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Database: UniProt
Entry: P00744
LinkDB: P00744
Original site: P00744 
ID   PROZ_BOVIN              Reviewed;         396 AA.
AC   P00744;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   01-OCT-2014, entry version 129.
DE   RecName: Full=Vitamin K-dependent protein Z;
GN   Name=PROZ;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-59; ASN-191; ASN-289 AND
RP   THR-388, HYDROXYLATION AT ASP-64, AND GAMMA-CARBOXYGLUTAMATION AT
RP   GLU-7; GLU-8; GLU-11; GLU-15; GLU-17; GLU-20; GLU-21; GLU-26; GLU-27;
RP   GLU-30; GLU-33; GLU-36 AND GLU-40.
RX   PubMed=3888670; DOI=10.1016/0014-5793(85)80633-5;
RA   Hoejrup P., Jensen M.S., Petersen T.E.;
RT   "Amino acid sequence of bovine protein Z: a vitamin K-dependent serine
RT   protease homolog.";
RL   FEBS Lett. 184:333-338(1985).
RN   [2]
RP   STRUCTURE OF CARBOHYDRATE ON SER-53.
RX   PubMed=2511201;
RA   Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T., Takao T.,
RA   Shimonishi Y., Iwanaga S.;
RT   "Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-
RT   Glc) O-glycosidically linked to a serine residue in the first
RT   epidermal growth factor-like domain of human factors VII and IX and
RT   protein Z and bovine protein Z.";
RL   J. Biol. Chem. 264:20320-20325(1989).
RN   [3]
RP   STRUCTURE OF CARBOHYDRATE ON SER-53.
RX   PubMed=2129367;
RA   Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T.;
RT   "A new trisaccharide sugar chain linked to a serine residue in the
RT   first EGF-like domain of clotting factors VII and IX and protein Z.";
RL   Adv. Exp. Med. Biol. 281:121-131(1990).
CC   -!- FUNCTION: Inhibits activity of the coagulation protease factor Xa
CC       in the presence of SERPINA10, calcium and phospholipids (By
CC       similarity). Appears to assist hemostasis by binding thrombin and
CC       promoting its association with phospholipid vesicles.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000269|PubMed:3888670}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- SIMILARITY: Contains 2 EGF-like domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00076}.
CC   -!- SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00463}.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -!- CAUTION: Although homologous with the vitamin K-dependent clotting
CC       factors, it has lost two of the essential catalytic residues and
CC       has no enzymatic activity. {ECO:0000305}.
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DR   PIR; A22171; KXBOZ.
DR   ProteinModelPortal; P00744; -.
DR   SMR; P00744; 6-46.
DR   MINT; MINT-1504379; -.
DR   STRING; 9913.ENSBTAP00000025894; -.
DR   MEROPS; S01.979; -.
DR   UniCarbKB; P00744; -.
DR   PRIDE; P00744; -.
DR   eggNOG; NOG145536; -.
DR   HOGENOM; HOG000251821; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; P00744; -.
DR   Reactome; REACT_212120; Gamma-carboxylation of protein precursors.
DR   Reactome; REACT_216819; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR   Reactome; REACT_216886; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
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:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.740.10; -; 1.
DR   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR   InterPro; IPR000742; EG-like_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR001254; Peptidase_S1.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR009003; Trypsin-like_Pept_dom.
DR   Pfam; PF00008; EGF; 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; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57630; SSF57630; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 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.
PE   1: Evidence at protein level;
KW   Blood coagulation; Calcium; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydroxylation;
KW   Reference proteome; Repeat; Secreted; Serine protease homolog.
FT   CHAIN         1    396       Vitamin K-dependent protein Z.
FT                                /FTId=PRO_0000088745.
FT   DOMAIN        1     46       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       47     83       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       85    126       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      135    357       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   MOD_RES       7      7       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3888670}.
FT   MOD_RES       8      8       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3888670}.
FT   MOD_RES      11     11       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3888670}.
FT   MOD_RES      15     15       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3888670}.
FT   MOD_RES      17     17       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3888670}.
FT   MOD_RES      20     20       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3888670}.
FT   MOD_RES      21     21       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3888670}.
FT   MOD_RES      26     26       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3888670}.
FT   MOD_RES      27     27       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3888670}.
FT   MOD_RES      30     30       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3888670}.
FT   MOD_RES      33     33       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3888670}.
FT   MOD_RES      36     36       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3888670}.
FT   MOD_RES      40     40       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3888670}.
FT   MOD_RES      64     64       (3R)-3-hydroxyaspartate.
FT                                {ECO:0000269|PubMed:3888670}.
FT   CARBOHYD     53     53       O-linked (Glc...).
FT                                /FTId=CAR_000032.
FT   CARBOHYD     59     59       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:3888670}.
FT   CARBOHYD    191    191       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:3888670}.
FT   CARBOHYD    289    289       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:3888670}.
FT   CARBOHYD    388    388       O-linked (GalNAc...).
FT                                {ECO:0000269|PubMed:3888670}.
FT   DISULFID     18     23       {ECO:0000250}.
FT   DISULFID     51     62       {ECO:0000250}.
FT   DISULFID     56     71       {ECO:0000250}.
FT   DISULFID     73     82       {ECO:0000250}.
FT   DISULFID     89    101       {ECO:0000250}.
FT   DISULFID     97    110       {ECO:0000250}.
FT   DISULFID    112    125       {ECO:0000250}.
FT   DISULFID    169    185       {ECO:0000250}.
FT   DISULFID    284    298       {ECO:0000250}.
SQ   SEQUENCE   396 AA;  43113 MW;  04C5D7A35849B116 CRC64;
     AGSYLLEELF EGHLEKECWE EICVYEEARE VFEDDETTDE FWRTYMGGSP CASQPCLNNG
     SCQDSIRGYA CTCAPGYEGP NCAFAESECH PLRLDGCQHF CYPGPESYTC SCARGHKLGQ
     DRRSCLPHDR CACGTLGPEC CQRPQGSQQN LLPFPWQVKL TNSEGKDFCG GVLIQDNFVL
     TTATCSLLYA NISVKTRSHF RLHVRGVHVH TRFEADTGHN DVALLDLARP VRCPDAGRPV
     CTADADFADS VLLPQPGVLG GWTLRGREMV PLRLRVTHVE PAECGRALNA TVTTRTSCER
     GAAAGAARWV AGGAVVREHR GAWFLTGLLG AAPPEGPGPL LLIKVPRYAL WLRQVTQQPS
     RASPRGDRGQ GRDGEPVPGD RGGRWAPTAL PPGPLV
//
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