(data stored in ACNUC19913 zone)

HOGENOM: BOVIN12_87_PE5

ID   BOVIN12_87_PE5                       STANDARD;      PRT;   439 AA.
AC   BOVIN12_87_PE5; P00744;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Vitamin K-dependent protein Z; (BOVIN12_87.PE5).
GN   Name=PROZ;
OS   BOS TAURUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BOVIN12_87.PE5.
CC       Bos taurus chromosome 12 Btau_4.0 partial sequence 84460455..85358539
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:PROZ_BOVIN
CC   -!- FUNCTION: 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.
CC   -!- GENE_FAMILY: HOG000251821 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Bos_taurus;ENSBTAG00000019440;ENSBTAT00000025894;ENSBTAP00000025894.
DR   UniProtKB/Swiss-Prot; P00744; -.
DR   IPI; IPI00704719; -.
DR   PIR; A22171; KXBOZ.
DR   UniGene; Bt.17776; -.
DR   ProteinModelPortal; P00744; -.
DR   SMR; P00744; 6-46.
DR   STRING; P00744; -.
DR   MEROPS; S01.979; -.
DR   GlycoSuiteDB; P00744; -.
DR   PRIDE; P00744; -.
DR   eggNOG; maNOG12279; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   InParanoid; P00744; -.
DR   OrthoDB; EOG45756N; -.
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   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR009003; Pept_cys/ser_Trypsin-like.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Gene3D; G3DSA:4.10.740.10; Coagulation_factor_Gla; 1.
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.
DR   HOGENOMDNA; BOVIN12_87.PE5; -.
KW   ENSBTAG00000019440fold_1320000031; ENSBTAP00000025894fold_1320000031;
KW   PROZ_BOVIN;
KW   Blood coagulation; Calcium; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hydroxylation;
KW   Reference proteome; Repeat; Secreted; Serine protease homolog.
SQ   SEQUENCE   439 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAGCVPPPLA VLGLLVLLAP HAAWPTVFLP ASKAHELLAR WRRAGSYLLE ELFEGHLEKE
     CWEEICVYEE AREVFEDDET TDEFWRTYMG GSPCASQPCL NNGSCQDSIR GYACTCAPGY
     EGPNCAFAES ECHPLRLDGC QHFCYPGPES YTCSCARGHK LGQDRRSCLP HDRCACGTLG
     PECCQRPQGS QQNLLPFPWQ VKLTNSEGKD FCGGVLIQDN FVLTTATCSL LYANISVKTR
     SHFRLHVRGV HVHTRFEADT GHNDVALLDL ARPVRCPDAG RPVCTADADF ADSVLLPQPG
     VLGGWTLRGR EMVPLRLRVT HVEPAECGRA LNATVTTRTS CERGAAAGAA RWVAGGAVVR
     EHRGAWFLTG LLGAAPPEGP GPLLLIKVPR YALWLRQVTQ QPSRASPRGD RGQGRDGEPV
     PGDRGGRWAP TALPPGPLV
//

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