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Protein

Vitamin K-dependent protein Z

Gene

Proz

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

GO - Molecular functioni

  • calcium ion binding Source: MGI
  • serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  • blood coagulation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Serine protease homolog

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

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

Protein family/group databases

MEROPSiS01.996.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin K-dependent protein Z
Gene namesi
Name:Proz
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1860488. Proz.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • extracellular region Source: MGI
  • extracellular space Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000002849023 – 40By similarityAdd BLAST18
ChainiPRO_000002849141 – 399Vitamin K-dependent protein ZAdd BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei474-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei484-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei554-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei574-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi58 ↔ 63By similarity
Modified residuei604-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei614-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei664-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei674-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei704-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei734-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei804-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi91 ↔ 102By similarity
Disulfide bondi96 ↔ 111By similarity
Glycosylationi99N-linked (GlcNAc...)Sequence analysis1
Modified residuei104(3R)-3-hydroxyaspartateBy similarity1
Disulfide bondi113 ↔ 122By similarity
Disulfide bondi129 ↔ 141By similarity
Disulfide bondi137 ↔ 150By similarity
Disulfide bondi152 ↔ 165By similarity
Disulfide bondi208 ↔ 224By similarity
Glycosylationi230N-linked (GlcNAc...)1 Publication1
Glycosylationi305N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi326 ↔ 340By similarity
Glycosylationi331N-linked (GlcNAc...)Sequence analysis1

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

MaxQBiQ9CQW3.
PaxDbiQ9CQW3.
PRIDEiQ9CQW3.

PTM databases

PhosphoSitePlusiQ9CQW3.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiENSMUSG00000031445.
ExpressionAtlasiQ9CQW3. baseline and differential.
GenevisibleiQ9CQW3. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033822.

Structurei

3D structure databases

ProteinModelPortaliQ9CQW3.
SMRiQ9CQW3.
ModBaseiSearch...
MobiDBiSearch...

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
Domaini172 – 399Peptidase S1PROSITE-ProRule annotationAdd BLAST228

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.
InParanoidiQ9CQW3.
OMAiWFLTGIL.
OrthoDBiEOG091G06UA.
PhylomeDBiQ9CQW3.
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]

Sequencei

Sequence statusi: Complete.

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

Q9CQW3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGCILLLRG FILTLILHQV ELSVFLPAPK ANNVLRRWRR GSSYFLEEIF
60 70 80 90 100
QGNLEKECYE EVCNYEEARE VFENDVITDE FWRQYGGGSP CVSQPCLNNG
110 120 130 140 150
TCEDHIRSYS CTCSPGYEGK TCAMAKNECH LERTDGCQHF CHPGQSSYMC
160 170 180 190 200
SCAKGYKLGK DQKSCGPSDK CACGALTSEH IRMTKSSQSQ PSFPWQVRLT
210 220 230 240 250
NSEGEDFCAG VLLQEDFVLT TAKCSLLHSN ISVKANVDQR IRIKSTHVHM
260 270 280 290 300
RYDEESGEND VSLLQLEEPL QCPSSGLPVC VPERDFAEHV LIPGTEGLLS
310 320 330 340 350
GWMLNGTHLA TTPMLLSVTQ ADGEECGQTL NVTVTTRTSC EKGSVVMGPW
360 370 380 390
VEGSVVTREH KGTWFLTGIL GSPPPPGQSQ MLLLTAVPRY SMWFKQIMK
Length:399
Mass (Da):44,304
Last modified:June 1, 2001 - v1
Checksum:i4FC85C9598F27E03
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005011 mRNA. No translation available.
AK008819 mRNA. Translation: BAB25912.1.
CCDSiCCDS22105.1.
RefSeqiNP_080110.1. NM_025834.3.
UniGeneiMm.441140.

Genome annotation databases

EnsembliENSMUST00000033822; ENSMUSP00000033822; ENSMUSG00000031445.
GeneIDi66901.
KEGGimmu:66901.
UCSCiuc009kwu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005011 mRNA. No translation available.
AK008819 mRNA. Translation: BAB25912.1.
CCDSiCCDS22105.1.
RefSeqiNP_080110.1. NM_025834.3.
UniGeneiMm.441140.

3D structure databases

ProteinModelPortaliQ9CQW3.
SMRiQ9CQW3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033822.

Protein family/group databases

MEROPSiS01.996.

PTM databases

PhosphoSitePlusiQ9CQW3.

Proteomic databases

MaxQBiQ9CQW3.
PaxDbiQ9CQW3.
PRIDEiQ9CQW3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033822; ENSMUSP00000033822; ENSMUSG00000031445.
GeneIDi66901.
KEGGimmu:66901.
UCSCiuc009kwu.1. mouse.

Organism-specific databases

CTDi8858.
MGIiMGI:1860488. Proz.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiQ9CQW3.
OMAiWFLTGIL.
OrthoDBiEOG091G06UA.
PhylomeDBiQ9CQW3.
TreeFamiTF327329.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ9CQW3.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031445.
ExpressionAtlasiQ9CQW3. baseline and differential.
GenevisibleiQ9CQW3. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: Q9CQW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Although homologous with the vitamin K-dependent clotting factors, it has lost two of the essential catalytic residues and has no enzymatic activity.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.