ID   NPY1R_CAVPO             Reviewed;         383 AA.
AC   Q9WVD0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Neuropeptide Y receptor type 1;
DE            Short=NPY1-R;
GN   Name=NPY1R;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10499421; DOI=10.1016/s0196-9781(99)00098-4;
RA   Berglund M.M., Holmberg S.K.S., Eriksson H., Gedda K., Maffrand J.-P.,
RA   Serradeil-Le Gal C., Chhajlani V., Grundemar L., Larhammar D.;
RT   "The cloned guinea pig neuropeptide Y receptor Y1 conforms to other
RT   mammalian Y1 receptors.";
RL   Peptides 20:1043-1053(1999).
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; AF135061; AAD43060.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9WVD0; -.
DR   SMR; Q9WVD0; -.
DR   STRING; 10141.ENSCPOP00000014934; -.
DR   BindingDB; Q9WVD0; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q9WVD0; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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   3: Inferred from homology;
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..383
FT                   /note="Neuropeptide Y receptor type 1"
FT                   /id="PRO_0000069919"
FT   TOPO_DOM        1..34
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..116
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..211
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        233..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..299
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..320
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..383
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         368
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21555"
FT   MOD_RES         376
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q04573"
FT   LIPID           338
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        11
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        17
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        113..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   383 AA;  44281 MW;  E53B0D93FA735F8E CRC64;
     MNSTSFSQLE NHSVHYNLSE EKPSFFAFEN DDCHLPLAVI FTLALAYGAV IILGVSGNLA
     LILIILKQKE MRNVTNILIV NLSFSDLLVA IMCLPFTFVY TLMDHWIFGE IMCKLNPFVQ
     CVSITVSIFS LVLIAVERHQ LIINPRGWRP NNRHAYIGIA VIWVLAVASS LPFMIYQVLT
     DEPFQNVTLD AFKDKLVCFD QFPSDSHRLS YTTLLLVLQY FGPLCFIFIC YFKIYIRLKR
     RNNMMDKMRD SKYRSSESKR INIMLLSIVV AFAVCWLPLT IFNTVFDWNH QIIATCNHNL
     LFLLCHLTAM ISTCVNPIFY GFLNKNFQRD LQFFFNFCDF RSRDDDYETI AMSTMHTDVS
     KTSLKQASPL AFKKISCVEN EKI