NPY1R_CANLF
ID NPY1R_CANLF Reviewed; 382 AA.
AC O02813;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Neuropeptide Y receptor type 1;
DE Short=NPY1-R;
GN Name=NPY1R;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
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; AF005778; AAC08046.1; -; mRNA.
DR RefSeq; NP_001002930.1; NM_001002930.1.
DR RefSeq; XP_005628870.1; XM_005628813.1.
DR RefSeq; XP_005628871.1; XM_005628814.1.
DR RefSeq; XP_005628872.1; XM_005628815.2.
DR RefSeq; XP_005628874.1; XM_005628817.1.
DR RefSeq; XP_005628877.1; XM_005628820.2.
DR AlphaFoldDB; O02813; -.
DR SMR; O02813; -.
DR STRING; 9615.ENSCAFP00000012917; -.
DR PaxDb; O02813; -.
DR Ensembl; ENSCAFT00030035362; ENSCAFP00030030844; ENSCAFG00030019229.
DR Ensembl; ENSCAFT00040010410; ENSCAFP00040009036; ENSCAFG00040005550.
DR Ensembl; ENSCAFT00845011414; ENSCAFP00845008915; ENSCAFG00845006432.
DR GeneID; 399518; -.
DR KEGG; cfa:399518; -.
DR CTD; 4886; -.
DR VEuPathDB; HostDB:ENSCAFG00845006432; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000160268; -.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; O02813; -.
DR OMA; KRNNMMD; -.
DR OrthoDB; 609835at2759; -.
DR TreeFam; TF315303; -.
DR Reactome; R-CFA-375276; Peptide ligand-binding receptors.
DR Reactome; R-CFA-418594; G alpha (i) signalling events.
DR Proteomes; UP000002254; Chromosome 15.
DR Bgee; ENSCAFG00000008791; Expressed in spleen and 47 other tissues.
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:0001602; F:pancreatic polypeptide receptor activity; IEA:Ensembl.
DR GO; GO:0001601; F:peptide YY receptor activity; IEA:Ensembl.
DR GO; GO:0007631; P:feeding behavior; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
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..382
FT /note="Neuropeptide Y receptor type 1"
FT /id="PRO_0000069918"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21555"
FT LIPID 337
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 CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 112..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 382 AA; 44245 MW; 95B57D20D6299803 CRC64;
MNSTSFSQVE NHSIFCNFSE NSQFLAFESD DCHLPLAMIF TLALAYGAVI ILGVTGNLAL
IMIILKQKEM RNVTNILIVN LSFSDLLVAI MCLPFTFVYT LMDHWVFGEA MCKLNPFVQC
VSITVSIFSL VLIAVERHQL IINPRGWRPN NRHAYVGIAV IWVLAVVSSL PFLIYQVLTD
EPFQNVTLDA FKDKYVCFDK FPSDSHRLSY TTLLLMLQYF GPLCFIFICY FKIYIRLKRR
NNMMDKMRDN KYRSSETKRI NIMLLSIVVA FAVCWLPLTI FNTVFDWNHQ IIATCNHNLL
FLLCHLTAMI STCVNPIFYG FLNKNFQRDL QFFFNFCDFR SRDDDYETIA MSTMHTDVSK
TSLKQASPVA FKKINNDDNE KI
