ID   NPY1R_XENLA             Reviewed;         366 AA.
AC   P34992;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Neuropeptide Y receptor type 1;
DE            Short=NPY1-R;
GN   Name=npy1r;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hypothalamus;
RX   PubMed=7742373; DOI=10.1016/0167-4781(95)00051-h;
RA   Blomqvist A.G., Roubos E.W., Larhammar D., Martens G.J.M.;
RT   "Cloning and sequence analysis of a neuropeptide Y/peptide YY receptor Y1
RT   cDNA from Xenopus laevis.";
RL   Biochim. Biophys. Acta 1261:439-441(1995).
CC   -!- FUNCTION: Receptor for neuropeptide Y and peptide YY.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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; L25416; AAA49918.1; -; mRNA.
DR   PIR; S71152; S71152.
DR   RefSeq; NP_001079348.1; NM_001085879.1.
DR   AlphaFoldDB; P34992; -.
DR   SMR; P34992; -.
DR   GeneID; 378693; -.
DR   KEGG; xla:378693; -.
DR   CTD; 378693; -.
DR   Xenbase; XB-GENE-6252364; npy2r.S.
DR   OrthoDB; 609835at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 378693; Expressed in brain and 1 other tissue.
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:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000351; NPY1_rcpt.
DR   InterPro; IPR000611; NPY_rcpt.
DR   PANTHER; PTHR24235:SF24; PTHR24235:SF24; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01013; NRPEPTIDEY1R.
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; Phosphoprotein; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..366
FT                   /note="Neuropeptide Y receptor type 1"
FT                   /id="PRO_0000069925"
FT   TOPO_DOM        1..39
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        61..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..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        171..203
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        225..260
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        282..294
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..315
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        316..366
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           333
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        9
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        15
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        108..193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   366 AA;  42253 MW;  B82C3C19A603FC67 CRC64;
     MNFSTYFENL SVPNNISGNI TFPISEDCAL PLPMIFTLAL AYGAVIILGL SGNLALIIII
     LKQKEMRNVT NILIVNLSFS DLLATIMCLP FTLIYTLMDH WIFGEVMCKL NEYIQCVSVT
     VSIFSLVLIA IERHQLIINP RGWRPNNRHA CFGITVIWGF AMACSTPLMM YSVLTDEPFK
     NISLDSYIGK YVCLEDFPED KFRLSYTTLL FILQYLGPLC FIFVCYTKIF LRLKRRNNMM
     DKIRDNKYRS SETKRINIML LSIVVGFALC WLPFFIFNLV FDWNHEAVAT CNHNLLFLIC
     HLTAMISTCV NPIFYGFLNK NFQRDLQFFF NFCDFRSRED DYETIAMSTM HTDVSKTSLK
     QASPIA