PGRC1_PONAB
ID PGRC1_PONAB Reviewed; 195 AA.
AC Q5RED0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Membrane-associated progesterone receptor component 1;
GN Name=PGRMC1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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
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}.
CC -!- DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved iron-
CC binding His residues at positions 107 and 131. {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; CR857601; CAH89877.1; -; mRNA.
DR RefSeq; NP_001127207.1; NM_001133735.1.
DR AlphaFoldDB; Q5RED0; -.
DR SMR; Q5RED0; -.
DR STRING; 9601.ENSPPYP00000023134; -.
DR Ensembl; ENSPPYT00000024104; ENSPPYP00000023134; ENSPPYG00000020666.
DR GeneID; 100174262; -.
DR KEGG; pon:100174262; -.
DR CTD; 10857; -.
DR eggNOG; KOG1110; Eukaryota.
DR GeneTree; ENSGT00940000160619; -.
DR HOGENOM; CLU_042860_1_0_1; -.
DR InParanoid; Q5RED0; -.
DR OMA; ANEWETQ; -.
DR OrthoDB; 1331617at2759; -.
DR TreeFam; TF314562; -.
DR Proteomes; UP000001595; Chromosome X.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; Steroid-binding; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..195
FT /note="Membrane-associated progesterone receptor component
FT 1"
FT /id="PRO_0000253629"
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..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 72..171
FT /note="Cytochrome b5 heme-binding"
FT REGION 173..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113
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 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00264"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00264"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00264"
SQ SEQUENCE 195 AA; 21685 MW; 2C64E803E10F3DAF CRC64;
MAAEDVVATG ADPSELESGG LLHEIFTSPL NLLLLGLCIF LLYKIVRGDQ PAASGDSDDD
EPPPLPRLKR RDFTPAELRR FDGVQDPRIL MAINGKVFDV TKGRKFYGPE GPYGVFAGRD
ASRGLATFCL DKEALKDEYD DLSDLTAAQQ ETLSDWESQF TFKYHHVGKL LKEGEEPTVY
SDEEEPKDES ARKND
