PAQR8_MOUSE
ID PAQR8_MOUSE Reviewed; 354 AA.
AC Q80ZE5; Q3UHI5; Q8C891; Q8CCW9; Q9DA71;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Membrane progestin receptor beta {ECO:0000250|UniProtKB:Q8TEZ7};
DE Short=mPR beta {ECO:0000250|UniProtKB:Q8TEZ7};
DE AltName: Full=Lysosomal membrane protein in brain 1 {ECO:0000303|PubMed:11676489};
DE AltName: Full=Membrane progesterone P4 receptor beta {ECO:0000250|UniProtKB:Q8TEZ7};
DE AltName: Full=Membrane progesterone receptor beta {ECO:0000250|UniProtKB:Q8TEZ7};
DE AltName: Full=Progesterone and adipoQ receptor family member 8;
DE AltName: Full=Progestin and adipoQ receptor family member 8 {ECO:0000250|UniProtKB:Q8TEZ7};
DE AltName: Full=Progestin and adipoQ receptor family member VIII;
GN Name=Paqr8 {ECO:0000312|MGI:MGI:1921479}; Synonyms=Mprb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=CD-1; 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].
RC STRAIN=C57BL/6J;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Medulla oblongata, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=11676489; DOI=10.1006/bbrc.2001.5825;
RA Suzuki T., Ganesh S., Agarwala K.L., Morita R., Sugimoto Y., Inazawa J.,
RA Delgado-Escueta A.V., Yamakawa K.;
RT "A novel gene in the chromosomal region for juvenile myoclonic epilepsy on
RT 6p12 encodes a brain-specific lysosomal membrane protein.";
RL Biochem. Biophys. Res. Commun. 288:626-636(2001).
CC -!- FUNCTION: Plasma membrane progesterone (P4) receptor coupled to G
CC proteins. Seems to act through a G(i) mediated pathway (By similarity).
CC May be involved in oocyte maturation (PubMed:12601167). Also binds
CC dehydroepiandrosterone (DHEA), pregnanolone, pregnenolone and
CC allopregnanolone (By similarity). {ECO:0000250|UniProtKB:Q8TEZ7,
CC ECO:0000269|PubMed:12601167}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8TEZ7};
CC Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with a
CC lysosomal protein CTSD/cathepsin D. {ECO:0000250|UniProtKB:Q8TEZ7}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and testis.
CC {ECO:0000269|PubMed:11676489}.
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:Q8TEZ7}.
CC -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27629.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF313617; AAO47230.1; -; mRNA.
DR EMBL; AY424297; AAR08385.1; -; mRNA.
DR EMBL; AK006107; BAB24412.1; -; mRNA.
DR EMBL; AK029772; BAC26609.1; -; mRNA.
DR EMBL; AK031969; BAC27629.1; ALT_FRAME; mRNA.
DR EMBL; AK048045; BAC33221.1; -; mRNA.
DR EMBL; AK147376; BAE27872.1; -; mRNA.
DR EMBL; BC059813; AAH59813.1; -; mRNA.
DR CCDS; CCDS14844.1; -.
DR RefSeq; NP_083105.3; NM_028829.3.
DR RefSeq; XP_006495640.1; XM_006495577.2.
DR RefSeq; XP_006495641.1; XM_006495578.3.
DR AlphaFoldDB; Q80ZE5; -.
DR SMR; Q80ZE5; -.
DR STRING; 10090.ENSMUSP00000141054; -.
DR iPTMnet; Q80ZE5; -.
DR PhosphoSitePlus; Q80ZE5; -.
DR MaxQB; Q80ZE5; -.
DR PaxDb; Q80ZE5; -.
DR PRIDE; Q80ZE5; -.
DR ProteomicsDB; 294380; -.
DR Antibodypedia; 30905; 115 antibodies from 23 providers.
DR DNASU; 74229; -.
DR Ensembl; ENSMUST00000068880; ENSMUSP00000069127; ENSMUSG00000025931.
DR Ensembl; ENSMUST00000167119; ENSMUSP00000128781; ENSMUSG00000025931.
DR Ensembl; ENSMUST00000187651; ENSMUSP00000140913; ENSMUSG00000025931.
DR Ensembl; ENSMUST00000189400; ENSMUSP00000141054; ENSMUSG00000025931.
DR GeneID; 74229; -.
DR KEGG; mmu:74229; -.
DR UCSC; uc007ald.1; mouse.
DR CTD; 85315; -.
DR MGI; MGI:1921479; Paqr8.
DR VEuPathDB; HostDB:ENSMUSG00000025931; -.
DR eggNOG; KOG0748; Eukaryota.
DR GeneTree; ENSGT00940000159860; -.
DR HOGENOM; CLU_052356_0_0_1; -.
DR InParanoid; Q80ZE5; -.
DR OMA; QYGCSLG; -.
DR OrthoDB; 1524940at2759; -.
DR PhylomeDB; Q80ZE5; -.
DR TreeFam; TF319738; -.
DR BioGRID-ORCS; 74229; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Paqr8; mouse.
DR PRO; PR:Q80ZE5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q80ZE5; protein.
DR Bgee; ENSMUSG00000025931; Expressed in cerebellar nuclear complex and 183 other tissues.
DR Genevisible; Q80ZE5; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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 2: Evidence at transcript level;
KW Cell membrane; Developmental protein; Differentiation; Lipid-binding;
KW Membrane; Oogenesis; Receptor; Reference proteome; Steroid-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..354
FT /note="Membrane progestin receptor beta"
FT /id="PRO_0000218841"
FT TOPO_DOM 1..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..213
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CONFLICT 41
FT /note="D -> G (in Ref. 3; AAR08385/BAC33221)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="I -> V (in Ref. 1; AAO47230)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="I -> L (in Ref. 1; AAO47230)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="T -> S (in Ref. 1; AAO47230)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 40430 MW; 14544CBB3338B538 CRC64;
MTTAILERLS TLSMSGQQLR RLPKILEEGL PKMPCTVPET DVPQLFREPY IHAGYRPTGH
EWRYYFFSLF QKHNEVVNVW THLLAALAVL LRFWAFVEAG ALQWASPHTL PLLLFILSSI
TYLTCSLLAH LLQSKSELSH YTFYFVDYVG VSVYQYGSAL AHFFYSSDQA WYELFWIFFL
PAAAFCGWLS CAGCCYAKYR YRRPYPVMRK ICQVVPAGLA FVLDISPVAH RVALCHLAGC
QEQAAWYHTL QILFFLVSAY FFSCPVPEKY FPGSCDIVGH GHQIFHAFLS VCTLSQLEAI
LLDYQGRHEI FLQRHGPLSV YSACLSFFVL AACSAATATL LRHKVKDRLI KKDS
