NPY1R_PIG
ID NPY1R_PIG Reviewed; 383 AA.
AC O02835;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Neuropeptide Y receptor type 1;
DE Short=NPY1-R;
GN Name=NPY1R;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Hypothalamus;
RX PubMed=9802394; DOI=10.1016/s0167-0115(98)00053-6;
RA Malmstroem R.E., Hoekfelt T., Bjoerkman J.-A., Nihlen C., Bystroem M.,
RA Ekstrand A.J., Lundberg J.M.;
RT "Characterization and molecular cloning of vascular neuropeptide Y receptor
RT subtypes in pig and dog.";
RL Regul. Pept. 75:55-70(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wraith A., Tornsten A., Chardon P., Harbitz I., Chowdhary B.P.,
RA Andersson L., Larhammar D.;
RT "Porcine NPY receptors NPY1R, NPY2R and NPY5R: cloning, mapping and
RT comparative analysis.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AF005779; AAC26836.1; -; mRNA.
DR EMBL; AF106081; AAD13776.2; -; Genomic_DNA.
DR RefSeq; NP_999453.1; NM_214288.1.
DR RefSeq; XP_005666733.1; XM_005666676.2.
DR RefSeq; XP_005666734.1; XM_005666677.2.
DR AlphaFoldDB; O02835; -.
DR SMR; O02835; -.
DR STRING; 9823.ENSSSCP00000009480; -.
DR PaxDb; O02835; -.
DR PRIDE; O02835; -.
DR GeneID; 397547; -.
DR KEGG; ssc:397547; -.
DR CTD; 4886; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; O02835; -.
DR OrthoDB; 609835at2759; -.
DR TreeFam; TF315303; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; O02835; SS.
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; 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..383
FT /note="Neuropeptide Y receptor type 1"
FT /id="PRO_0000069922"
FT TOPO_DOM 1..44
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..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 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"
FT CONFLICT 203
FT /note="L -> P (in Ref. 2; AAD13776)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 44327 MW; 0D58CBCA549B62CF CRC64;
MNSTLSSQVE NHSIYYNFSE KNSQFLAFEN DDCHLPLAMI FTLALAYGAV IILGVSGNLA
LIIIILKQKE MRNVTNILIV NLSFSDLLVA IMCLPFTFVY TLMDHWVFGE VMCKLNPFVQ
CVSITVSIFS LVLIAVERHQ LIINPRGWRP SNRHAYVGIA VIWVLAVASS LPFLIYQVLT
DEPFQNVTLD AFKDKYVCFD KFLSDSHRLS YTTLLLVLQY FGPLCFIFIC YFKIYIRLKR
RNNMMDKMRD NKYRSSETKR INVMLLSIVV AFAVCWLPLT IFNTVFDWNH QIIATCNHNL
LFLLCHLTAM ISTCINPIFY GFLNKNFQRD LQFFFNFCDF RSRDDDYEVI AMSTMHTDVS
KTSLKQASPV ALKKIHSDDN EKI
