ID   PAQR7_HUMAN             Reviewed;         346 AA.
AC   Q86WK9; A2A2D3; Q5XKF9; Q86VE4;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 144.
DE   RecName: Full=Membrane progestin receptor alpha {ECO:0000303|PubMed:23763432};
DE            Short=mPR alpha {ECO:0000303|PubMed:23763432};
DE   AltName: Full=Membrane progesterone P4 receptor alpha {ECO:0000303|PubMed:23763432};
DE   AltName: Full=Membrane progesterone receptor alpha {ECO:0000303|PubMed:23763432};
DE   AltName: Full=Progesterone and adipoQ receptor family member 7;
DE   AltName: Full=Progestin and adipoQ receptor family member 7 {ECO:0000303|PubMed:16044242};
DE   AltName: Full=Progestin and adipoQ receptor family member VII;
GN   Name=PAQR7 {ECO:0000312|HGNC:HGNC:23146}; Synonyms=MRPA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=12601167; DOI=10.1073/pnas.0436133100;
RA   Zhu Y., Bond J., Thomas P.;
RT   "Identification, classification, and partial characterization of genes in
RT   humans and other vertebrates homologous to a fish membrane progestin
RT   receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:2237-2242(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=16044242; DOI=10.1007/s00239-004-0375-2;
RA   Tang Y.T., Hu T., Arterburn M., Boyle B., Bright J.M., Emtage P.C.,
RA   Funk W.D.;
RT   "PAQR proteins: a novel membrane receptor family defined by an ancient 7-
RT   transmembrane pass motif.";
RL   J. Mol. Evol. 61:372-380(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-227.
RC   TISSUE=Duodenum, and Uterus;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   REVIEW.
RX   PubMed=12606724; DOI=10.1073/pnas.0530224100;
RA   Hammes S.R.;
RT   "The further redefining of steroid-mediated signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:2168-2170(2003).
RN   [7]
RP   FUNCTION, REVIEW, AND SUBCELLULAR LOCATION.
RX   PubMed=23763432; DOI=10.1111/jne.12060;
RA   Petersen S.L., Intlekofer K.A., Moura-Conlon P.J., Brewer D.N.,
RA   Del Pino Sans J., Lopez J.A.;
RT   "Nonclassical progesterone signalling molecules in the nervous system.";
RL   J. Neuroendocrinol. 25:991-1001(2013).
RN   [8]
RP   FUNCTION.
RX   PubMed=23161870; DOI=10.1210/en.2012-1772;
RA   Pang Y., Dong J., Thomas P.;
RT   "Characterization, neurosteroid binding and brain distribution of human
RT   membrane progesterone receptors delta and {epsilon} (mPRdelta and
RT   mPR{epsilon}) and mPRdelta involvement in neurosteroid inhibition of
RT   apoptosis.";
RL   Endocrinology 154:283-295(2013).
CC   -!- FUNCTION: Plasma membrane progesterone (P4) receptor coupled to G
CC       proteins (PubMed:23763432). Seems to act through a G(i) mediated
CC       pathway (PubMed:23763432). May be involved in oocyte maturation
CC       (PubMed:12601167). Involved in neurosteroid inhibition of apoptosis
CC       (PubMed:23161870). Also binds dehydroepiandrosterone (DHEA),
CC       pregnanolone, pregnenolone and allopregnanolone (PubMed:23161870).
CC       {ECO:0000269|PubMed:12601167, ECO:0000269|PubMed:23161870,
CC       ECO:0000303|PubMed:23763432}.
CC   -!- INTERACTION:
CC       Q86WK9; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-10694587, EBI-781551;
CC       Q86WK9; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-10694587, EBI-18304435;
CC       Q86WK9; P42858: HTT; NbExp=3; IntAct=EBI-10694587, EBI-466029;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000303|PubMed:23763432};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in a wide range of tissues including
CC       ovary, testis, placenta, uterus and bladder.
CC       {ECO:0000269|PubMed:12601167, ECO:0000269|PubMed:16044242}.
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:0000303|PubMed:23763432}.
CC   -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}.
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DR   EMBL; AF313620; AAO47233.1; -; mRNA.
DR   EMBL; AY424285; AAR08373.1; -; mRNA.
DR   EMBL; AL033528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX07862.1; -; Genomic_DNA.
DR   EMBL; BC034015; AAH34015.1; -; mRNA.
DR   EMBL; BC042298; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS267.1; -.
DR   RefSeq; NP_848509.1; NM_178422.5.
DR   RefSeq; XP_005245802.1; XM_005245745.3.
DR   RefSeq; XP_005245803.1; XM_005245746.3.
DR   RefSeq; XP_011539163.1; XM_011540861.1.
DR   RefSeq; XP_011539164.1; XM_011540862.2.
DR   AlphaFoldDB; Q86WK9; -.
DR   SMR; Q86WK9; -.
DR   BioGRID; 127887; 8.
DR   IntAct; Q86WK9; 4.
DR   STRING; 9606.ENSP00000363414; -.
DR   iPTMnet; Q86WK9; -.
DR   PhosphoSitePlus; Q86WK9; -.
DR   BioMuta; PAQR7; -.
DR   DMDM; 51316435; -.
DR   EPD; Q86WK9; -.
DR   jPOST; Q86WK9; -.
DR   MassIVE; Q86WK9; -.
DR   MaxQB; Q86WK9; -.
DR   PaxDb; 9606-ENSP00000363414; -.
DR   PeptideAtlas; Q86WK9; -.
DR   ProteomicsDB; 70180; -.
DR   Antibodypedia; 30521; 188 antibodies from 26 providers.
DR   DNASU; 164091; -.
DR   Ensembl; ENST00000374296.4; ENSP00000363414.3; ENSG00000182749.6.
DR   Ensembl; ENST00000675840.1; ENSP00000502514.1; ENSG00000182749.6.
DR   GeneID; 164091; -.
DR   KEGG; hsa:164091; -.
DR   MANE-Select; ENST00000675840.1; ENSP00000502514.1; NM_178422.6; NP_848509.1.
DR   UCSC; uc001bkx.4; human.
DR   AGR; HGNC:23146; -.
DR   CTD; 164091; -.
DR   DisGeNET; 164091; -.
DR   GeneCards; PAQR7; -.
DR   HGNC; HGNC:23146; PAQR7.
DR   HPA; ENSG00000182749; Low tissue specificity.
DR   MIM; 607779; gene.
DR   neXtProt; NX_Q86WK9; -.
DR   OpenTargets; ENSG00000182749; -.
DR   PharmGKB; PA142671200; -.
DR   VEuPathDB; HostDB:ENSG00000182749; -.
DR   eggNOG; KOG0748; Eukaryota.
DR   GeneTree; ENSGT00940000161438; -.
DR   HOGENOM; CLU_052356_0_0_1; -.
DR   InParanoid; Q86WK9; -.
DR   OMA; AIEKEWH; -.
DR   OrthoDB; 373478at2759; -.
DR   PhylomeDB; Q86WK9; -.
DR   TreeFam; TF319738; -.
DR   PathwayCommons; Q86WK9; -.
DR   SignaLink; Q86WK9; -.
DR   BioGRID-ORCS; 164091; 15 hits in 1154 CRISPR screens.
DR   ChiTaRS; PAQR7; human.
DR   GenomeRNAi; 164091; -.
DR   Pharos; Q86WK9; Tbio.
DR   PRO; PR:Q86WK9; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q86WK9; Protein.
DR   Bgee; ENSG00000182749; Expressed in oviduct epithelium and 181 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003707; F:nuclear steroid receptor activity; IBA:GO_Central.
DR   GO; GO:0005496; F:steroid binding; IBA:GO_Central.
DR   GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0048545; P:response to steroid hormone; IBA:GO_Central.
DR   InterPro; IPR004254; AdipoR/HlyIII-related.
DR   PANTHER; PTHR20855; ADIPOR/PROGESTIN RECEPTOR-RELATED; 1.
DR   PANTHER; PTHR20855:SF41; MEMBRANE PROGESTIN RECEPTOR ALPHA; 1.
DR   Pfam; PF03006; HlyIII; 1.
DR   Genevisible; Q86WK9; HS.
PE   1: Evidence at protein level;
KW   Cell membrane; Developmental protein; Differentiation; Lipid-binding;
KW   Membrane; Oogenesis; Receptor; Reference proteome; Steroid-binding;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..346
FT                   /note="Membrane progestin receptor alpha"
FT                   /id="PRO_0000218835"
FT   TOPO_DOM        1..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..103
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..169
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        191..237
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..276
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        298..316
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        338..346
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   VARIANT         227
FT                   /note="V -> M (in dbSNP:rs55948644)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_060999"
FT   VARIANT         272
FT                   /note="G -> R (in dbSNP:rs6689014)"
FT                   /id="VAR_048204"
SQ   SEQUENCE   346 AA;  39719 MW;  7D12639DD4756501 CRC64;
     MAMAQKLSHL LPSLRQVIQE PQLSLQPEPV FTVDRAEVPP LFWKPYIYAG YRPLHQTWRF
     YFRTLFQQHN EAVNVWTHLL AALVLLLRLA LFVETVDFWG DPHALPLFII VLASFTYLSF
     SALAHLLQAK SEFWHYSFFF LDYVGVAVYQ FGSALAHFYY AIEPAWHAQV QAVFLPMAAF
     LAWLSCIGSC YNKYIQKPGL LGRTCQEVPS VLAYALDISP VVHRIFVSSD PTTDDPALLY
     HKCQVVFFLL AAAFFSTFMP ERWFPGSCHV FGQGHQLFHI FLVLCTLAQL EAVALDYEAR
     RPIYEPLHTH WPHNFSGLFL LTVGSSILTA FLLSQLVQRK LDQKTK
//