RBCC

Full text data of PGRMC1

PGRMC1 (HPR6.6, PGRMC) [Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Membrane-associated progesterone receptor component 1; mPR

UniProt O00264
ID PGRC1_HUMAN Reviewed; 195 AA.
AC O00264; Q9UGJ9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Membrane-associated progesterone receptor component 1;
DE Short=mPR;
GN Name=PGRMC1; Synonyms=HPR6.6, PGRMC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9705155;
RA Gerdes D., Wehling M., Leube B., Falkenstein E.;
RT "Cloning and tissue expression of two putative steroid membrane
RT receptors.";
RL Biol. Chem. 379:907-911(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-109.
RX PubMed=11697142;
RA Bernauer S., Wehling M., Gerdes D., Falkenstein E.;
RT "The human membrane progesterone receptor gene: genomic structure and
RT promoter analysis.";
RL DNA Seq. 12:13-25(2001).
RN [4]
RP PROTEIN SEQUENCE OF 48-67; 81-88; 105-119; 124-132 AND 173-192,
RP PHOSPHORYLATION AT SER-181, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND MASS
RP SPECTROMETRY.
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-57, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Receptor for progesterone (By similarity).
CC -!- INTERACTION:
CC P00181:CYP2C2 (xeno); NbExp=6; IntAct=EBI-1045534, EBI-4320576;
CC P16435:POR; NbExp=5; IntAct=EBI-1045534, EBI-726554;
CC -!- SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane
CC protein (By similarity). Endoplasmic reticulum membrane; Single-
CC pass membrane protein (By similarity).
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
CC liver and kidney.
CC -!- DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved
CC iron-binding His residues at positions 107 and 131 (By
CC similarity).
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
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DR EMBL; Y12711; CAA73248.1; -; mRNA.
DR EMBL; BC034238; AAH34238.1; -; mRNA.
DR EMBL; AJ249131; CAB65109.1; -; Genomic_DNA.
DR RefSeq; NP_006658.1; NM_006667.4.
DR UniGene; Hs.90061; -.
DR ProteinModelPortal; O00264; -.
DR SMR; O00264; 72-171.
DR IntAct; O00264; 11.
DR MINT; MINT-2997519; -.
DR STRING; 9606.ENSP00000217971; -.
DR PhosphoSite; O00264; -.
DR OGP; O00264; -.
DR PaxDb; O00264; -.
DR PeptideAtlas; O00264; -.
DR PRIDE; O00264; -.
DR DNASU; 10857; -.
DR Ensembl; ENST00000217971; ENSP00000217971; ENSG00000101856.
DR GeneID; 10857; -.
DR KEGG; hsa:10857; -.
DR UCSC; uc004erb.3; human.
DR CTD; 10857; -.
DR GeneCards; GC0XP118370; -.
DR HGNC; HGNC:16090; PGRMC1.
DR HPA; HPA002877; -.
DR MIM; 300435; gene.
DR neXtProt; NX_O00264; -.
DR PharmGKB; PA33248; -.
DR eggNOG; NOG291734; -.
DR HOGENOM; HOG000187840; -.
DR HOVERGEN; HBG059971; -.
DR InParanoid; O00264; -.
DR KO; K17278; -.
DR OMA; EHDDLSD; -.
DR OrthoDB; EOG7KWSKJ; -.
DR PhylomeDB; O00264; -.
DR GeneWiki; PGRMC1; -.
DR GenomeRNAi; 10857; -.
DR NextBio; 41215; -.
DR PRO; PR:O00264; -.
DR ArrayExpress; O00264; -.
DR Bgee; O00264; -.
DR CleanEx; HS_PGRMC1; -.
DR Genevestigator; O00264; -.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005496; F:steroid binding; TAS:ProtInc.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR Pfam; PF00173; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; FALSE_NEG.
DR PROSITE; PS50255; CYTOCHROME_B5_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; Endoplasmic reticulum;
KW Lipid-binding; Membrane; Microsome; Phosphoprotein; Receptor;
KW Reference proteome; Steroid-binding; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 195 Membrane-associated progesterone receptor
FT component 1.
FT /FTId=PRO_0000121739.
FT TOPO_DOM 2 24 Lumenal (Potential).
FT TRANSMEM 25 43 Helical; (Potential).
FT TOPO_DOM 44 195 Cytoplasmic (Potential).
FT DOMAIN 72 171 Cytochrome b5 heme-binding.
FT MOD_RES 54 54 Phosphoserine.
FT MOD_RES 57 57 Phosphoserine.
FT MOD_RES 181 181 Phosphoserine.
SQ SEQUENCE 195 AA; 21671 MW; CCD5E802E1C9E604 CRC64;
MAAEDVVATG ADPSDLESGG LLHEIFTSPL NLLLLGLCIF LLYKIVRGDQ PAASGDSDDD
EPPPLPRLKR RDFTPAELRR FDGVQDPRIL MAINGKVFDV TKGRKFYGPE GPYGVFAGRD
ASRGLATFCL DKEALKDEYD DLSDLTAAQQ ETLSDWESQF TFKYHHVGKL LKEGEEPTVY
SDEEEPKDES ARKND
//

MIM 300435
*RECORD*
*FIELD* NO
300435
*FIELD* TI
*300435 PROGESTERONE RECEPTOR MEMBRANE COMPONENT 1; PGRMC1
*FIELD* TX

CLONING

Using the sequence of a porcine progesterone receptor as probe, Gerdes
read moreet al. (1998) cloned PGRMC1, which they designated HPR6.6. The deduced
protein contains 195 amino acids and has an N-terminal 26-residue
hydrophobic region. It has no N-glycosylation site. PGRMC1 shares about
50% identity overall with PGRMC2 (607735), and they share 68% identity
in their C termini, including a highly conserved 58-amino acid sequence.
Northern blot analysis revealed expression of 2.0- and 5.0-kb
transcripts in all tissues examined, with highest expression in liver
and kidney. Transfection in HEK293 cells resulted in a protein with an
apparent molecular mass of about 28 kD.

MAPPING

By PCR analysis of human-hamster hybrid panels and by genomic sequence
analysis, Gerdes et al. (1998) mapped the PGRMC1 gene to chromosome
Xq22-q24.

*FIELD* RF
1. Gerdes, D.; Wehling, M.; Leube, B.; Falkenstein, E.: Cloning and
tissue expression of two putative steroid membrane receptors. Biol.
Chem. 379: 907-911, 1998.

*FIELD* CD
Patricia A. Hartz: 4/30/2003

*FIELD* ED
mgross: 04/30/2003

RBCC Red Blood Cell Collection

Full text data of PGRMC1