFFAGGHLN SSWIVLAMHH GKLELQLKYG TVSRVTSSGP
VVNDGEWRKI SVEEQGRSLV IKIDREAVMK IAVNGDLFTL NKGMHELNLT VGGVPFREDG
LVNQVNPRLD GCMKEWKWLT GEDTSIQETI RSNDNMQCFN TEKPGTYYPG TGFALFNISY
EPQSLSVQLT LRPTSAIGVL FALVHQDRVP LSIALADYHP GTDEWRDFVL VSVSDVIVAS
SPAPLCDGES HEILVTISGN QTLLLVDGQA GRSEETDIST DVLSQSSTFI GGLPDVSLVT
TLVSAPYSGC MEVSVNGQPL DLDQAIHKHN DIRSHSCPLL DSHQ
//
