Protein Z

PROZ
Identifiers
Aliases	PROZ, PZ, Protein Z, protein Z, vitamin K dependent plasma glycoprotein
External IDs	OMIM: 176895; MGI: 1860488; GeneCards: PROZ
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3F1S
Gene location (Human)
Chr.	Chromosome 13 (human)
End	113,172,386 bp
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)
End	13,126,026 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; kidney tubule; ; glomerulus; ; metanephric glomerulus; ; human kidney; ; mucosa of transverse colon; ; right testis; ; cerebellar hemisphere; ; right hemisphere of cerebellum; ; pituitary gland;
	Top expressed in
	liver; ; left lobe of liver; ; yolk sac; ; granulocyte; ; epithelium of small intestine; ; right kidney; ; duodenum; ; dentate gyrus of hippocampal formation granule cell; ; superior frontal gyrus; ; primary visual cortex;
	More reference expression data
	n/a
Gene ontology
Molecular function	calcium ion binding; serine-type endopeptidase activity;
Cellular component	Golgi lumen; extracellular region; endoplasmic reticulum lumen; extracellular exosome; extracellular space;
Biological process	hemostasis; endoplasmic reticulum to Golgi vesicle-mediated transport; peptidyl-glutamic acid carboxylation; signal peptide processing; proteolysis; blood coagulation; negative regulation of blood coagulation;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	8858
	66901
	ENSG00000126231
	ENSMUSG00000031445
	P22891
	Q9CQW3
	NM_001256134; NM_003891
	NM_025834; NM_001357219; NM_001357220
	NP_001243063; NP_003882
	NP_080110; NP_001344148; NP_001344149
	Wikidata
View/Edit Human	View/Edit Mouse

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Protein Z (PZ or PROZ), vitamin K-dependent protein Z, is a protein encoded in the human by the PROZ gene.

Protein Z is a member of the coagulation cascade, the group of blood proteins that leads to the formation of blood clots. It is a glycoprotein. Protein Z functions to inhibit blood coagulation by binding to an inhibitor. It is a GLA domain protein and thus Vitamin K-dependent, and its functionality is therefore impaired in warfarin therapy.