PGRMC1

PGRMC1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPGRMC1, HPR6.6, MPR, progesterone receptor membrane component 1, Dap1, IZA, 25-Dx
External IDsOMIM: 300435; MGI: 1858305; HomoloGene: 48457; GeneCards: PGRMC1; OMA:PGRMC1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_006667
NM_001282621

NM_016783

RefSeq (protein)

NP_001269550
NP_006658
NP_006658.1

NP_058063

Location (UCSC)Chr X: 119.24 – 119.24 MbChr X: 35.86 – 35.87 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101856Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000006373Ensembl, 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.
  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.
  6. ^ 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.
  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.
  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.
  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.
  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.
  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.
  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.
  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.
  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.
  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.