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GHSR_MUSPF
ID   GHSR_MUSPF              Reviewed;         366 AA.
AC   A5A4L1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Growth hormone secretagogue receptor type 1;
DE            Short=GHS-R;
DE   AltName: Full=GH-releasing peptide receptor;
DE            Short=GHRP;
DE   AltName: Full=Ghrelin receptor;
GN   Name=GHSR;
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC   Mustela.
OX   NCBI_TaxID=9669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   van der Keyl H.K.;
RT   "Ghrelin receptor orthologs.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for ghrelin, coupled to G-alpha-11 proteins.
CC       Stimulates growth hormone secretion. Binds also other growth hormone
CC       releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as
CC       non-peptide, low molecular weight secretagogues (e.g. L-692,429, MK-
CC       0677, adenosine) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; EF526307; ABP88931.1; -; mRNA.
DR   RefSeq; NP_001297094.1; NM_001310165.1.
DR   AlphaFoldDB; A5A4L1; -.
DR   SMR; A5A4L1; -.
DR   STRING; 9669.ENSMPUP00000017053; -.
DR   Ensembl; ENSMPUT00000017307; ENSMPUP00000017053; ENSMPUG00000017162.
DR   GeneID; 101675017; -.
DR   CTD; 2693; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244813; -.
DR   HOGENOM; CLU_009579_6_5_1; -.
DR   InParanoid; A5A4L1; -.
DR   OMA; MVWTSSI; -.
DR   Proteomes; UP000000715; Unassembled WGS sequence.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001616; F:growth hormone secretagogue receptor activity; IEA:Ensembl.
DR   GO; GO:0016520; F:growth hormone-releasing hormone receptor activity; IEA:Ensembl.
DR   GO; GO:0008154; P:actin polymerization or depolymerization; IEA:Ensembl.
DR   GO; GO:0008343; P:adult feeding behavior; IEA:Ensembl.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR   GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR   GO; GO:0030252; P:growth hormone secretion; IEA:Ensembl.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IEA:Ensembl.
DR   GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
DR   GO; GO:0032100; P:positive regulation of appetite; IEA:Ensembl.
DR   GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0051963; P:regulation of synapse assembly; IEA:Ensembl.
DR   GO; GO:0032094; P:response to food; IEA:Ensembl.
DR   InterPro; IPR039129; 7tmA_GHSR.
DR   InterPro; IPR003905; GHS-R/MTLR.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24243:SF7; PTHR24243:SF7; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01417; GHSRECEPTOR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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..366
FT                   /note="Growth hormone secretagogue receptor type 1"
FT                   /id="PRO_0000310945"
FT   TOPO_DOM        1..40
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..66
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        67..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..96
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..117
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..139
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        140..162
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..211
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..235
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        236..263
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..285
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        286..302
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..326
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        327..366
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        13
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        116..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   366 AA;  41223 MW;  43A2C5814C93ED62 CRC64;
     MWNATLSEEP GYNLTLPDLG WDAPADNDSL TDELLPLFPA PLLAGVTATC VALFVVGIAG
     NLLTMLVVSR FRELRTTTNL YLSSMAFSDL LIFLCMPLDL VRLWQYRPWN FGDLLCKLFQ
     FVSESCTYAT VLTITALSVE RYFAICFPLR AKVVVTKGRV KLVILVIWAV AFCSAGPIFV
     LVGVEHENGT DPRDTNECRA TEFAVRSGLL TVMVWVSSVF FFLPVFCLTV LYSLIGRKLW
     RRKRGEAAVG ASLRDQNHKQ TVKMLAVVVF AFILCWLPFH VGRYLFSKSF EPGSLEIAQI
     SQYCNLVSFV LFYLSAAINP ILYNIMSKKY RVAVFKLLGF EPFSQRKLST LKDESSRAWT
     ETSINT
 
 
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