ID PGRC1_BOVIN Reviewed; 194 AA.
AC Q17QC0; Q9N0T7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Membrane-associated progesterone receptor component 1;
DE Short=mPR {ECO:0000250|UniProtKB:O00264};
GN Name=PGRMC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-194.
RC TISSUE=Lens epithelium;
RA Zhu X.L., Cenedella R.J.;
RT "Steroid binding protein of bovine lens epithelial cell membranes.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of a progesterone-binding protein complex. Binds
CC progesterone (By similarity). Has many reported cellular functions
CC (heme homeostasis, interaction with CYPs). Required for the maintenance
CC of uterine histoarchitecture and normal female reproductive lifespan
CC (By similarity). Intracellular heme chaperone. Regulates heme synthesis
CC via interactions with FECH and acts as a heme donor for at least some
CC hemoproteins (By similarity). Forms a ternary complex with TMEM97
CC receptor and low density lipid receptor/LDLR, which increases LDLR-
CC mediated LDL lipoprotein internalization (By similarity).
CC {ECO:0000250|UniProtKB:O00264, ECO:0000250|UniProtKB:O55022}.
CC -!- SUBUNIT: Homodimer. Forms stable homodimer through hydrophobic heme-
CC heme stacking interactions. Interacts with FECH; the interaction
CC results in decreased FECH activity. Interacts with EGFR, CYP1A1 and
CC CYP3A4; the interactions require PGRMC1 homodimerization. Interacts
CC with TMEM97 and LDLR; the interaction increases LDL internalization.
CC {ECO:0000250|UniProtKB:O00264}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:Q95250}; Single-pass membrane protein
CC {ECO:0000255}. Smooth endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O00264}; Single-pass membrane protein
CC {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}. Secreted
CC {ECO:0000250|UniProtKB:O00264}.
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; BC118444; AAI18445.1; -; mRNA.
DR EMBL; AF254804; AAF67749.1; -; mRNA.
DR RefSeq; NP_001068601.1; NM_001075133.1.
DR AlphaFoldDB; Q17QC0; -.
DR SMR; Q17QC0; -.
DR STRING; 9913.ENSBTAP00000026053; -.
DR PaxDb; 9913-ENSBTAP00000026053; -.
DR PeptideAtlas; Q17QC0; -.
DR GeneID; 317706; -.
DR KEGG; bta:317706; -.
DR CTD; 10857; -.
DR eggNOG; KOG1110; Eukaryota.
DR InParanoid; Q17QC0; -.
DR OrthoDB; 148785at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:AgBase.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; ISS:AgBase.
DR GO; GO:0042585; C:germinal vesicle; IDA:AgBase.
DR GO; GO:1990385; C:meiotic spindle midzone; IDA:AgBase.
DR GO; GO:0016020; C:membrane; ISS:AgBase.
DR GO; GO:0030496; C:midbody; IDA:AgBase.
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 GO; GO:1903537; P:meiotic cell cycle process involved in oocyte maturation; IMP:AgBase.
DR GO; GO:0140077; P:positive regulation of lipoprotein transport; ISS:UniProtKB.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR PANTHER; PTHR10281:SF23; MEMBRANE-ASSOCIATED PROGESTERONE RECEPTOR COMPONENT 1; 1.
DR PANTHER; PTHR10281; MEMBRANE-ASSOCIATED PROGESTERONE RECEPTOR COMPONENT-RELATED; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Iron; Lipid-binding; Membrane; Metal-binding;
KW Microsome; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Receptor; Reference proteome; Secreted; Steroid-binding; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..194
FT /note="Membrane-associated progesterone receptor component
FT 1"
FT /id="PRO_0000253628"
FT TOPO_DOM 1..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 174..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"
FT CONFLICT 172
FT /note="D -> E (in Ref. 2; AAF67749)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="K -> E (in Ref. 2; AAF67749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 194 AA; 21622 MW; 281EE019668B5FDC CRC64;
MAAEDVAATG ADTSELESGG LLQEIFTSPL NLLLLGLCIF LLYKIVRGDQ PAASDSDDDE
PPPLPRLKRR DFTPAELRRF DGVQDPRILM AINGKVFDVT KGRKFYGPEG PYGVFAGRDA
SRGLATFCLD KEALKDEYDD LSDLTPAQQE TLSDWDSQFT FKYHHVGKLL KDGEEPTVYS
DKEEPKDEST RKND
//
