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NPY6R_MOUSE
ID   NPY6R_MOUSE             Reviewed;         371 AA.
AC   Q61212; Q3ZAW3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Neuropeptide Y receptor type 6;
DE            Short=NPY6-R;
DE   AltName: Full=Pancreatic polypeptide receptor 2;
DE            Short=PP2;
GN   Name=Npy6r; Synonyms=Npy5r, Ppyr2, Y2b;
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 [GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=8663568; DOI=10.1074/jbc.271.28.16435;
RA   Weinberg D.H., Sirinathsinghji D.J.S., Tan C.P., Shiao L.-L., Morin N.,
RA   Rigby M.R., Heavens R.H., Rapoport D.R., Bayne M.L., Cascieri M.A.,
RA   Strader C.D., Linemeyer D.L., Macneil D.J.;
RT   "Cloning and expression of a novel neuropeptide Y receptor.";
RL   J. Biol. Chem. 271:16435-16438(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=129/Sv;
RX   PubMed=8910373; DOI=10.1074/jbc.271.44.27776;
RA   Gregor P., Feng Y., Decarr L.B., Cornfield L.J., McCaleb M.L.;
RT   "Molecular characterization of a second mouse pancreatic polypeptide
RT   receptor and its inactivated human homologue.";
RL   J. Biol. Chem. 271:27776-27781(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Ovary;
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].
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 neuropeptide Y and peptide YY. The rank order of
CC       affinity of this receptor for pancreatic polypeptides is NPY = PYY >=
CC       NPY (2-36) = [Leu-31, Pro-34] NPY > NPY (13-36) > PP. The activity of
CC       this receptor is mediated by G proteins that inhibits adenylate cyclase
CC       activity.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Kidney and discrete regions of the hypothalamus
CC       including the suprachiasmatic nucleus, anterior hypothalamus, bed
CC       nucleus stria terminalis, and the ventromedial nucleus.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo at 7 dpc.
CC       {ECO:0000269|PubMed:8910373}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- CAUTION: Was originally called NPY5-R. {ECO:0000305}.
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DR   EMBL; U58367; AAB18624.1; -; Genomic_DNA.
DR   EMBL; U59430; AAB19188.1; -; Genomic_DNA.
DR   EMBL; AK030279; BAC26875.1; -; mRNA.
DR   EMBL; BC103620; AAI03621.1; -; mRNA.
DR   EMBL; BC103621; AAI03622.1; -; mRNA.
DR   EMBL; BC103622; AAI03623.1; -; mRNA.
DR   EMBL; BC103667; AAI03668.1; -; mRNA.
DR   CCDS; CCDS29227.1; -.
DR   RefSeq; NP_035065.1; NM_010935.3.
DR   AlphaFoldDB; Q61212; -.
DR   SMR; Q61212; -.
DR   STRING; 10090.ENSMUSP00000040797; -.
DR   GlyGen; Q61212; 3 sites.
DR   PhosphoSitePlus; Q61212; -.
DR   PaxDb; Q61212; -.
DR   PRIDE; Q61212; -.
DR   ProteomicsDB; 293886; -.
DR   DNASU; 18169; -.
DR   Ensembl; ENSMUST00000042747; ENSMUSP00000040797; ENSMUSG00000038071.
DR   GeneID; 18169; -.
DR   KEGG; mmu:18169; -.
DR   UCSC; uc008euv.1; mouse.
DR   CTD; 4888; -.
DR   MGI; MGI:1098590; Npy6r.
DR   VEuPathDB; HostDB:ENSMUSG00000038071; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000163511; -.
DR   HOGENOM; CLU_009579_6_1_1; -.
DR   InParanoid; Q61212; -.
DR   OMA; FNVVFDW; -.
DR   OrthoDB; 609835at2759; -.
DR   PhylomeDB; Q61212; -.
DR   TreeFam; TF315303; -.
DR   BioGRID-ORCS; 18169; 2 hits in 72 CRISPR screens.
DR   PRO; PR:Q61212; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q61212; protein.
DR   Bgee; ENSMUSG00000038071; Expressed in seminal vesicle and 19 other tissues.
DR   Genevisible; Q61212; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR   GO; GO:0008188; F:neuropeptide receptor activity; IBA:GO_Central.
DR   GO; GO:0004983; F:neuropeptide Y receptor activity; IDA:MGI.
DR   GO; GO:0001601; F:peptide YY receptor activity; IDA:MGI.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000986; NeuroY6_rcpt.
DR   InterPro; IPR000611; NPY_rcpt.
DR   PANTHER; PTHR24235:SF16; PTHR24235:SF16; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01017; NRPEPTIDEY6R.
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   Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..371
FT                   /note="Neuropeptide Y receptor type 6"
FT                   /id="PRO_0000069943"
FT   TOPO_DOM        1..31
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..82
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..111
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..150
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        172..206
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        228..263
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        285..297
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..371
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           336
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        11
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        18
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        109..196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   371 AA;  42714 MW;  E4AABB987CEB74B7 CRC64;
     MEVLTNQPTP NKTSGKSNNS AFFYFESCQP PFLAILLLLI AYTVILIMGI FGNLSLIIII
     FKKQREAQNV TNILIANLSL SDILVCVMCI PFTVIYTLMD HWVFGNTMCK LTSYVQSVSV
     SVSIFSLVLI AIERYQLIVN PRGWKPRVAH AYWGIILIWL ISLTLSIPLF LSYHLTNEPF
     HNLSLPTDIY THQVACVEIW PSKLNQLLFS TSLFMLQYFV PLGFILICYL KIVLCLRKRT
     RQVDRRKENK SRLNENKRVN VMLISIVVTF GACWLPLNIF NVIFDWYHEM LMSCHHDLVF
     VVCHLIAMVS TCINPLFYGF LNKNFQKDLM MLIHHCWCGE PQESYENIAM STMHTDESKG
     SLKLAHIPTG I
 
 
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