PGRMC1

PGRMC1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4X8Y
Identifiers
Aliases	PGRMC1, HPR6.6, MPR, progesterone receptor membrane component 1, Dap1, IZA, 25-Dx
External IDs	OMIM: 300435; MGI: 1858305; HomoloGene: 48457; GeneCards: PGRMC1; OMA:PGRMC1 - orthologs
Gene location (Human)
Chr.	X chromosome (human)
End	119,244,466 bp
Gene location (Mouse)
Chr.	X chromosome (mouse)
End	35,869,732 bp
RNA expression pattern
	Top expressed in
	seminal vesicula; ; caput epididymis; ; corpus epididymis; ; tail of epididymis; ; bronchial epithelial cell; ; pons; ; endometrium; ; skin of thigh; ; middle temporal gyrus; ; Pars compacta;
	Top expressed in
	olfactory epithelium; ; transitional epithelium of urinary bladder; ; paraventricular nucleus of hypothalamus; ; arcuate nucleus; ; ventromedial nucleus; ; suprachiasmatic nucleus; ; anterior amygdaloid area; ; lateral septal nucleus; ; left lobe of liver; ; dorsomedial hypothalamic nucleus;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	steroid binding; protein binding; heme binding; lipid binding; amyloid-beta binding;
Cellular component	organelle membrane; integral component of membrane; extracellular exosome; endoplasmic reticulum membrane; endomembrane system; membrane; intracellular membrane-bounded organelle; endoplasmic reticulum; plasma membrane; specific granule membrane; integral component of plasma membrane; smooth endoplasmic reticulum membrane; neuron projection; neuronal cell body; cell body; synapse;
Biological process	neutrophil degranulation;
	Sources:Amigo / QuickGO
Orthologs
	10857
	53328
	ENSG00000101856
	ENSMUSG00000006373
	O00264; Q6IB11
	O55022
	NM_006667; NM_001282621
	NM_016783
	NP_001269550; NP_006658; NP_006658.1
	NP_058063
	Wikidata
View/Edit Human	View/Edit Mouse

Progesterone receptor membrane component 1 (abbreviated PGRMC1) is a protein which co-purifies with progesterone binding proteins in the liver and ovary.^[5]^[6] In humans, the PGRMC1 protein is encoded by the PGRMC1 gene.^[7]

The sole biochemical function of PGRMC1 is heme-binding.^[8]^[9] PGRMC1 shares key structural motifs with cytochrome b₅.^[10] PGRMC1 binds and activates P450 proteins,^[11]^[12]^[13] which are important in drug, hormone and lipid metabolism. PGRMC1 also binds to PAIR-BP1 (plasminogen activator inhibitor RNA-binding protein-1).^[6] However, its expression outside of the reproductive tract and in males suggests multiple functions for the protein. These may include binding to Insig (insulin-induced gene),^[14] which regulates cholesterol synthesis.^[15]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000101856 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000006373 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Meyer C, Schmid R, Scriba PC, Wehling M (Aug 1996). "Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes". European Journal of Biochemistry. 239 (3): 726–31. doi:10.1111/j.1432-1033.1996.0726u.x. PMID 8774719.
^ ^a ^b Peluso JJ, Romak J, Liu X (Feb 2008). "Progesterone receptor membrane component-1 (PGRMC1) is the mediator of progesterone's antiapoptotic action in spontaneously immortalized granulosa cells as revealed by PGRMC1 small interfering ribonucleic acid treatment and functional analysis of PGRMC1 mutations". Endocrinology. 149 (2): 534–43. doi:10.1210/en.2007-1050. PMC 2219306. PMID 17991724.
^ Gerdes D, Wehling M, Leube B, Falkenstein E (Jul 1998). "Cloning and tissue expression of two putative steroid membrane receptors". Biological Chemistry. 379 (7): 907–11. doi:10.1515/bchm.1998.379.7.907. PMID 9705155.
^ Crudden G, Chitti RE, Craven RJ (Jan 2006). "Hpr6 (heme-1 domain protein) regulates the susceptibility of cancer cells to chemotherapeutic drugs". The Journal of Pharmacology and Experimental Therapeutics. 316 (1): 448–55. doi:10.1124/jpet.105.094631. PMID 16234411. S2CID 18928996.
^ Ghosh K, Thompson AM, Goldbeck RA, Shi X, Whitman S, Oh E, Zhiwu Z, Vulpe C, Holman TR (Dec 2005). "Spectroscopic and biochemical characterization of heme binding to yeast Dap1p and mouse PGRMC1p". Biochemistry. 44 (50): 16729–36. doi:10.1021/bi0511585. PMC 2577039. PMID 16342963.
^ Mifsud W, Bateman A (2002). "Membrane-bound progesterone receptors contain a cytochrome b5-like ligand-binding domain". Genome Biology. 3 (12): RESEARCH0068. doi:10.1186/gb-2002-3-12-research0068. PMC 151170. PMID 12537557.
^ Hughes AL, Powell DW, Bard M, Eckstein J, Barbuch R, Link AJ, Espenshade PJ (Feb 2007). "Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes". Cell Metabolism. 5 (2): 143–9. doi:10.1016/j.cmet.2006.12.009. PMID 17276356.
^ Min L, Strushkevich NV, Harnastai IN, Iwamoto H, Gilep AA, Takemori H, Usanov SA, Nonaka Y, Hori H, Vinson GP, Okamoto M (Nov 2005). "Molecular identification of adrenal inner zone antigen as a heme-binding protein". The FEBS Journal. 272 (22): 5832–43. doi:10.1111/j.1742-4658.2005.04977.x. PMID 16279947.
^ Min L, Takemori H, Nonaka Y, Katoh Y, Doi J, Horike N, Osamu H, Raza FS, Vinson GP, Okamoto M (Feb 2004). "Characterization of the adrenal-specific antigen IZA (inner zone antigen) and its role in the steroidogenesis". Molecular and Cellular Endocrinology. 215 (1–2): 143–8. doi:10.1016/j.mce.2003.11.025. PMID 15026187. S2CID 20640748.
^ Suchanek M, Radzikowska A, Thiele C (Apr 2005). "Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells". Nature Methods. 2 (4): 261–7. doi:10.1038/nmeth752. PMID 15782218.
^ Yang T, Espenshade PJ, Wright ME, Yabe D, Gong Y, Aebersold R, Goldstein JL, Brown MS (Aug 2002). "Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER". Cell. 110 (4): 489–500. doi:10.1016/S0092-8674(02)00872-3. PMID 12202038.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000101856 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000006373 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8774719-5] Meyer C, Schmid R, Scriba PC, Wehling M (Aug 1996). "Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes". European Journal of Biochemistry. 239 (3): 726–31. doi:10.1111/j.1432-1033.1996.0726u.x. PMID 8774719.

[peluso2008b-6] Peluso JJ, Romak J, Liu X (Feb 2008). "Progesterone receptor membrane component-1 (PGRMC1) is the mediator of progesterone's antiapoptotic action in spontaneously immortalized granulosa cells as revealed by PGRMC1 small interfering ribonucleic acid treatment and functional analysis of PGRMC1 mutations". Endocrinology. 149 (2): 534–43. doi:10.1210/en.2007-1050. PMC 2219306. PMID 17991724.

[pmid9705155-7] Gerdes D, Wehling M, Leube B, Falkenstein E (Jul 1998). "Cloning and tissue expression of two putative steroid membrane receptors". Biological Chemistry. 379 (7): 907–11. doi:10.1515/bchm.1998.379.7.907. PMID 9705155.

[crudden2006-8] Crudden G, Chitti RE, Craven RJ (Jan 2006). "Hpr6 (heme-1 domain protein) regulates the susceptibility of cancer cells to chemotherapeutic drugs". The Journal of Pharmacology and Experimental Therapeutics. 316 (1): 448–55. doi:10.1124/jpet.105.094631. PMID 16234411. S2CID 18928996.

[ghosh2005-9] Ghosh K, Thompson AM, Goldbeck RA, Shi X, Whitman S, Oh E, Zhiwu Z, Vulpe C, Holman TR (Dec 2005). "Spectroscopic and biochemical characterization of heme binding to yeast Dap1p and mouse PGRMC1p". Biochemistry. 44 (50): 16729–36. doi:10.1021/bi0511585. PMC 2577039. PMID 16342963.

[pmid12537557-10] Mifsud W, Bateman A (2002). "Membrane-bound progesterone receptors contain a cytochrome b5-like ligand-binding domain". Genome Biology. 3 (12): RESEARCH0068. doi:10.1186/gb-2002-3-12-research0068. PMC 151170. PMID 12537557.

[hughes2007-11] Hughes AL, Powell DW, Bard M, Eckstein J, Barbuch R, Link AJ, Espenshade PJ (Feb 2007). "Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes". Cell Metabolism. 5 (2): 143–9. doi:10.1016/j.cmet.2006.12.009. PMID 17276356.

[pmid16279947-12] Min L, Strushkevich NV, Harnastai IN, Iwamoto H, Gilep AA, Takemori H, Usanov SA, Nonaka Y, Hori H, Vinson GP, Okamoto M (Nov 2005). "Molecular identification of adrenal inner zone antigen as a heme-binding protein". The FEBS Journal. 272 (22): 5832–43. doi:10.1111/j.1742-4658.2005.04977.x. PMID 16279947.

[min2004-13] Min L, Takemori H, Nonaka Y, Katoh Y, Doi J, Horike N, Osamu H, Raza FS, Vinson GP, Okamoto M (Feb 2004). "Characterization of the adrenal-specific antigen IZA (inner zone antigen) and its role in the steroidogenesis". Molecular and Cellular Endocrinology. 215 (1–2): 143–8. doi:10.1016/j.mce.2003.11.025. PMID 15026187. S2CID 20640748.

[pmid15782218-14] Suchanek M, Radzikowska A, Thiele C (Apr 2005). "Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells". Nature Methods. 2 (4): 261–7. doi:10.1038/nmeth752. PMID 15782218.

[pmid12202038-15] Yang T, Espenshade PJ, Wright ME, Yabe D, Gong Y, Aebersold R, Goldstein JL, Brown MS (Aug 2002). "Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER". Cell. 110 (4): 489–500. doi:10.1016/S0092-8674(02)00872-3. PMID 12202038.

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