NPFF1_HUMAN
ID NPFF1_HUMAN Reviewed; 430 AA.
AC Q9GZQ6; A2RRF0; Q8NGR0; Q96RN3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Neuropeptide FF receptor 1;
DE AltName: Full=G-protein coupled receptor 147;
DE AltName: Full=RFamide-related peptide receptor OT7T022;
GN Name=NPFFR1; Synonyms=GPR147, NPFF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spinal cord;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11025660; DOI=10.1038/35036326;
RA Hinuma S., Shintani Y., Fukusumi S., Iijima N., Matsumoto Y., Hosoya M.,
RA Fujii R., Watanabe T., Kikuchi K., Terao Y., Yano T., Yamamoto T.,
RA Kawamata Y., Habata Y., Asada M., Kitada C., Kurokawa T., Onda H.,
RA Nishimura O., Tanaka M., Ibata Y., Fujino M.;
RT "New neuropeptides containing carboxy-terminal RFamide and their receptor
RT in mammals.";
RL Nat. Cell Biol. 2:703-708(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Liu Q., Guan X.-M., McDonald T.P., Jiang Q., Zeng Z., Marlene J.,
RA Williams D.L. Jr., Hong Y., Figueroa D., Clements M.K., Mallee J., Wang R.,
RA Evans J., Gould R., Austin C.P.;
RT "Identification and characterization of two cognate receptors for mammalian
RT FMRFamide-like neuropeptides.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spinal cord;
RA Kaighin V.A., Martin A.L., Aronstam R.S.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- INTERACTION:
CC Q9GZQ6; P13637: ATP1A3; NbExp=3; IntAct=EBI-18212103, EBI-948169;
CC Q9GZQ6; P16284: PECAM1; NbExp=3; IntAct=EBI-18212103, EBI-716404;
CC Q9GZQ6; Q8WWU5-7: TCP11; NbExp=3; IntAct=EBI-18212103, EBI-17721485;
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=BAC05950.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF268898; AAG41397.1; -; mRNA.
DR EMBL; AB040104; BAB17677.1; -; mRNA.
DR EMBL; AF330055; AAK94199.1; -; mRNA.
DR EMBL; AB065729; BAC05950.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EU432128; ABY87927.1; -; mRNA.
DR EMBL; BC131580; AAI31581.1; -; mRNA.
DR CCDS; CCDS53539.1; -.
DR RefSeq; NP_071429.1; NM_022146.4.
DR AlphaFoldDB; Q9GZQ6; -.
DR SMR; Q9GZQ6; -.
DR BioGRID; 122064; 1.
DR IntAct; Q9GZQ6; 3.
DR STRING; 9606.ENSP00000277942; -.
DR BindingDB; Q9GZQ6; -.
DR ChEMBL; CHEMBL5951; -.
DR GuidetoPHARMACOLOGY; 300; -.
DR GlyGen; Q9GZQ6; 5 sites.
DR iPTMnet; Q9GZQ6; -.
DR PhosphoSitePlus; Q9GZQ6; -.
DR BioMuta; NPFFR1; -.
DR DMDM; 13878599; -.
DR PaxDb; Q9GZQ6; -.
DR PeptideAtlas; Q9GZQ6; -.
DR PRIDE; Q9GZQ6; -.
DR Antibodypedia; 7444; 182 antibodies from 31 providers.
DR DNASU; 64106; -.
DR Ensembl; ENST00000277942.7; ENSP00000277942.5; ENSG00000148734.8.
DR GeneID; 64106; -.
DR KEGG; hsa:64106; -.
DR MANE-Select; ENST00000277942.7; ENSP00000277942.5; NM_022146.5; NP_071429.1.
DR UCSC; uc021psj.2; human.
DR CTD; 64106; -.
DR DisGeNET; 64106; -.
DR GeneCards; NPFFR1; -.
DR HGNC; HGNC:17425; NPFFR1.
DR HPA; ENSG00000148734; Group enriched (brain, retina).
DR MIM; 607448; gene.
DR neXtProt; NX_Q9GZQ6; -.
DR OpenTargets; ENSG00000148734; -.
DR PharmGKB; PA134934991; -.
DR VEuPathDB; HostDB:ENSG00000148734; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230390; -.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; Q9GZQ6; -.
DR OMA; WGSHREA; -.
DR OrthoDB; 1308959at2759; -.
DR PhylomeDB; Q9GZQ6; -.
DR TreeFam; TF315303; -.
DR PathwayCommons; Q9GZQ6; -.
DR Reactome; R-HSA-389397; Orexin and neuropeptides FF and QRFP bind to their respective receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; Q9GZQ6; -.
DR SIGNOR; Q9GZQ6; -.
DR BioGRID-ORCS; 64106; 9 hits in 1063 CRISPR screens.
DR ChiTaRS; NPFFR1; human.
DR GeneWiki; Neuropeptide_FF_receptor_1; -.
DR GenomeRNAi; 64106; -.
DR Pharos; Q9GZQ6; Tchem.
DR PRO; PR:Q9GZQ6; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9GZQ6; protein.
DR Bgee; ENSG00000148734; Expressed in dorsal motor nucleus of vagus nerve and 80 other tissues.
DR Genevisible; Q9GZQ6; HS.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0008188; F:neuropeptide receptor activity; NAS:UniProtKB.
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 InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR005395; NPFF_rcpt.
DR InterPro; IPR005396; NPFF_rcpt_1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01570; NPFFRECEPTOR.
DR PRINTS; PR01571; NPFFRECEPTR1.
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 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..430
FT /note="Neuropeptide FF receptor 1"
FT /id="PRO_0000069913"
FT TOPO_DOM 1..43
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..307
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 145
FT /note="I -> L (in dbSNP:rs3812694)"
FT /id="VAR_059327"
FT CONFLICT 376
FT /note="V -> A (in Ref. 3; AAK94199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 47819 MW; BBB0146281B2B9A0 CRC64;
MEGEPSQPPN SSWPLSQNGT NTEATPATNL TFSSYYQHTS PVAAMFIVAY ALIFLLCMVG
NTLVCFIVLK NRHMHTVTNM FILNLAVSDL LVGIFCMPTT LVDNLITGWP FDNATCKMSG
LVQGMSVSAS VFTLVAIAVE RFRCIVHPFR EKLTLRKALV TIAVIWALAL LIMCPSAVTL
TVTREEHHFM VDARNRSYPL YSCWEAWPEK GMRRVYTTVL FSHIYLAPLA LIVVMYARIA
RKLCQAPGPA PGGEEAADPR ASRRRARVVH MLVMVALFFT LSWLPLWALL LLIDYGQLSA
PQLHLVTVYA FPFAHWLAFF NSSANPIIYG YFNENFRRGF QAAFRARLCP RPSGSHKEAY
SERPGGLLHR RVFVVVRPSD SGLPSESGPS SGAPRPGRLP LRNGRVAHHG LPREGPGCSH
LPLTIPAWDI
