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Database: UniProt
Entry: G3QDS4_GORGO
LinkDB: G3QDS4_GORGO
Original site: G3QDS4_GORGO 
ID   G3QDS4_GORGO            Unreviewed;       422 AA.
AC   G3QDS4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Protein Z, vitamin K dependent plasma glycoprotein {ECO:0000313|Ensembl:ENSGGOP00000000401.3};
GN   Name=PROZ {ECO:0000313|Ensembl:ENSGGOP00000000401.3};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000000401.3, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000000401.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000000401.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000000401.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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; CABD030090966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030090967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030090968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004054814.2; XM_004054766.2.
DR   AlphaFoldDB; G3QDS4; -.
DR   STRING; 9593.ENSGGOP00000000401; -.
DR   MEROPS; S01.979; -.
DR   Ensembl; ENSGGOT00000000410.3; ENSGGOP00000000401.3; ENSGGOG00000000407.3.
DR   GeneID; 101136586; -.
DR   CTD; 8858; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000154505; -.
DR   InParanoid; G3QDS4; -.
DR   OMA; NTARYMI; -.
DR   OrthoDB; 5172471at2759; -.
DR   TreeFam; TF327329; -.
DR   Proteomes; UP000001519; Chromosome 13.
DR   Bgee; ENSGGOG00000000407; Expressed in liver and 4 other cell types or tissues.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProt.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005796; C:Golgi lumen; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 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; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
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; IPR001254; Trypsin_dom.
DR   PANTHER; PTHR24278; COAGULATION FACTOR; 1.
DR   PANTHER; PTHR24278:SF20; VITAMIN K-DEPENDENT PROTEIN Z; 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; PR00001; GLABLOOD.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57630; GLA-domain; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   4: Predicted;
KW   Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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   Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..422
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030171760"
FT   DOMAIN          63..109
FT                   /note="Gla"
FT                   /evidence="ECO:0000259|PROSITE:PS50998"
FT   DOMAIN          109..145
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          197..422
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        135..144
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   422 AA;  46966 MW;  722450933CBBE619 CRC64;
     MAGCVPLLQG LVLVLALHRV EPSATSLKER HGLHSDSACT GVQESLFLPA SKANDVLVRW
     KRAGSYLLEE LFEGNLEKEC YEEICVYEEA REVFENEVVT DEFWRRYKGG SPCISQPCLH
     NGSCQDSIWG YTCTCSPGYE GSNCELAKNE CHPERTDGCQ HFCLPGQESY TCSCAQGYRL
     GEDHKQCVPH DQCACGVLTS EKRAPDLQDL PWQVKLTNSE GKDFCGGVII RENFVLTTAK
     CSLLHRNITV KTYFNRTSQD PLMIKITHVH VHMRYDADAG ENDLSLLELE WPIQCPGAGL
     PVCTPEKDFA EHLLIPRTRG LLSGWARNGT DLGNSLTTRP VTLVEGEECG QVLNVTVTTR
     AYCERSSVAA MHWMEGSVVT REHGGSWFLT GVLGSQPVGG QAHMVLVTKV SRYSLWFKRI
     MN
//
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