O00264 (PGRC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Membrane-associated progesterone receptor component 1
Short name=mPR

Gene names

Name:	PGRMC1
Synonyms:	HPR6.6, PGRMC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	195 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for progesterone By similarity.
Subcellular location	Microsome membrane; Single-pass membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass membrane protein By similarity.
Tissue specificity	Widely expressed, with highest expression in liver and kidney.
Domain	The cytochrome b5 heme-binding domain lacks the conserved iron-binding His residues at positions 107 and 131 By similarity.
Sequence similarities	Belongs to the cytochrome b5 family. MAPR subfamily. Contains 1 cytochrome b5 heme-binding domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane Transmembrane helix
Ligand	Lipid-binding Steroid-binding
Molecular function	Receptor
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Inferred from electronic annotation. Source: Compara
Cellular_component	cell surface Inferred from direct assay PubMed 12493773. Source: UniProtKB endoplasmic reticulum Inferred from direct assay. Source: HPA endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleolus Inferred from direct assay. Source: HPA
Molecular_function	heme binding Inferred from electronic annotation. Source: InterPro steroid binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CYP2C2	P00181	6	EBI-1045534,EBI-4320576	From a different organism.
POR	P16435	5	EBI-1045534,EBI-726554

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 195	194	Membrane-associated progesterone receptor component 1		PRO_0000121739
Regions
	Topological domain	2 – 24	23	Lumenal Potential
	Transmembrane	25 – 43	19	Helical; Potential
	Topological domain	44 – 195	152	Cytoplasmic Potential
	Domain	72 – 171	100	Cytochrome b5 heme-binding
Amino acid modifications
	Modified residue	54	1	Phosphoserine Ref.10
	Modified residue	57	1	Phosphoserine Ref.5 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17
	Modified residue	178	1	Phosphothreonine By similarity
	Modified residue	180	1	Phosphotyrosine By similarity
	Modified residue	181	1	Phosphoserine Ref.4 Ref.11 Ref.15 Ref.17

Sequences

	Sequence		Length	Mass (Da)
	O00264 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: CCD5E802E1C9E604	FASTA	195	21,671
	10 20 30 40 50 60 MAAEDVVATG ADPSDLESGG LLHEIFTSPL NLLLLGLCIF LLYKIVRGDQ PAASGDSDDD 70 80 90 100 110 120 EPPPLPRLKR RDFTPAELRR FDGVQDPRIL MAINGKVFDV TKGRKFYGPE GPYGVFAGRD 130 140 150 160 170 180 ASRGLATFCL DKEALKDEYD DLSDLTAAQQ ETLSDWESQF TFKYHHVGKL LKEGEEPTVY 190 SDEEEPKDES ARKND

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and tissue expression of two putative steroid membrane receptors." Gerdes D., Wehling M., Leube B., Falkenstein E. Biol. Chem. 379:907-911(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[3]	"The human membrane progesterone receptor gene: genomic structure and promoter analysis." Bernauer S., Wehling M., Gerdes D., Falkenstein E. DNA Seq. 12:13-25(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-109.
[4]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 48-67; 81-88; 105-119; 124-132 AND 173-192, PHOSPHORYLATION AT SER-181, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[5]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Prostate cancer.
[7]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[8]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, MASS SPECTROMETRY. Tissue: T-cell.
[9]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-57, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, MASS SPECTROMETRY. Tissue: Liver.
[13]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, MASS SPECTROMETRY.
[14]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y12711 mRNA. Translation: CAA73248.1. BC034238 mRNA. Translation: AAH34238.1. AJ249131 Genomic DNA. Translation: CAB65109.1.
IPI	IPI00220739.
RefSeq	NP_006658.1. NM_006667.3.
UniGene	Hs.90061.
3D structure databases
ProteinModelPortal	O00264.
ModBase	Search...
Protein-protein interaction databases
IntAct	O00264. 9 interactions.
STRING	9606.ENSP00000217971.
PTM databases
PhosphoSite	O00264.
2D gel databases
OGP	O00264.
Proteomic databases
PaxDb	O00264.
PeptideAtlas	O00264.
PRIDE	O00264.
Protocols and materials databases
DNASU	10857.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000217971; ENSP00000217971; ENSG00000101856.
GeneID	10857.
KEGG	hsa:10857.
UCSC	uc004erb.3. human.
Organism-specific databases
CTD	10857.
GeneCards	GC0XP118370.
HGNC	HGNC:16090. PGRMC1.
HPA	HPA002877.
MIM	300435. gene.
neXtProt	NX_O00264.
PharmGKB	PA33248.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG291734.
HOGENOM	HOG000187840.
HOVERGEN	HBG059971.
InParanoid	O00264.
OMA	EHDDLSD.
OrthoDB	EOG4SXNDQ.
PhylomeDB	O00264.
Gene expression databases
ArrayExpress	O00264.
Bgee	O00264.
CleanEx	HS_PGRMC1.
Genevestigator	O00264.
GermOnline	ENSG00000101856. Homo sapiens.
Family and domain databases
Gene3D	3.10.120.10. 1 hit.
InterPro	IPR001199. Cyt_B5-like_heme/steroid-bd. [Graphical view]
Pfam	PF00173. Cyt-b5. 1 hit. [Graphical view]
SUPFAM	SSF55856. Cyt_B5. 1 hit.
PROSITE	PS00191. CYTOCHROME_B5_1. False negative. PS50255. CYTOCHROME_B5_2. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10857.
NextBio	41215.
SOURCE	Search...

Entry information

Entry name

PGRC1_HUMAN

Accession

Primary (citable) accession number: O00264
Secondary accession number(s): Q9UGJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.