PGRC1_PIG
ID PGRC1_PIG Reviewed; 194 AA.
AC Q95250;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Membrane-associated progesterone receptor component 1;
DE Short=mPR {ECO:0000250|UniProtKB:O00264};
GN Name=PGRMC1; Synonyms=PGRMC;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Vascular smooth muscle;
RX PubMed=8954087; DOI=10.1006/bbrc.1996.1761;
RA Falkenstein E., Meyer C., Eisen C., Scriba P.C., Wehling M.;
RT "Full-length cDNA sequence of a progesterone membrane-binding protein from
RT porcine vascular smooth muscle cells.";
RL Biochem. Biophys. Res. Commun. 229:86-89(1996).
RN [2]
RP PROTEIN SEQUENCE OF 2-21, CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=8774719; DOI=10.1111/j.1432-1033.1996.0726u.x;
RA Meyer C., Schmid R., Scriba P.C., Wehling M.;
RT "Purification and partial sequencing of high-affinity progesterone-binding
RT site(s) from porcine liver membranes.";
RL Eur. J. Biochem. 239:726-731(1996).
CC -!- FUNCTION: Component of a progesterone-binding protein complex. Binds
CC progesterone. Has many reported cellular functions (heme homeostasis,
CC interaction with CYPs). Required for the maintenance of uterine
CC histoarchitecture and normal female reproductive lifespan.
CC Intracellular heme chaperone. Regulates heme synthesis via interactions
CC with FECH and acts as a heme donor for at least some hemoproteins.
CC {ECO:0000250|UniProtKB:O00264}.
CC -!- SUBUNIT: Homodimer. Forms stable homodimer through hydrophobic heme-
CC heme stacking interactions. Interacts with FECH; the interaction
CC results in decreased FECH activity (By similarity). Interacts with
CC EGFR, CYP1A1 and CYP3A4; the interactions require PGRMC1
CC homodimerization (By similarity). {ECO:0000250|UniProtKB:O00264}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:8774719};
CC Single-pass membrane protein {ECO:0000255}. Smooth endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:O00264}; Single-pass membrane
CC protein {ECO:0000255}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:O55022}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:O00264}; Extracellular side
CC {ECO:0000250|UniProtKB:O55022}.
CC -!- DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved iron-
CC binding His residues at positions 106 and 130. {ECO:0000250}.
CC -!- MISCELLANEOUS: Non-classical progesterone receptors involved in
CC extranuclear signaling are classified in 2 groups: the class II
CC progestin and adipoQ receptor (PAQR) family (also called mPRs) (PAQR5,
CC PAQR6, PAQR7, PAQR8 and PAQR9) and the b5-like heme/steroid-binding
CC protein family (also called MAPRs) (PGRMC1, PGRMC2, NENF and CYB5D2).
CC {ECO:0000250|UniProtKB:O00264}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC {ECO:0000305}.
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DR EMBL; X99714; CAA68050.1; -; mRNA.
DR PIR; JC5260; JC5260.
DR RefSeq; NP_999076.1; NM_213911.1.
DR AlphaFoldDB; Q95250; -.
DR SMR; Q95250; -.
DR STRING; 9823.ENSSSCP00000013423; -.
DR iPTMnet; Q95250; -.
DR PaxDb; Q95250; -.
DR PeptideAtlas; Q95250; -.
DR PRIDE; Q95250; -.
DR Ensembl; ENSSSCT00000035161; ENSSSCP00000029059; ENSSSCG00000012625.
DR Ensembl; ENSSSCT00015012355; ENSSSCP00015004831; ENSSSCG00015009336.
DR Ensembl; ENSSSCT00025096587; ENSSSCP00025042403; ENSSSCG00025070346.
DR Ensembl; ENSSSCT00030047828; ENSSSCP00030021548; ENSSSCG00030034525.
DR Ensembl; ENSSSCT00035101064; ENSSSCP00035042984; ENSSSCG00035074446.
DR Ensembl; ENSSSCT00040046175; ENSSSCP00040019365; ENSSSCG00040034317.
DR Ensembl; ENSSSCT00045059480; ENSSSCP00045041702; ENSSSCG00045034716.
DR Ensembl; ENSSSCT00050101110; ENSSSCP00050043942; ENSSSCG00050073899.
DR Ensembl; ENSSSCT00055053272; ENSSSCP00055042506; ENSSSCG00055026958.
DR Ensembl; ENSSSCT00060055303; ENSSSCP00060023627; ENSSSCG00060040801.
DR Ensembl; ENSSSCT00065046988; ENSSSCP00065020212; ENSSSCG00065034517.
DR Ensembl; ENSSSCT00070016400; ENSSSCP00070013576; ENSSSCG00070008491.
DR GeneID; 396946; -.
DR KEGG; ssc:396946; -.
DR CTD; 10857; -.
DR VGNC; VGNC:91363; PGRMC1.
DR eggNOG; KOG1110; Eukaryota.
DR GeneTree; ENSGT00940000160619; -.
DR HOGENOM; CLU_042860_1_0_1; -.
DR InParanoid; Q95250; -.
DR OMA; ANEWETQ; -.
DR OrthoDB; 1331617at2759; -.
DR TreeFam; TF314562; -.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Proteomes; UP000008227; Chromosome X.
DR Proteomes; UP000314985; Unassembled WGS sequence.
DR Bgee; ENSSSCG00000012625; Expressed in adult mammalian kidney and 43 other tissues.
DR ExpressionAtlas; Q95250; baseline and differential.
DR Genevisible; Q95250; SS.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR Pfam; PF00173; Cyt-b5; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Iron; Lipid-binding;
KW Membrane; Metal-binding; Microsome; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Receptor; Reference proteome;
KW Steroid-binding; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8774719"
FT CHAIN 2..194
FT /note="Membrane-associated progesterone receptor component
FT 1"
FT /id="PRO_0000121741"
FT TOPO_DOM 2..24
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 71..170
FT /note="Cytochrome b5 heme-binding"
FT REGION 50..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:O00264"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00264"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00264"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00264"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00264"
SQ SEQUENCE 194 AA; 21609 MW; A852E79E5F5C74D3 CRC64;
MAAEDVAATG ADPSELEGGG LLHEIFTSPL NLLLLGLCIF LLYKIVRGDQ PAASDSDDDE
PPPLPRLKRR DFTPAELRRF DGVQDPRILM AINGKVFDVT KGRKFYGPEG PYGVFAGRDA
SRGLATFCLD KEALKDEYDD LSDLTPAQQE TLNDWDSQFT FKYHHVGKLL KEGEEPTVYS
DEEEPKDESA RKND
