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NPFF1_RAT
ID   NPFF1_RAT               Reviewed;         432 AA.
AC   Q9EP86;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 124.
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   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], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain stem;
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Hypothalamus;
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   [3]
RP   PROTEIN SEQUENCE OF 185-194, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
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   -!- TISSUE SPECIFICITY: Expressed at high levels in the hypothalamus.
CC       Moderate levels found in the midbrain, thalamus, medulla oblongata,
CC       testis, eye, whole brain, cerebral cortex, striatum, hippocampus,
CC       cerebellum, optic nerve, placenta, spinal cord, pituitary gland and
CC       ovary. {ECO:0000269|PubMed:11025660}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AB040103; BAB17676.1; -; mRNA.
DR   EMBL; AF268901; AAG41400.1; -; mRNA.
DR   AlphaFoldDB; Q9EP86; -.
DR   SMR; Q9EP86; -.
DR   STRING; 10116.ENSRNOP00000000675; -.
DR   BindingDB; Q9EP86; -.
DR   ChEMBL; CHEMBL4571; -.
DR   GlyGen; Q9EP86; 4 sites.
DR   PhosphoSitePlus; Q9EP86; -.
DR   PaxDb; Q9EP86; -.
DR   UCSC; RGD:621570; rat.
DR   RGD; 621570; Npffr1.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q9EP86; -.
DR   PhylomeDB; Q9EP86; -.
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:Q9EP86; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005929; C:cilium; ISO:RGD.
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: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; Direct protein sequencing; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..432
FT                   /note="Neuropeptide FF receptor 1"
FT                   /id="PRO_0000069914"
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..273
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        295..309
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        331..432
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          380..422
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        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"
SQ   SEQUENCE   432 AA;  48324 MW;  827325849444C408 CRC64;
     MEAEPSQPPN GSWPLGQNGS DVETSMATSL TFSSYYQHSS PVAAMFIAAY VLIFLLCMVG
     NTLVCFIVLK NRHMRTVTNM FILNLAVSDL LVGIFCMPTT LVDNLITGWP FDNATCKMSG
     LVQGMSVSAS VFTLVAIAVE RFRCIVHPFR EKLTLRKALF TIAVIWALAL LIMCPSAVTL
     TVTREEHHFM LDARNRSYPL YSCWEAWPEK GMRKVYTAVL FAHIYLVPLA LIVVMYVRIA
     RKLCQAPGPA RDTEEAVAEG GRTSRRRARV VHMLVMVALF FTLSWLPLWV LLLLIDYGEL
     SELQLHLLSV YAFPLAHWLA FFHSSANPII YGYFNENFRR GFQAAFRAQL CWPPWAAHKQ
     AYSERPNRLL RRRVVVDVQP SDSGLPSESG PSSGVPGPGR LPLRNGRVAH QDGPGEGPGC
     NHMPLTIPAW NI
 
 
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