NPFF2_RAT
ID NPFF2_RAT Reviewed; 417 AA.
AC Q9EQD2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Neuropeptide FF receptor 2;
DE AltName: Full=G-protein coupled receptor 74;
DE AltName: Full=Neuropeptide G-protein coupled receptor;
GN Name=Npffr2; Synonyms=Gpr74, Npff2, Npgpr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=11024015; DOI=10.1074/jbc.m004385200;
RA Bonini J.A., Jones K.A., Adham N., Forray C., Artymyshyn R., Durkin M.M.,
RA Smith K.E., Tamm J.A., Boteju L.W., Lakhlani P.P., Raddatz R., Yao W.-J.,
RA Ogozalek K.L., Boyle N., Kouranova E.V., Quan Y., Vaysse P.J., Wetzel J.M.,
RA Branchek T.A., Gerald C., Borowsky B.;
RT "Identification and characterization of two G protein-coupled receptors for
RT neuropeptide FF.";
RL J. Biol. Chem. 275:39324-39331(2000).
CC -!- FUNCTION: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide)
CC neuropeptides, also known as morphine-modulating peptides. Can also be
CC activated by a variety of naturally occurring or synthetic FMRF-amide
CC like ligands. This receptor mediates its action by association with G
CC proteins that activate a phosphatidylinositol-calcium second messenger
CC system.
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; AF268900; AAG41399.1; -; mRNA.
DR RefSeq; NP_076470.1; NM_023980.1.
DR RefSeq; XP_006250849.1; XM_006250787.3.
DR RefSeq; XP_017454875.1; XM_017599386.1.
DR AlphaFoldDB; Q9EQD2; -.
DR SMR; Q9EQD2; -.
DR STRING; 10116.ENSRNOP00000004153; -.
DR BindingDB; Q9EQD2; -.
DR ChEMBL; CHEMBL3425; -.
DR GlyGen; Q9EQD2; 4 sites.
DR PhosphoSitePlus; Q9EQD2; -.
DR PaxDb; Q9EQD2; -.
DR Ensembl; ENSRNOT00000004153; ENSRNOP00000004153; ENSRNOG00000003067.
DR GeneID; 78964; -.
DR KEGG; rno:78964; -.
DR UCSC; RGD:620168; rat.
DR CTD; 10886; -.
DR RGD; 620168; Npffr2.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230390; -.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; Q9EQD2; -.
DR OMA; FKMTVPH; -.
DR OrthoDB; 1308959at2759; -.
DR PhylomeDB; Q9EQD2; -.
DR TreeFam; TF315303; -.
DR Reactome; R-RNO-389397; Orexin and neuropeptides FF and QRFP bind to their respective receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:Q9EQD2; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000003067; Expressed in heart and 2 other tissues.
DR Genevisible; Q9EQD2; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0008188; F:neuropeptide receptor activity; IEA:InterPro.
DR GO; GO:0031628; F:opioid receptor binding; IEA:InterPro.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0045761; P:regulation of adenylate cyclase activity; IEA:InterPro.
DR GO; GO:2000479; P:regulation of cAMP-dependent protein kinase activity; IEA:InterPro.
DR GO; GO:0043408; P:regulation of MAPK cascade; IEA:InterPro.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR005395; NPFF_rcpt.
DR InterPro; IPR005397; NPFF_rcpt_2.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01570; NPFFRECEPTOR.
DR PRINTS; PR01572; NPFFRECEPTR2.
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 Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..417
FT /note="Neuropeptide FF receptor 2"
FT /id="PRO_0000069917"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..119
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..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..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 378..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 118..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 417 AA; 47711 MW; DFEB6AC63AF2AAD6 CRC64;
MGKRWDSNSS GSWDHIWSGN DTQHPWYSDI NITYMNYYLH QPHVTAVFIS SYFLIFFLCM
VGNTVVCFVV IRNRYMHTVT NFFIFNLAIS DLLVGIFCMP ITLLDNIIAG WPFGSSMCKI
SGLVQGISVA ASVFTLVAIA VDRFRCVVYP FKPKLTVKTA FVMIVIIWGL AITIMTPSAI
MLHVQEEKYY RVRLSSHNKT STVYWCREDW PNQEMRRIYT TVLFATIYLA PLSLIVIMYA
RIGASLFKTS AHSTGKQRLE QWHVSKKKQK VIKMLLTVAL LFILSWLPLW TLMMLSDYAD
LSPNKLRVIN IYVYPFAHWL AFCNSSVNPI IYGFFNENFR SGFQDAFQFC QKKVKPQEAY
GLRAKRNLDI NTSGLLVHEP ASQNPSGENL GCRKSADNPT QESLMEETGE ATNSTET
