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 28-JUN-2023, entry version 131. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 ProteomicsDB; 294380; -. DR Antibodypedia; 30905; 131 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 AGR; MGI:1921479; -. 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; CAGCCFA; -. DR OrthoDB; 373478at2759; -. DR PhylomeDB; Q80ZE5; -. DR TreeFam; TF319738; -. DR BioGRID-ORCS; 74229; 3 hits in 78 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:0005886; C:plasma membrane; ISO:MGI. 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:SF22; MEMBRANE PROGESTIN RECEPTOR BETA; 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 //