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GLP2R_MOUSE
ID   GLP2R_MOUSE             Reviewed;         512 AA.
AC   Q5IXF8; Q5SU65;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Glucagon-like peptide 2 receptor;
DE            Short=GLP-2 receptor;
DE            Short=GLP-2-R;
DE            Short=GLP-2R;
GN   Name=Glp2r;
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].
RC   STRAIN=C57BL/6J; TISSUE=Jejunum;
RA   Estall J.L., Drucker D.J.;
RT   "Murine glucagon-like peptide-2 receptor cDNA.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: This is a receptor for glucagon-like peptide 2. The activity
CC       of this receptor is mediated by G proteins which activate adenylyl
CC       cyclase (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AY605231; AAT46060.1; -; mRNA.
DR   EMBL; AL646097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS24860.1; -.
DR   RefSeq; NP_783612.2; NM_175681.3.
DR   AlphaFoldDB; Q5IXF8; -.
DR   SMR; Q5IXF8; -.
DR   STRING; 10090.ENSMUSP00000061560; -.
DR   GlyGen; Q5IXF8; 1 site.
DR   PhosphoSitePlus; Q5IXF8; -.
DR   PaxDb; Q5IXF8; -.
DR   PRIDE; Q5IXF8; -.
DR   ProteomicsDB; 263368; -.
DR   Antibodypedia; 12679; 375 antibodies from 34 providers.
DR   DNASU; 93896; -.
DR   Ensembl; ENSMUST00000051765; ENSMUSP00000061560; ENSMUSG00000049928.
DR   GeneID; 93896; -.
DR   KEGG; mmu:93896; -.
DR   UCSC; uc007jna.1; mouse.
DR   CTD; 9340; -.
DR   MGI; MGI:2136733; Glp2r.
DR   VEuPathDB; HostDB:ENSMUSG00000049928; -.
DR   eggNOG; KOG4564; Eukaryota.
DR   GeneTree; ENSGT00940000158127; -.
DR   HOGENOM; CLU_002753_4_0_1; -.
DR   InParanoid; Q5IXF8; -.
DR   OMA; STDIWRD; -.
DR   OrthoDB; 651627at2759; -.
DR   PhylomeDB; Q5IXF8; -.
DR   TreeFam; TF315710; -.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR   BioGRID-ORCS; 93896; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Glp2r; mouse.
DR   PRO; PR:Q5IXF8; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5IXF8; protein.
DR   Bgee; ENSMUSG00000049928; Expressed in retinal neural layer and 23 other tissues.
DR   ExpressionAtlas; Q5IXF8; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0004967; F:glucagon receptor activity; ISO:MGI.
DR   GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   Gene3D; 4.10.1240.10; -; 1.
DR   InterPro; IPR039125; GLP2R.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   PANTHER; PTHR45620:SF23; PTHR45620:SF23; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF02793; HRM; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00008; HormR; 1.
DR   SUPFAM; SSF111418; SSF111418; 1.
DR   PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 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..512
FT                   /note="Glucagon-like peptide 2 receptor"
FT                   /id="PRO_0000307111"
FT   TOPO_DOM        1..135
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        136..160
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        161..172
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        173..197
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        198..223
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        224..247
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        248..261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        262..283
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        284..301
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        302..324
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        325..348
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        349..367
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        368..379
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        380..400
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        401..512
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          458..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        43..65
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..119
FT                   /evidence="ECO:0000250"
FT   CONFLICT        263
FT                   /note="P -> H (in Ref. 1; AAT46060)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        459..460
FT                   /note="GV -> AF (in Ref. 1; AAT46060)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        485
FT                   /note="R -> L (in Ref. 1; AAT46060)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   512 AA;  59105 MW;  B7CBEE79F0267867 CRC64;
     MRRLWGPGTP FLALLLLVSI KQVTTGSLLE ETVQKWAQYK ETCLKDLLEK PSGVFCNGTF
     DKYVCWPHSF PGNVSVPCPS YLPWWNKESP GRAYRHCLAQ GTWQKQENST DTWQDESECS
     ENHSFKQNVD HYHHTLLSTL QLMYTVGYSL SLISLFLALT LFLFLRKLHC TRNYIHMNLF
     ASFILRALVV LVKDMVFYNS YSRRPDSESG WMSYLSEISA SCRSVQVLLH YFVGTNHLWL
     LVEGLYLHAL LEPTVLPERR LWPKYLVVGW AFPMLFVIPW IFVRASLENT GCWAVNENKK
     IWWIIRGPIL LCVTVNFFIF LKILKLLISK FRAHQMCFRD YKYRLAKSTL LLILLMGVHE
     FLFTFFTDDQ VQGFSRLIRL FIQLTLSSFH GFLVALQYGF ASREVKAELR KTWGRFLLAR
     HWGCRACVLG KNFRFLGKCS KKLSEGDGAE TLQKLQSSGV SSHLTAGNLR DHGAQPHRGR
     GAWPRASSLS ESSEGDFTLA NTMEEILEES EI
 
 
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