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 29-MAY-2013, entry version 121.
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, AND GLYCOSYLATION AT ASN-59; ASN-191; ASN-289 AND
RP THR-388.
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 -!- 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 -!- SIMILARITY: Belongs to the peptidase S1 family.
CC -!- SIMILARITY: Contains 2 EGF-like domains.
CC -!- SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
CC -!- SIMILARITY: Contains 1 peptidase S1 domain.
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.
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DR IPI; IPI00704719; -.
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 GlycoSuiteDB; P00744; -.
DR PRIDE; P00744; -.
DR eggNOG; NOG145536; -.
DR HOGENOM; HOG000251821; -.
DR HOVERGEN; HBG013304; -.
DR InParanoid; P00744; -.
DR OrthoDB; EOG45756N; -.
DR ArrayExpress; P00744; -.
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 GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; Pept_Ser_Cys; 1.
DR SUPFAM; SSF57630; VitK_dep_GLA; 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.
FT DOMAIN 47 83 EGF-like 1.
FT DOMAIN 85 126 EGF-like 2.
FT DOMAIN 135 357 Peptidase S1.
FT MOD_RES 7 7 4-carboxyglutamate.
FT MOD_RES 8 8 4-carboxyglutamate.
FT MOD_RES 11 11 4-carboxyglutamate.
FT MOD_RES 15 15 4-carboxyglutamate.
FT MOD_RES 17 17 4-carboxyglutamate.
FT MOD_RES 20 20 4-carboxyglutamate.
FT MOD_RES 21 21 4-carboxyglutamate.
FT MOD_RES 26 26 4-carboxyglutamate.
FT MOD_RES 27 27 4-carboxyglutamate.
FT MOD_RES 30 30 4-carboxyglutamate.
FT MOD_RES 33 33 4-carboxyglutamate.
FT MOD_RES 36 36 4-carboxyglutamate.
FT MOD_RES 40 40 4-carboxyglutamate.
FT MOD_RES 64 64 (3R)-3-hydroxyaspartate.
FT CARBOHYD 53 53 O-linked (Glc...).
FT /FTId=CAR_000032.
FT CARBOHYD 59 59 N-linked (GlcNAc...).
FT CARBOHYD 191 191 N-linked (GlcNAc...).
FT CARBOHYD 289 289 N-linked (GlcNAc...).
FT CARBOHYD 388 388 O-linked (GalNAc...).
FT DISULFID 18 23 By similarity.
FT DISULFID 51 62 By similarity.
FT DISULFID 56 71 By similarity.
FT DISULFID 73 82 By similarity.
FT DISULFID 89 101 By similarity.
FT DISULFID 97 110 By similarity.
FT DISULFID 112 125 By similarity.
FT DISULFID 169 185 By similarity.
FT DISULFID 284 298 By similarity.
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
//
