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Protein

Vitamin K-dependent protein Z

Gene

PROZ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Appears to assist hemostasis by binding thrombin and promoting its association with phospholipid vesicles. Inhibits activity of the coagulation protease factor Xa in the presence of SERPINA10, calcium and phospholipids.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Serine protease homolog

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciZFISH:ENSG00000126231-MONOMER.
ReactomeiR-HSA-159740. Gamma-carboxylation of protein precursors.
R-HSA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-HSA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

Protein family/group databases

MEROPSiS01.979.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin K-dependent protein Z
Gene namesi
Name:PROZ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:9460. PROZ.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi8858.
MalaCardsiPROZ.
OpenTargetsiENSG00000126231.
Orphaneti329217. Cerebral sinovenous thrombosis.
PharmGKBiPA33813.

Chemistry databases

DrugBankiDB00170. Menadione.

Polymorphism and mutation databases

BioMutaiPROZ.
DMDMi131092.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Add BLAST23
PropeptideiPRO_000002848824 – 40Add BLAST17
ChainiPRO_000002848941 – 400Vitamin K-dependent protein Z1 PublicationAdd BLAST360

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei474-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei484-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei514-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei554-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei574-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi58 ↔ 63By similarity
Modified residuei604-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei614-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei664-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei674-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei704-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei734-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei754-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei804-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi91 ↔ 102
Glycosylationi93O-linked (Glc...)1
Disulfide bondi96 ↔ 111
Glycosylationi99N-linked (GlcNAc...)1 Publication1
Modified residuei104(3R)-3-hydroxyaspartateBy similarity1
Disulfide bondi113 ↔ 122
Disulfide bondi129 ↔ 141
Disulfide bondi137 ↔ 150
Disulfide bondi152 ↔ 165
Disulfide bondi203 ↔ 219
Glycosylationi225N-linked (GlcNAc...)1 Publication1
Glycosylationi233N-linked (GlcNAc...)2 Publications1
Glycosylationi306N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi327 ↔ 341
Glycosylationi332N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP22891.
PeptideAtlasiP22891.
PRIDEiP22891.

PTM databases

iPTMnetiP22891.
PhosphoSitePlusiP22891.
UniCarbKBiP22891.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiENSG00000126231.
CleanExiHS_PROZ.
GenevisibleiP22891. HS.

Organism-specific databases

HPAiHPA052006.

Interactioni

Subunit structurei

Interacts with SERPINA10.2 Publications

Protein-protein interaction databases

BioGridi114382. 31 interactors.
IntActiP22891. 1 interactor.
STRINGi9606.ENSP00000364697.

Structurei

Secondary structure

1400
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni97 – 99Combined sources3
Beta strandi106 – 108Combined sources3
Beta strandi114 – 116Combined sources3
Beta strandi119 – 122Combined sources4
Beta strandi126 – 128Combined sources3
Beta strandi134 – 136Combined sources3
Beta strandi138 – 140Combined sources3
Beta strandi145 – 147Combined sources3
Beta strandi149 – 151Combined sources3
Beta strandi156 – 158Combined sources3
Beta strandi165 – 167Combined sources3
Beta strandi191 – 195Combined sources5
Beta strandi197 – 199Combined sources3
Beta strandi201 – 209Combined sources9
Beta strandi212 – 215Combined sources4
Helixi217 – 220Combined sources4
Beta strandi227 – 230Combined sources4
Beta strandi240 – 249Combined sources10
Turni255 – 258Combined sources4
Beta strandi263 – 269Combined sources7
Turni273 – 276Combined sources4
Helixi285 – 290Combined sources6
Turni291 – 295Combined sources5
Beta strandi298 – 302Combined sources5
Beta strandi309 – 311Combined sources3
Beta strandi315 – 322Combined sources8
Helixi324 – 331Combined sources8
Beta strandi339 – 343Combined sources5
Helixi348 – 350Combined sources3
Beta strandi356 – 360Combined sources5
Beta strandi365 – 371Combined sources7
Helixi376 – 378Combined sources3
Beta strandi380 – 387Combined sources8
Helixi388 – 391Combined sources4
Helixi392 – 399Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3F1SX-ray2.30B125-400[»]
3H5CX-ray3.26B84-400[»]
ProteinModelPortaliP22891.
SMRiP22891.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22891.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 86GlaPROSITE-ProRule annotationAdd BLAST46
Domaini87 – 123EGF-like 1PROSITE-ProRule annotationAdd BLAST37
Domaini125 – 166EGF-like 2PROSITE-ProRule annotationAdd BLAST42
Domaini175 – 400Peptidase S1PROSITE-ProRule annotationAdd BLAST226

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP22891.
OMAiWFLTGIL.
OrthoDBiEOG091G06UA.
PhylomeDBiP22891.
TreeFamiTF327329.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001254. Trypsin_dom.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P22891-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGCVPLLQG LVLVLALHRV EPSVFLPASK ANDVLVRWKR AGSYLLEELF
60 70 80 90 100
EGNLEKECYE EICVYEEARE VFENEVVTDE FWRRYKGGSP CISQPCLHNG
110 120 130 140 150
SCQDSIWGYT CTCSPGYEGS NCELAKNECH PERTDGCQHF CLPGQESYTC
160 170 180 190 200
SCAQGYRLGE DHKQCVPHDQ CACGVLTSEK RAPDLQDLPW QVKLTNSEGK
210 220 230 240 250
DFCGGVIIRE NFVLTTAKCS LLHRNITVKT YFNRTSQDPL MIKITHVHVH
260 270 280 290 300
MRYDADAGEN DLSLLELEWP IQCPGAGLPV CTPEKDFAEH LLIPRTRGLL
310 320 330 340 350
SGWARNGTDL GNSLTTRPVT LVEGEECGQV LNVTVTTRTY CERSSVAAMH
360 370 380 390 400
WMDGSVVTRE HRGSWFLTGV LGSQPVGGQA HMVLVTKVSR YSLWFKQIMN
Length:400
Mass (Da):44,744
Last modified:November 1, 1991 - v2
Checksum:i7EBD2DCC48860268
GO
Isoform 2 (identifier: P22891-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     24-24: V → ATSLKERHGLHSDSACTGVQESL

Show »
Length:422
Mass (Da):47,053
Checksum:iB8824CE1ECAEEEAE
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01312470E → K.1 PublicationCorresponds to variant rs3024778dbSNPEnsembl.1
Natural variantiVAR_013125295R → H.1 PublicationCorresponds to variant rs3024772dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00541524V → ATSLKERHGLHSDSACTGVQ ESL in isoform 2. Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55670 mRNA. Translation: AAA36500.1.
M55671 mRNA. Translation: AAA36501.1.
AB033749 Genomic DNA. Translation: BAA85763.1.
AB033749 Genomic DNA. Translation: BAA85764.1.
AF440358 Genomic DNA. Translation: AAL27631.1.
EF445049 Genomic DNA. Translation: ACA06105.1.
AL137002 Genomic DNA. Translation: CAI41389.1.
AL137002 Genomic DNA. Translation: CAI41388.1.
CH471085 Genomic DNA. Translation: EAX09186.1.
CH471085 Genomic DNA. Translation: EAX09187.1.
BC074906 mRNA. Translation: AAH74906.1.
BC074907 mRNA. Translation: AAH74907.1.
M59303 mRNA. Translation: AAA36499.1.
CCDSiCCDS58300.1. [P22891-2]
CCDS9531.1. [P22891-1]
PIRiA36244. KXHUZ.
RefSeqiNP_001243063.1. NM_001256134.1. [P22891-2]
NP_003882.1. NM_003891.2. [P22891-1]
UniGeneiHs.1011.

Genome annotation databases

EnsembliENST00000342783; ENSP00000344458; ENSG00000126231. [P22891-2]
ENST00000375547; ENSP00000364697; ENSG00000126231. [P22891-1]
GeneIDi8858.
KEGGihsa:8858.
UCSCiuc001vta.3. human. [P22891-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55670 mRNA. Translation: AAA36500.1.
M55671 mRNA. Translation: AAA36501.1.
AB033749 Genomic DNA. Translation: BAA85763.1.
AB033749 Genomic DNA. Translation: BAA85764.1.
AF440358 Genomic DNA. Translation: AAL27631.1.
EF445049 Genomic DNA. Translation: ACA06105.1.
AL137002 Genomic DNA. Translation: CAI41389.1.
AL137002 Genomic DNA. Translation: CAI41388.1.
CH471085 Genomic DNA. Translation: EAX09186.1.
CH471085 Genomic DNA. Translation: EAX09187.1.
BC074906 mRNA. Translation: AAH74906.1.
BC074907 mRNA. Translation: AAH74907.1.
M59303 mRNA. Translation: AAA36499.1.
CCDSiCCDS58300.1. [P22891-2]
CCDS9531.1. [P22891-1]
PIRiA36244. KXHUZ.
RefSeqiNP_001243063.1. NM_001256134.1. [P22891-2]
NP_003882.1. NM_003891.2. [P22891-1]
UniGeneiHs.1011.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3F1SX-ray2.30B125-400[»]
3H5CX-ray3.26B84-400[»]
ProteinModelPortaliP22891.
SMRiP22891.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114382. 31 interactors.
IntActiP22891. 1 interactor.
STRINGi9606.ENSP00000364697.

Chemistry databases

DrugBankiDB00170. Menadione.

Protein family/group databases

MEROPSiS01.979.

PTM databases

iPTMnetiP22891.
PhosphoSitePlusiP22891.
UniCarbKBiP22891.

Polymorphism and mutation databases

BioMutaiPROZ.
DMDMi131092.

Proteomic databases

PaxDbiP22891.
PeptideAtlasiP22891.
PRIDEiP22891.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342783; ENSP00000344458; ENSG00000126231. [P22891-2]
ENST00000375547; ENSP00000364697; ENSG00000126231. [P22891-1]
GeneIDi8858.
KEGGihsa:8858.
UCSCiuc001vta.3. human. [P22891-1]

Organism-specific databases

CTDi8858.
DisGeNETi8858.
GeneCardsiPROZ.
H-InvDBHIX0037352.
HGNCiHGNC:9460. PROZ.
HPAiHPA052006.
MalaCardsiPROZ.
MIMi176895. gene.
neXtProtiNX_P22891.
OpenTargetsiENSG00000126231.
Orphaneti329217. Cerebral sinovenous thrombosis.
PharmGKBiPA33813.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP22891.
OMAiWFLTGIL.
OrthoDBiEOG091G06UA.
PhylomeDBiP22891.
TreeFamiTF327329.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000126231-MONOMER.
ReactomeiR-HSA-159740. Gamma-carboxylation of protein precursors.
R-HSA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-HSA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

Miscellaneous databases

EvolutionaryTraceiP22891.
GenomeRNAii8858.
PROiP22891.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000126231.
CleanExiHS_PROZ.
GenevisibleiP22891. HS.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001254. Trypsin_dom.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPROZ_HUMAN
AccessioniPrimary (citable) accession number: P22891
Secondary accession number(s): A6NMB4
, Q15213, Q5JVF5, Q5JVF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1991
Last modified: November 30, 2016
This is version 182 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Although related to peptidase S1 family vitamin K-dependent clotting factors, it has lost two of the essential catalytic residues and therefore lacks protease activity.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.