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PAQR5_MOUSE
ID   PAQR5_MOUSE             Reviewed;         330 AA.
AC   Q9DCU0; Q7TPQ5; Q8C6Z8;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Membrane progestin receptor gamma {ECO:0000250|UniProtKB:Q9NXK6};
DE            Short=mPR gamma {ECO:0000250|UniProtKB:Q9NXK6};
DE   AltName: Full=Membrane progesterone P4 receptor gamma {ECO:0000250|UniProtKB:Q9NXK6};
DE   AltName: Full=Membrane progesterone receptor gamma {ECO:0000250|UniProtKB:Q9NXK6};
DE   AltName: Full=Progesterone and adipoQ receptor family member 5;
DE   AltName: Full=Progestin and adipoQ receptor family member 5 {ECO:0000250|UniProtKB:Q9NXK6};
DE   AltName: Full=Progestin and adipoQ receptor family member V;
GN   Name=Paqr5 {ECO:0000312|MGI:MGI:1921340}; Synonyms=Mprg;
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].
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head, Kidney, and Urinary bladder;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-325.
RC   STRAIN=FVB/N; TISSUE=Colon;
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).
CC   -!- FUNCTION: Plasma membrane progesterone (P4) receptor coupled to G
CC       proteins. Seems to act through a G(i) mediated pathway. May be involved
CC       in oocyte maturation. {ECO:0000250|UniProtKB:Q9NXK6}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NXK6};
CC       Multi-pass membrane protein {ECO:0000255}.
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:Q9NXK6}.
CC   -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH54855.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=BAC35142.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY424294; AAR08382.1; -; mRNA.
DR   EMBL; AK002481; BAB22133.1; -; mRNA.
DR   EMBL; AK035475; BAC29072.1; -; mRNA.
DR   EMBL; AK052776; BAC35142.1; ALT_INIT; mRNA.
DR   EMBL; AK085411; BAC39443.1; -; mRNA.
DR   EMBL; AK086679; BAC39718.1; -; mRNA.
DR   EMBL; BC054855; AAH54855.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS23261.1; -.
DR   RefSeq; NP_083024.1; NM_028748.2.
DR   AlphaFoldDB; Q9DCU0; -.
DR   SMR; Q9DCU0; -.
DR   STRING; 10090.ENSMUSP00000034817; -.
DR   PhosphoSitePlus; Q9DCU0; -.
DR   PaxDb; Q9DCU0; -.
DR   PRIDE; Q9DCU0; -.
DR   ProteomicsDB; 287949; -.
DR   Antibodypedia; 13981; 109 antibodies from 22 providers.
DR   DNASU; 74090; -.
DR   Ensembl; ENSMUST00000034817; ENSMUSP00000034817; ENSMUSG00000032278.
DR   GeneID; 74090; -.
DR   KEGG; mmu:74090; -.
DR   UCSC; uc009qaa.1; mouse.
DR   CTD; 54852; -.
DR   MGI; MGI:1921340; Paqr5.
DR   VEuPathDB; HostDB:ENSMUSG00000032278; -.
DR   eggNOG; KOG0748; Eukaryota.
DR   GeneTree; ENSGT00940000158844; -.
DR   HOGENOM; CLU_052356_1_0_1; -.
DR   InParanoid; Q9DCU0; -.
DR   OMA; GLCKMLR; -.
DR   OrthoDB; 1524940at2759; -.
DR   PhylomeDB; Q9DCU0; -.
DR   TreeFam; TF319738; -.
DR   BioGRID-ORCS; 74090; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Paqr5; mouse.
DR   PRO; PR:Q9DCU0; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9DCU0; protein.
DR   Bgee; ENSMUSG00000032278; Expressed in urinary bladder urothelium and 160 other tissues.
DR   ExpressionAtlas; Q9DCU0; baseline and differential.
DR   Genevisible; Q9DCU0; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
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..330
FT                   /note="Membrane progestin receptor gamma"
FT                   /id="PRO_0000218844"
FT   TOPO_DOM        1..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..81
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..101
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..113
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..141
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..186
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        208..253
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..294
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..315
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        316..330
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   330 AA;  38151 MW;  A68EE63260F2214D CRC64;
     MLSLKLPRLF RIDQVPQVFH EQGILFGYRH PQSSATACIL SLFQMTNETL NIWTHLLPFW
     FFVWRFMTAL YVTDIQNDSY SWPMLVYMCT SCVYPLASSC AHTFSSMSKN ARHICYFLDY
     GAVNLFSLGS AIAYSAYTFP DALVCSTFHE CYVALAVLNT ILSTGLSCYS RFLELQKPRL
     CKLLRVLAFA YPYTWDSLPI FYRLFLFPGE SSRNEAMLYH QKHMGMTLLA SFFYSAHLPE
     RLAPGRFDYI GHSHQLFHVC VILATHLQME AILLDKTLRR EWLLATSRPF SFPQIAAAML
     LCIIFSLSNI IYFSAALYRI PEPELHEKET
 
 
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