ID A0A2U9BC83_SCOMX Unreviewed; 650 AA.
AC A0A2U9BC83;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Putative growth arrest-specific protein 6 {ECO:0000313|EMBL:AWP01416.1};
GN ORFNames=F2P81_004403 {ECO:0000313|EMBL:KAF0043066.1}, SMAX5B_012715
GN {ECO:0000313|EMBL:AWP01416.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP01416.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP01416.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF0043066.1, ECO:0000313|Proteomes:UP000438429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ysfricsl-2016a {ECO:0000313|EMBL:KAF0043066.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KAF0043066.1};
RA Xu H., Xu X.-W., Shao C., Chen S.;
RT "Draft genomes of female and male turbot (Scophthalmus maximus).";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CP026247; AWP01416.1; -; Genomic_DNA.
DR EMBL; VEVO01000004; KAF0043066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BC83; -.
DR STRING; 52904.ENSSMAP00000034876; -.
DR OMA; YHGVGRV; -.
DR OrthoDB; 19806at2759; -.
DR Proteomes; UP000246464; Chromosome 5.
DR Proteomes; UP000438429; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 3.
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; IPR009030; Growth_fac_rcpt_cys_sf.
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; PF00008; EGF; 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; 1.
DR SUPFAM; SSF57630; GLA-domain; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 3.
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:UP000246464};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..650
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036052896"
FT DOMAIN 42..88
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 110..148
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 150..189
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 286..463
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 460..643
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 119..136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 138..147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 616..643
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 650 AA; 72044 MW; C2A1908725144E59 CRC64;
MRLTPTKSAA PAALLILLLA RWSDGISLSP EEANQFLSRQ RRANQVFEET KQGHLERECV
EERCTKEEAR EVFENDPETD YFYPKYVACV DKFGDSEKKK QDLVTCVHNI PDQCSPSPCN
DRGTVRCEDK KGDFLCHCFT GWTGARCDKD VDECSKRNGG CDHECNNTIG SYRCSCHQGY
MLVGRQMCND VDECEDTSVC GTARCENNDG SYDCLCDTGF VYDNETKTCV DVDECVSGVC
AEECLNTPGS FRCFCDGRQG KKLGQDLRSC KPITPCLSPS LKRNSRSLYL GRMFSAVPVV
RLRFRRRIQT GFSAEFDFRT WDPEGVIFFA GGHLNSSWIV LAMHHGRLEL QLKYGTVSRV
TSSGPIVSDG QWRKISVEEQ GRSLVIKIDR EAVMKIAVNG DLFTLKKGMH ELNLTVGGVP
FREDGLINQV NPRLDGCMKE WRWLTGEDTS IQETIRSNDN MQCFGTENPG AYFPGTGFAL
FNISCESQNL SVQLNLRPTS AIGVLFALVY QDRVPLSIAL ADYHPGTDEW RDFVLVSTGD
AIIASSPAPL CDGESHEIQV VISGNQTMLL VDGQPGRSED AEVPTALLTQ SSTFIGGLPD
DVSLVSSLVS APYSGCMEVS VNGQSLDLDQ AIHKHNDIRS HSCPLLDSHQ
//
