NPY2R_PIG
ID NPY2R_PIG Reviewed; 382 AA.
AC O02836; Q9TSI1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 116.
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 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=Spleen;
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 SEQUENCE REVISION TO 207.
RA Ekstrand A.J.;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11287083; DOI=10.1016/s0196-9781(01)00331-x;
RA Larhammar D., Wraith A., Berglund M.M., Holmberg S.K., Lundell I.;
RT "Origins of the many NPY-family receptors in mammals.";
RL Peptides 22:295-307(2001).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAD13777.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF005780; AAC26670.2; -; mRNA.
DR EMBL; AF106082; AAD13777.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_999315.1; NM_214150.1.
DR AlphaFoldDB; O02836; -.
DR SMR; O02836; -.
DR STRING; 9823.ENSSSCP00000009597; -.
DR PaxDb; O02836; -.
DR PRIDE; O02836; -.
DR GeneID; 397291; -.
DR KEGG; ssc:397291; -.
DR CTD; 4887; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; O02836; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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..382
FT /note="Neuropeptide Y receptor type 2"
FT /id="PRO_0000069932"
FT TOPO_DOM 1..46
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..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..125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 343
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 124..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 4
FT /note="I -> L (in Ref. 3; AAD13777)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="L -> V (in Ref. 3; AAD13777)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="I -> N (in Ref. 3; AAD13777)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="A -> V (in Ref. 3; AAD13777)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 42557 MW; 5C01FAF3A0423858 CRC64;
MGPIGAEADE NQTVEEMKME PSGPGHTTPR GELAPDSEPE LKDSTKLIEV QIILILAYCS
IILLGVVGNS LVIHVVIKFK SMRTVTNFFI ANLAVADLLV NTLCLPFTLT YTLMGEWKMG
PVLCHLVPYA QGLAVQVSTI TLTVIALDRH RCIVYHLESK ISKRISFLII GLAWGISALL
ASPLAIFREY SLIEIIPDFE IVACTEKWPG EEKSIYGTVY SLSSLLILYV LPLGIISFSY
ARIWSKLKNH VSPGGVNDHY HQRRQKTTKM LVCVVVVFAV SWLPLHAFQL AVDIDSQVLD
LKEYKLIFTV FHIIAMCSTF ANPLLYGWMN SNYRKAFLSA FRCEQRLDAI HSEVSMTSKA
KKNLEATKNG GPDDSFTEAT NV
