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PKR2_MOUSE
ID   PKR2_MOUSE              Reviewed;         381 AA.
AC   Q8K458; A2AMQ8; Q80XQ0; Q8BIR4;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Prokineticin receptor 2;
DE            Short=PK-R2;
DE   AltName: Full=G-protein coupled receptor 73-like 1;
GN   Name=Prokr2; Synonyms=Gpr73l1, Pkr2;
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=12024206; DOI=10.1038/417405a;
RA   Cheng M.Y., Bullock C.M., Li C., Lee A.G., Bermak J.C., Belluzzi J.,
RA   Weaver D.R., Leslie F.M., Zhou Q.-Y.;
RT   "Prokineticin 2 transmits the behavioural circadian rhythm of the
RT   suprachiasmatic nucleus.";
RL   Nature 417:405-410(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata, Pituitary, and Thymus;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
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).
CC   -!- FUNCTION: Receptor for prokineticin 2. Exclusively coupled to the G(q)
CC       subclass of heteromeric G proteins. Activation leads to mobilization of
CC       calcium, stimulation of phosphoinositide turnover and activation of
CC       p44/p42 mitogen-activated protein kinase (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NFJ6};
CC       Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in several regions of the brain,
CC       including paraventricular hypothalamic nucleus, dorsal medial
CC       hypothalamic nucleus, paratenial thalamic nuclei, paracentral thalamic
CC       nucleus, lateral habenular nucleus, lateral septal nucleus, lateral
CC       globus pallidus and amygdala. Highest expression seen in
CC       paraventricular thalamic nuclei and is also extensively expressed in
CC       the suprachiasmatic nucleus.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC26971.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF487279; AAM49571.1; -; mRNA.
DR   EMBL; AK030458; BAC26971.1; ALT_INIT; mRNA.
DR   EMBL; AK041586; BAC30994.1; -; mRNA.
DR   EMBL; AK080980; BAC38103.1; -; mRNA.
DR   EMBL; AL807793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC043116; AAH43116.1; -; mRNA.
DR   CCDS; CCDS16773.1; -.
DR   RefSeq; NP_659193.3; NM_144944.3.
DR   RefSeq; XP_011237857.1; XM_011239555.2.
DR   AlphaFoldDB; Q8K458; -.
DR   SMR; Q8K458; -.
DR   STRING; 10090.ENSMUSP00000056659; -.
DR   GlyGen; Q8K458; 2 sites.
DR   PhosphoSitePlus; Q8K458; -.
DR   PaxDb; Q8K458; -.
DR   PRIDE; Q8K458; -.
DR   TopDownProteomics; Q8K458; -.
DR   Antibodypedia; 8176; 245 antibodies from 32 providers.
DR   DNASU; 246313; -.
DR   Ensembl; ENSMUST00000049997; ENSMUSP00000056659; ENSMUSG00000050558.
DR   Ensembl; ENSMUST00000110156; ENSMUSP00000105784; ENSMUSG00000050558.
DR   GeneID; 246313; -.
DR   KEGG; mmu:246313; -.
DR   UCSC; uc008mmp.2; mouse.
DR   CTD; 128674; -.
DR   MGI; MGI:2181363; Prokr2.
DR   VEuPathDB; HostDB:ENSMUSG00000050558; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000154544; -.
DR   HOGENOM; CLU_009579_6_0_1; -.
DR   InParanoid; Q8K458; -.
DR   OMA; VDCIKLQ; -.
DR   OrthoDB; 664455at2759; -.
DR   PhylomeDB; Q8K458; -.
DR   TreeFam; TF315303; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   BioGRID-ORCS; 246313; 0 hits in 71 CRISPR screens.
DR   PRO; PR:Q8K458; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8K458; protein.
DR   Bgee; ENSMUSG00000050558; Expressed in rostral migratory stream and 76 other tissues.
DR   ExpressionAtlas; Q8K458; baseline and differential.
DR   Genevisible; Q8K458; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR   GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR   GO; GO:0007623; P:circadian rhythm; IDA:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000611; NPY_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01012; NRPEPTIDEYR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..381
FT                   /note="Prokineticin receptor 2"
FT                   /id="PRO_0000070084"
FT   TOPO_DOM        1..51
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..133
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        155..168
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..220
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        242..270
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        292..310
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..331
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        332..381
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        7
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        125..205
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        244
FT                   /note="S -> P (in Ref. 4; AAH43116)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        375
FT                   /note="V -> L (in Ref. 2; BAC26971)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   381 AA;  43375 MW;  1981FD101324166D CRC64;
     MGPQNRNTSF APDLNPPQDH VSLNYSYGDY DLPLGEDEDV TKTQTFFAAK IVIGVALAGI
     MLVCGIGNFV FIAALARYKK LRNLTNLLIA NLAISDFLVA IVCCPFEMDY YVVRQLSWAH
     GHVLCASVNY LRTVSLYVST NALLAIAIDR YLAIVHPLKP RMNYQTASFL IALVWMVSIL
     IAVPSAYFTT ETILVIVKNQ EKIFCGQIWS VDQQLYYKSY FLFVFGLEFV GPVVTMTLCY
     ARISQELWFK AVPGFQTEQI RKRLRCRRKT VLLLMGILTA YVLCWAPFYG FTIVRDFFPT
     VVVKEKHYLT AFYVVECIAM SNSMINTICF VTVKNNTMKY FKKMLRLHWR PSHYGSKSSA
     DLDLKTSGVP ATEEVDCIRL K
 
 
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