ID   NPY2R_PANTR             Reviewed;         381 AA.
AC   Q5IS62;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Neuropeptide Y receptor type 2;
DE            Short=NPY2-R;
DE   AltName: Full=NPY-Y2 receptor;
DE            Short=Y2 receptor;
GN   Name=NPY2R;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA   Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA   Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT   "Accelerated evolution of nervous system genes in the origin of Homo
RT   sapiens.";
RL   Cell 119:1027-1040(2004).
CC   -!- FUNCTION: Receptor for neuropeptide Y and peptide YY. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AY665266; AAV74304.1; -; mRNA.
DR   RefSeq; NP_001012655.1; NM_001012637.1.
DR   RefSeq; XP_009446710.1; XM_009448435.2.
DR   RefSeq; XP_009446711.1; XM_009448436.2.
DR   AlphaFoldDB; Q5IS62; -.
DR   BMRB; Q5IS62; -.
DR   SMR; Q5IS62; -.
DR   STRING; 9598.ENSPTRP00000028393; -.
DR   PaxDb; Q5IS62; -.
DR   GeneID; 461562; -.
DR   KEGG; ptr:461562; -.
DR   CTD; 4887; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   HOGENOM; CLU_009579_6_1_1; -.
DR   InParanoid; Q5IS62; -.
DR   OrthoDB; 746515at2759; -.
DR   TreeFam; TF315303; -.
DR   Proteomes; UP000002277; Unplaced.
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   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001358; NPY2_rcpt.
DR   InterPro; IPR000611; NPY_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01014; NRPEPTIDEY2R.
DR   PRINTS; PR01012; NRPEPTIDEYR.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
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..381
FT                   /note="Neuropeptide Y receptor type 2"
FT                   /id="PRO_0000069931"
FT   TOPO_DOM        1..51
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..124
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        146..165
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..216
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        238..268
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..304
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        326..381
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           342
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        11
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        123..203
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   381 AA;  42731 MW;  7D018C0169597BC7 CRC64;
     MGPIGAEADE NQTVEEMKVE QYGPQTTPRG ELVPDPEPEL IDSTKLIEVQ VVLILAYCSI
     ILLGVIGNSL VIHVVIKFKS MRTVTNFFIA NLAVADLLVN TLCLPFTLTY TLMGEWKMGP
     VLCHLVPYAQ GLAVQVSTIT LTVIALDRHR CIVYHLESKI SKRISFLIIG LAWGISALLA
     SPLAIFREYS LIEIIPDFEI VACTEKWPGE EKSIYGTVYS LSSLLILYVL PLGIISFSYT
     RIWSKLKNHV SPGAANDHYH QRRQKTTKML VCVVVVFAVS WLPLHAFQLA VDIDSQVLDL
     KEYKLIFTVF HIIAMCSTFA NPLLYGWMNS NYRKAFLSAF RCEQRLDAIH SEVSVTFKAK
     KNLEVRKNSG PNDSFTEATN V