ID A0A060W652_ONCMY Unreviewed; 483 AA.
AC A0A060W652;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CDQ62526.1, ECO:0000313|Ensembl:ENSOMYP00000096265.1};
GN ORFNames=GSONMT00067350001 {ECO:0000313|EMBL:CDQ62526.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ62526.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ62526.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ62526.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSOMYP00000096265.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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; FR904410; CDQ62526.1; -; Genomic_DNA.
DR STRING; 8022.A0A060W652; -.
DR PaxDb; 8022-A0A060W652; -.
DR Ensembl; ENSOMYT00000104586.2; ENSOMYP00000096265.1; ENSOMYG00000043835.2.
DR GeneTree; ENSGT00940000165072; -.
DR OrthoDB; 4629979at2759; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR Proteomes; UP000694395; Chromosome 15.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.740.10; Coagulation Factor IX; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR012224; Pept_S1A_FX.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24278; COAGULATION FACTOR; 1.
DR PANTHER; PTHR24278:SF25; COAGULATION FACTOR IX-LIKE; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57630; GLA-domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
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}; Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000193380};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..483
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040664747"
FT DOMAIN 42..88
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 88..124
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 243..474
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 284
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT ACT_SITE 329
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT ACT_SITE 426
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT DISULFID 114..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 483 AA; 54072 MW; 77AC5443315C74F5 CRC64;
MSQSDGWLLT VLLVSVCSLF ESKVFLEQRD AGQLLRGPRR PRANFFLEEM MPGNLERECY
EETCSQEEAA EIFQTNEKTM EFWYRYKNLN PCHYNPCKNG GICTIDRDGY LCLCPPRYDG
KTCAIEVFEC QFKNGGCLHY CTNQERTTGV QCSCAEGYQL DEDGKTCSEA VAFPCGKKQS
EASLHRSLLD ESEALTLRNS DRNLNISMEV EGNSTSRLSG INSTQPGGNS TEYMEGANED
NRIVGGQLER QGGSPWQVML WREDGYGFCG GTLISQRWVV SAAHCMQETP DHVTIGDYDK
RRPDPNEQKI KVAKVVVHPH FHDYTFDSDI ALVYLSAPVA LSPVAVPACL PNGQLAHHLQ
REDVRGLVTG WGATQYLGRS SRFLRKVALP VVDQQKCIRS TEQVITDNMF CAGYLEASLD
ACSGDSGGPF VVNYRGTWFL TGVVSWGEKC AAKGKYGIYT RLGNYLHWIQ DTIERQAHNI
SHT
//
