PGRC1_CHICK
ID PGRC1_CHICK Reviewed; 192 AA.
AC Q5ZKN2; Q5ZL66;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Membrane-associated progesterone receptor component 1;
DE Short=mPR {ECO:0000250|UniProtKB:O00264};
GN Name=PGRMC1; ORFNames=RCJMB04_7g20, RCJMB04_9p4;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Component of a progesterone-binding protein complex. Binds
CC progesterone. Has many reported cellular functions (heme homeostasis,
CC interaction with CYPs). May be 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. {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 105 and 129. {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; AJ719868; CAG31527.1; -; mRNA.
DR EMBL; AJ720052; CAG31711.1; -; mRNA.
DR RefSeq; NP_001258868.1; NM_001271939.1.
DR AlphaFoldDB; Q5ZKN2; -.
DR SMR; Q5ZKN2; -.
DR STRING; 9031.ENSGALP00000038260; -.
DR PaxDb; Q5ZKN2; -.
DR Ensembl; ENSGALT00000039050; ENSGALP00000038260; ENSGALG00000020260.
DR GeneID; 772196; -.
DR KEGG; gga:772196; -.
DR CTD; 10857; -.
DR VEuPathDB; HostDB:geneid_772196; -.
DR eggNOG; KOG1110; Eukaryota.
DR GeneTree; ENSGT00940000160619; -.
DR HOGENOM; CLU_042860_1_0_1; -.
DR InParanoid; Q5ZKN2; -.
DR OMA; ANEWETQ; -.
DR OrthoDB; 1331617at2759; -.
DR PhylomeDB; Q5ZKN2; -.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR PRO; PR:Q5ZKN2; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000020260; Expressed in spermatocyte and 14 other tissues.
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; IEA:Ensembl.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..192
FT /note="Membrane-associated progesterone receptor component
FT 1"
FT /id="PRO_0000253630"
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..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 70..169
FT /note="Cytochrome b5 heme-binding"
FT REGION 172..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 111
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 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CONFLICT 146
FT /note="T -> I (in Ref. 1; CAG31527)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21282 MW; 2FA6BE33FE48E09D CRC64;
MAAEEPAMAG EEAVATEGGG LLLEIVGSPL NLSLLGLCLF LLYQILRGER PAAQPGEAGP
PPLPKMKRRD FTLEQLRPYD GVRDPRILMA VNGKVFDVTR ASKFYGPDGP YGIFAGRDAS
RGLATFCLDK EALRDDYDDL SDLNATQQET LRDWESQFTF KYHHVGKLLK DGEEPTVYSD
EEEKDAQDAK KE
