PAQR7_HUMAN
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 03-AUG-2022, entry version 136.
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; 7.
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; Q86WK9; -.
DR PeptideAtlas; Q86WK9; -.
DR PRIDE; Q86WK9; -.
DR ProteomicsDB; 70180; -.
DR Antibodypedia; 30521; 171 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 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; VHRIYSC; -.
DR OrthoDB; 1524940at2759; -.
DR PhylomeDB; Q86WK9; -.
DR TreeFam; TF319738; -.
DR PathwayCommons; Q86WK9; -.
DR SignaLink; Q86WK9; -.
DR BioGRID-ORCS; 164091; 13 hits in 1077 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 179 other tissues.
DR Genevisible; Q86WK9; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0038023; F:signaling 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; PTHR20855; 1.
DR Pfam; PF03006; HlyIII; 1.
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
