(data stored in ACNUC19913 zone)

HOGENOM: HS13_PE1084

ID   HS13_PE1084                          STANDARD;      PRT;   400 AA.
AC   HS13_PE1084; P22891; A6NMB4; Q15213; Q5JVF5; Q5JVF6;
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;Flags: Precursor;
DE   (HS13.PE1084).
GN   Name=PROZ;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS13.PE1084.
CC       Homo sapiens chromosome 13 GRCh37  sequence 1..115109878 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:PROZ_HUMAN
CC   -!- FUNCTION: Appears to assist hemostasis by binding thrombin and
CC       promoting its association with phospholipid vesicles.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P22891-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P22891-2; Sequence=VSP_005415;
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       (By similarity).
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   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/proz/";
CC   -!- GENE_FAMILY: HOG000251821 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000126231;ENST00000375547;ENSP00000364697.
DR   EMBL; AB033749; - ;
DR   EMBL; AF440358; - ;
DR   EMBL; AL137002; - ;
DR   EMBL; BC074906; - ;
DR   EMBL; BC074907; - ;
DR   EMBL; CH471085; - ;
DR   EMBL; EF445049; - ;
DR   EMBL; M55670; - ;
DR   EMBL; M55671; - ;
DR   EMBL; M59303; - ;
DR   UniProtKB/Swiss-Prot; P22891; A6NMB4; Q15213; Q5JVF5; Q5JVF6; -.
DR   EMBL; M55670; AAA36500.1; -; mRNA.
DR   EMBL; M55671; AAA36501.1; -; mRNA.
DR   EMBL; AB033749; BAA85763.1; -; Genomic_DNA.
DR   EMBL; AB033749; BAA85764.1; -; Genomic_DNA.
DR   EMBL; AF440358; AAL27631.1; -; Genomic_DNA.
DR   EMBL; EF445049; ACA06105.1; -; Genomic_DNA.
DR   EMBL; AL137002; CAI41389.1; -; Genomic_DNA.
DR   EMBL; AL137002; CAI41388.1; -; Genomic_DNA.
DR   EMBL; CH471085; EAX09186.1; -; Genomic_DNA.
DR   EMBL; CH471085; EAX09187.1; -; Genomic_DNA.
DR   EMBL; BC074906; AAH74906.1; -; mRNA.
DR   EMBL; BC074907; AAH74907.1; -; mRNA.
DR   EMBL; M59303; AAA36499.1; -; mRNA.
DR   IPI; IPI00027843; -.
DR   IPI; IPI00216065; -.
DR   PIR; A36244; KXHUZ.
DR   RefSeq; NP_003882.1; NM_003891.1.
DR   UniGene; Hs.1011; -.
DR   PDB; 3F1S; X-ray; 2.30 A; B=125-400.
DR   PDB; 3H5C; X-ray; 3.26 A; B=84-400.
DR   PDBsum; 3F1S; -.
DR   PDBsum; 3H5C; -.
DR   ProteinModelPortal; P22891; -.
DR   SMR; P22891; 46-85, 89-400.
DR   STRING; P22891; -.
DR   MEROPS; S01.979; -.
DR   GlycoSuiteDB; P22891; -.
DR   PRIDE; P22891; -.
DR   Ensembl; ENST00000375547; ENSP00000364697; ENSG00000126231.
DR   GeneID; 8858; -.
DR   KEGG; hsa:8858; -.
DR   UCSC; uc001vta.1; human.
DR   UCSC; uc010agr.1; human.
DR   CTD; 8858; -.
DR   GeneCards; GC13P094251; -.
DR   H-InvDB; HIX0037352; -.
DR   HGNC; HGNC:9460; PROZ.
DR   HPA; HPA016503; -.
DR   MIM; 176895; gene.
DR   neXtProt; NX_P22891; -.
DR   PharmGKB; PA33813; -.
DR   eggNOG; prNOG08674; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   OMA; WFLTGIL; -.
DR   OrthoDB; EOG45756N; -.
DR   Reactome; REACT_17015; Metabolism of proteins.
DR   DrugBank; DB00170; Menadione.
DR   NextBio; 33263; -.
DR   ArrayExpress; P22891; -.
DR   Bgee; P22891; -.
DR   CleanEx; HS_PROZ; -.
DR   Genevestigator; P22891; -.
DR   GermOnline; ENSG00000126231; Homo sapiens.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
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:0017187; P:peptidyl-glutamic acid carboxylation; TAS:Reactome.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0006508; P:proteolysis; TAS:Reactome.
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   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; 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; 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.
DR   HOGENOMDNA; HS13.PE1084; -.
KW   ENSG000001262311755old_1320000031; ENSP000003646977901old_1320000031;
KW   AB033749; AF440358; AL137002; BC074906; BC074907; CH471085; EF445049;
KW   M55671; M59303;
KW   3D-structure; Alternative splicing; Blood coagulation; Calcium;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hydroxylation; Polymorphism;
KW   Reference proteome; Repeat; Secreted; Serine protease homolog; Signal.
SQ   SEQUENCE   400 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAGCVPLLQG LVLVLALHRV EPSVFLPASK ANDVLVRWKR AGSYLLEELF EGNLEKECYE
     EICVYEEARE VFENEVVTDE FWRRYKGGSP CISQPCLHNG SCQDSIWGYT CTCSPGYEGS
     NCELAKNECH PERTDGCQHF CLPGQESYTC SCAQGYRLGE DHKQCVPHDQ CACGVLTSEK
     RAPDLQDLPW QVKLTNSEGK DFCGGVIIRE NFVLTTAKCS LLHRNITVKT YFNRTSQDPL
     MIKITHVHVH MRYDADAGEN DLSLLELEWP IQCPGAGLPV CTPEKDFAEH LLIPRTRGLL
     SGWARNGTDL GNSLTTRPVT LVEGEECGQV LNVTVTTRTY CERSSVAAMH WMDGSVVTRE
     HRGSWFLTGV LGSQPVGGQA HMVLVTKVSR YSLWFKQIMN
//

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