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GALR1_RAT
ID   GALR1_RAT               Reviewed;         346 AA.
AC   Q62805;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Galanin receptor type 1;
DE            Short=GAL1-R;
DE            Short=GALR-1;
GN   Name=Galr1; Synonyms=Galnr, Galnr1;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Insulinoma;
RX   PubMed=8750821; DOI=10.1016/0169-328x(95)00159-p;
RA   Parker E.M., Izzarelli D.G., Nowak H.P., Mahle C.D., Iben L.G., Wang J.,
RA   Goldstein M.E.;
RT   "Cloning and characterization of the rat GALR1 galanin receptor from Rin14B
RT   insulinoma cells.";
RL   Brain Res. Mol. Brain Res. 34:179-189(1995).
CC   -!- FUNCTION: Receptor for the hormone galanin. The activity of this
CC       receptor is mediated by G proteins that inhibit adenylate cyclase
CC       activity. {ECO:0000250|UniProtKB:P47211, ECO:0000269|PubMed:8750821}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Spinal cord, small intestine, Rin14B insulinoma
CC       cells and several brain regions, particularly ventral hippocampus,
CC       amygdala, supraoptic nucleus, hypothalamus, thalamus, lateral
CC       parabrachial nucleus and locus coeruleus. {ECO:0000269|PubMed:8750821}.
CC   -!- PTM: Three cysteine residues are found in the C-terminus, at least one
CC       of which may be palmitoylated.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U30290; AAC52438.1; -; mRNA.
DR   RefSeq; NP_037090.2; NM_012958.3.
DR   AlphaFoldDB; Q62805; -.
DR   SMR; Q62805; -.
DR   STRING; 10116.ENSRNOP00000022400; -.
DR   BindingDB; Q62805; -.
DR   ChEMBL; CHEMBL5504; -.
DR   GuidetoPHARMACOLOGY; 243; -.
DR   GlyGen; Q62805; 3 sites.
DR   PhosphoSitePlus; Q62805; -.
DR   PaxDb; Q62805; -.
DR   Ensembl; ENSRNOT00000022401; ENSRNOP00000022400; ENSRNOG00000016654.
DR   GeneID; 50577; -.
DR   KEGG; rno:50577; -.
DR   CTD; 2587; -.
DR   RGD; 2656; Galr1.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244841; -.
DR   HOGENOM; CLU_009579_6_4_1; -.
DR   InParanoid; Q62805; -.
DR   OMA; LPHHIIH; -.
DR   OrthoDB; 1294084at2759; -.
DR   PhylomeDB; Q62805; -.
DR   TreeFam; TF315737; -.
DR   Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   PRO; PR:Q62805; -.
DR   Proteomes; UP000002494; Chromosome 18.
DR   Bgee; ENSRNOG00000016654; Expressed in jejunum and 5 other tissues.
DR   Genevisible; Q62805; RN.
DR   GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0004966; F:galanin receptor activity; IDA:RGD.
DR   GO; GO:0042923; F:neuropeptide binding; IDA:RGD.
DR   GO; GO:0017046; F:peptide hormone binding; ISS:UniProtKB.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:RGD.
DR   GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IEA:InterPro.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0051464; P:positive regulation of cortisol secretion; ISO:RGD.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   InterPro; IPR003906; GAL1_rcpt.
DR   InterPro; IPR000405; Galanin_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01418; GALANIN1R.
DR   PRINTS; PR00663; GALANINR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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..346
FT                   /note="Galanin receptor type 1"
FT                   /id="PRO_0000069465"
FT   TOPO_DOM        1..33
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..69
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        91..108
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..130
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        131..150
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        172..196
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        218..246
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        268..269
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        291..346
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          326..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           318
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        7
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        12
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        107..185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   346 AA;  38862 MW;  789FFBE40D1D3805 CRC64;
     MELAPVNLSE GNGSDPEPPA EPRPLFGIGV ENFITLVVFG LIFAMGVLGN SLVITVLARS
     KPGKPRSTTN LFILNLSIAD LAYLLFCIPF QATVYALPTW VLGAFICKFI HYFFTVSMLV
     SIFTLAAMSV DRYVAIVHSR RSSSLRVSRN ALLGVGFIWA LSIAMASPVA YYQRLFHRDS
     NQTFCWEHWP NQLHKKAYVV CTFVFGYLLP LLLICFCYAK VLNHLHKKLK NMSKKSEASK
     KKTAQTVLVV VVVFGISWLP HHVIHLWAEF GAFPLTPASF FFRITAHCLA YSNSSVNPII
     YAFLSENFRK AYKQVFKCRV CNESPHGDAK EKNRIDTPPS TNCTHV
 
 
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