NPFF2_MOUSE
ID NPFF2_MOUSE Reviewed; 417 AA.
AC Q924H0; Q8BKR6;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Neuropeptide FF receptor 2;
DE AltName: Full=G-protein coupled receptor 74;
DE AltName: Full=Neuropeptide NPFF receptor;
GN Name=Npffr2; Synonyms=Gpr74, Npff2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 (By similarity). {ECO:0000250}.
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; AF330054; AAK94198.1; -; mRNA.
DR EMBL; AK050939; BAC34468.1; -; mRNA.
DR CCDS; CCDS19408.1; -.
DR RefSeq; NP_573455.2; NM_133192.3.
DR RefSeq; XP_017176078.1; XM_017320589.1.
DR AlphaFoldDB; Q924H0; -.
DR SMR; Q924H0; -.
DR STRING; 10090.ENSMUSP00000040033; -.
DR ChEMBL; CHEMBL4523416; -.
DR GlyGen; Q924H0; 4 sites.
DR PhosphoSitePlus; Q924H0; -.
DR SwissPalm; Q924H0; -.
DR PaxDb; Q924H0; -.
DR PRIDE; Q924H0; -.
DR ProteomicsDB; 293949; -.
DR Antibodypedia; 3469; 228 antibodies from 27 providers.
DR DNASU; 104443; -.
DR Ensembl; ENSMUST00000048557; ENSMUSP00000040033; ENSMUSG00000035528.
DR GeneID; 104443; -.
DR KEGG; mmu:104443; -.
DR UCSC; uc008yan.1; mouse.
DR CTD; 10886; -.
DR MGI; MGI:1860130; Npffr2.
DR VEuPathDB; HostDB:ENSMUSG00000035528; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230390; -.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; Q924H0; -.
DR OMA; FKMTVPH; -.
DR OrthoDB; 1308959at2759; -.
DR PhylomeDB; Q924H0; -.
DR TreeFam; TF315303; -.
DR Reactome; R-MMU-389397; Orexin and neuropeptides FF and QRFP bind to their respective receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 104443; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Npffr2; mouse.
DR PRO; PR:Q924H0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q924H0; protein.
DR Bgee; ENSMUSG00000035528; Expressed in primary oocyte and 13 other tissues.
DR Genevisible; Q924H0; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; ISS:MGI.
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_0000069916"
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 382..401
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"
FT CONFLICT 89
FT /note="I -> T (in Ref. 1; AAK94198)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="V -> E (in Ref. 1; AAK94198)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="I -> M (in Ref. 1; AAK94198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 47449 MW; BB8D85EF405D5786 CRC64;
MSEKWDSNSS ESWNHIWSGN DTQHHWYSDI NITYVNYYLH QPQVAAVFIS SYLLIFVLCM
VGNTVVCFIV IRNRHMHTVT NFFILNLAIS DLLVGIFCMP ITLLDNIIAG WPFGSSMCKI
SGLVQGISVA ASVFTLVAIA VDRFRCVVYP FKPKLTVKTA FVTIVIIWGL AIAIMTPSAI
MLHVQEEKYY RVRLSSHNKT STVYWCREDW PRHEMRRIYT TVLFATIYLA PLSLIVIMYA
RIGASLFKTA AHCTGKQRPV QWHVSKKKQK VIKMLLTVAL LFILSWLPLW TLMMLSDYTD
LSPNKLRIIN IYIYPFAHWL AFCNSSVNPI IYGFFNENFR NGFQDAFQIC QKKAKPQEAY
SLRAKRNIVI NTSGLLVQEP VSQNPGGENL GCGKSADNPT QESLIEEMGE ATNSTVA
