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Protein

Vitamin K-dependent protein Z

Gene

Proz

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

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

GO - Molecular functioni

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

GO - Biological processi

  • blood coagulation Source: MGI
  • negative regulation of blood coagulation Source: GO_Central

Keywordsi

Molecular functionSerine protease homolog
Biological processBlood coagulation, Hemostasis
LigandCalcium

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1860488 Proz

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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...) asparagineSequence 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...) asparagine1 Publication1
Glycosylationi305N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi326 ↔ 340By similarity
Glycosylationi331N-linked (GlcNAc...) asparagineSequence 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

iPTMnetiQ9CQW3
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

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
InterProiView protein in InterPro
IPR017857 Coagulation_fac-like_Gla_dom
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR035972 GLA-like_dom_SF
IPR000294 GLA_domain
IPR012224 Pept_S1A_FX
IPR009003 Peptidase_S1_PA
IPR001254 Trypsin_dom
PfamiView protein in Pfam
PF00008 EGF, 1 hit
PF00594 Gla, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001143 Factor_X, 1 hit
PRINTSiPR00001 GLABLOOD
SMARTiView protein in SMART
SM00181 EGF, 2 hits
SM00179 EGF_CA, 2 hits
SM00069 GLA, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57630 SSF57630, 1 hit
PROSITEiView protein in PROSITE
PS00010 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

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

Similar proteinsi

Entry informationi

Entry nameiPROZ_MOUSE
AccessioniPrimary (citable) accession number: Q9CQW3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2001
Last modified: March 28, 2018
This is version 132 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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
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Main funding by: National Institutes of Health