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 24-JAN-2024, entry version 169.
DE RecName: Full=Vitamin K-dependent protein Z;
GN Name=PROZ;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-59; ASN-191; ASN-289 AND THR-388,
RP HYDROXYLATION AT ASP-64, AND GAMMA-CARBOXYGLUTAMATION AT GLU-7; GLU-8;
RP GLU-11; GLU-15; GLU-17; GLU-20; GLU-21; GLU-26; GLU-27; GLU-30; GLU-33;
RP 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 GLYCOSYLATION AT SER-53, AND STRUCTURE OF CARBOHYDRATE ON SER-53.
RX PubMed=2511201; DOI=10.1016/s0021-9258(19)47065-8;
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-Glc)
RT O-glycosidically linked to a serine residue in the first epidermal growth
RT factor-like domain of human factors VII and IX and protein Z and bovine
RT protein Z.";
RL J. Biol. Chem. 264:20320-20325(1989).
RN [3]
RP GLYCOSYLATION AT SER-53, AND STRUCTURE OF CARBOHYDRATE ON SER-53.
RX PubMed=2129367; DOI=10.1007/978-1-4615-3806-6_12;
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 first
RT 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 in
CC the presence of SERPINA10, calcium and phospholipids (By similarity).
CC Appears to assist hemostasis by binding thrombin and promoting its
CC association with phospholipid vesicles. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains.
CC {ECO:0000269|PubMed:3888670}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {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 has no
CC enzymatic activity. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A22171; KXBOZ.
DR AlphaFoldDB; P00744; -.
DR SMR; P00744; -.
DR STRING; 9913.ENSBTAP00000066682; -.
DR MEROPS; S01.979; -.
DR GlyConnect; 622; 1 O-Glc glycan (1 site), 1 O-Linked glycan (1 site).
DR GlyCosmos; P00744; 5 sites, 2 glycans.
DR iPTMnet; P00744; -.
DR PaxDb; 9913-ENSBTAP00000025894; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_19_5_1; -.
DR InParanoid; P00744; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; IPR001314; Peptidase_S1A.
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; PR00722; CHYMOTRYPSIN.
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; 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; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis;
KW Hydroxylation; Reference proteome; Repeat; Secreted;
KW Serine protease homolog.
FT CHAIN 1..396
FT /note="Vitamin K-dependent protein Z"
FT /id="PRO_0000088745"
FT DOMAIN 1..46
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 47..83
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 85..126
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 135..357
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 356..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3888670"
FT MOD_RES 8
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3888670"
FT MOD_RES 11
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3888670"
FT MOD_RES 15
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3888670"
FT MOD_RES 17
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3888670"
FT MOD_RES 20
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3888670"
FT MOD_RES 21
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3888670"
FT MOD_RES 26
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3888670"
FT MOD_RES 27
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3888670"
FT MOD_RES 30
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3888670"
FT MOD_RES 33
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3888670"
FT MOD_RES 36
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3888670"
FT MOD_RES 40
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:3888670"
FT MOD_RES 64
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000269|PubMed:3888670"
FT CARBOHYD 53
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:2129367,
FT ECO:0000269|PubMed:2511201"
FT /id="CAR_000032"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3888670"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3888670"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3888670"
FT CARBOHYD 388
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:3888670"
FT DISULFID 18..23
FT /evidence="ECO:0000250"
FT DISULFID 51..62
FT /evidence="ECO:0000250"
FT DISULFID 56..71
FT /evidence="ECO:0000250"
FT DISULFID 73..82
FT /evidence="ECO:0000250"
FT DISULFID 89..101
FT /evidence="ECO:0000250"
FT DISULFID 97..110
FT /evidence="ECO:0000250"
FT DISULFID 112..125
FT /evidence="ECO:0000250"
FT DISULFID 169..185
FT /evidence="ECO:0000250"
FT DISULFID 284..298
FT /evidence="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
//
