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GLP2R_HUMAN
ID   GLP2R_HUMAN             Reviewed;         553 AA.
AC   O95838; Q4VAT3;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 158.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Stomach;
RX   PubMed=9990065; DOI=10.1073/pnas.96.4.1569;
RA   Munroe D.G., Gupta A.K., Kooshesh F., Vyas T.B., Rizkalla G., Wang H.,
RA   Demchyshyn L., Yang Z.-H., Kamboj R.K., Chen H., McCallum K.,
RA   Sumner-Smith M., Drucker D.J., Crivici A.;
RT   "Prototypic G protein-coupled receptor for the intestinotrophic factor
RT   glucagon-like peptide 2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:1569-1573(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-470.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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.
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; AF105367; AAD16895.1; -; mRNA.
DR   EMBL; BC096262; AAH96262.1; -; mRNA.
DR   CCDS; CCDS11150.1; -.
DR   RefSeq; NP_004237.1; NM_004246.2.
DR   PDB; 7D68; EM; 3.00 A; R=1-490.
DR   PDBsum; 7D68; -.
DR   AlphaFoldDB; O95838; -.
DR   SMR; O95838; -.
DR   BioGRID; 114746; 2.
DR   IntAct; O95838; 1.
DR   MINT; O95838; -.
DR   STRING; 9606.ENSP00000262441; -.
DR   BindingDB; O95838; -.
DR   ChEMBL; CHEMBL5844; -.
DR   DrugBank; DB00040; Glucagon.
DR   DrugBank; DB08900; Teduglutide.
DR   DrugCentral; O95838; -.
DR   GuidetoPHARMACOLOGY; 250; -.
DR   GlyGen; O95838; 4 sites.
DR   iPTMnet; O95838; -.
DR   PhosphoSitePlus; O95838; -.
DR   BioMuta; GLP2R; -.
DR   MassIVE; O95838; -.
DR   PaxDb; O95838; -.
DR   PeptideAtlas; O95838; -.
DR   PRIDE; O95838; -.
DR   ProteomicsDB; 51084; -.
DR   Antibodypedia; 12679; 375 antibodies from 34 providers.
DR   DNASU; 9340; -.
DR   Ensembl; ENST00000262441.10; ENSP00000262441.5; ENSG00000065325.13.
DR   GeneID; 9340; -.
DR   KEGG; hsa:9340; -.
DR   MANE-Select; ENST00000262441.10; ENSP00000262441.5; NM_004246.3; NP_004237.1.
DR   UCSC; uc002gmd.2; human.
DR   CTD; 9340; -.
DR   DisGeNET; 9340; -.
DR   GeneCards; GLP2R; -.
DR   HGNC; HGNC:4325; GLP2R.
DR   HPA; ENSG00000065325; Tissue enhanced (gallbladder, intestine, urinary bladder).
DR   MIM; 603659; gene.
DR   neXtProt; NX_O95838; -.
DR   OpenTargets; ENSG00000065325; -.
DR   PharmGKB; PA28726; -.
DR   VEuPathDB; HostDB:ENSG00000065325; -.
DR   eggNOG; KOG4564; Eukaryota.
DR   GeneTree; ENSGT00940000158127; -.
DR   HOGENOM; CLU_002753_4_0_1; -.
DR   InParanoid; O95838; -.
DR   OMA; STDIWRD; -.
DR   OrthoDB; 651627at2759; -.
DR   PhylomeDB; O95838; -.
DR   TreeFam; TF315710; -.
DR   PathwayCommons; O95838; -.
DR   Reactome; R-HSA-418555; G alpha (s) signalling events.
DR   Reactome; R-HSA-420092; Glucagon-type ligand receptors.
DR   Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR   SignaLink; O95838; -.
DR   BioGRID-ORCS; 9340; 15 hits in 1072 CRISPR screens.
DR   GeneWiki; Glucagon-like_peptide_2_receptor; -.
DR   GenomeRNAi; 9340; -.
DR   Pharos; O95838; Tclin.
DR   PRO; PR:O95838; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; O95838; protein.
DR   Bgee; ENSG00000065325; Expressed in colonic epithelium and 84 other tissues.
DR   ExpressionAtlas; O95838; baseline and differential.
DR   Genevisible; O95838; HS.
DR   GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
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:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR   GO; GO:0004967; F:glucagon receptor activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
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   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..553
FT                   /note="Glucagon-like peptide 2 receptor"
FT                   /id="PRO_0000012838"
FT   TOPO_DOM        1..173
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        174..198
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        199..210
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        211..235
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        236..261
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        262..285
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        286..299
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        300..321
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        322..339
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        340..362
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        363..386
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        387..405
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        406..417
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        418..438
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        439..550
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        97
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        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..105
FT                   /evidence="ECO:0000250"
FT   DISULFID        96..137
FT                   /evidence="ECO:0000250"
FT   DISULFID        118..159
FT                   /evidence="ECO:0000250"
FT   VARIANT         22
FT                   /note="H -> L (in dbSNP:rs8072568)"
FT                   /id="VAR_033967"
FT   VARIANT         470
FT                   /note="D -> N (in dbSNP:rs17681684)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_033968"
FT   VARIANT         523
FT                   /note="R -> H (in dbSNP:rs16958918)"
FT                   /id="VAR_033969"
FT   HELIX           167..202
FT                   /evidence="ECO:0007829|PDB:7D68"
FT   HELIX           209..238
FT                   /evidence="ECO:0007829|PDB:7D68"
FT   HELIX           253..256
FT                   /evidence="ECO:0007829|PDB:7D68"
FT   HELIX           259..287
FT                   /evidence="ECO:0007829|PDB:7D68"
FT   STRAND          290..292
FT                   /evidence="ECO:0007829|PDB:7D68"
FT   TURN            300..302
FT                   /evidence="ECO:0007829|PDB:7D68"
FT   HELIX           303..307
FT                   /evidence="ECO:0007829|PDB:7D68"
FT   HELIX           312..324
FT                   /evidence="ECO:0007829|PDB:7D68"
FT   STRAND          336..338
FT                   /evidence="ECO:0007829|PDB:7D68"
FT   HELIX           341..370
FT                   /evidence="ECO:0007829|PDB:7D68"
FT   HELIX           376..394
FT                   /evidence="ECO:0007829|PDB:7D68"
FT   HELIX           399..403
FT                   /evidence="ECO:0007829|PDB:7D68"
FT   HELIX           412..436
FT                   /evidence="ECO:0007829|PDB:7D68"
FT   TURN            437..439
FT                   /evidence="ECO:0007829|PDB:7D68"
FT   HELIX           441..451
FT                   /evidence="ECO:0007829|PDB:7D68"
SQ   SEQUENCE   553 AA;  63001 MW;  DA37379DF774A8F4 CRC64;
     MKLGSSRAGP GRGSAGLLPG VHELPMGIPA PWGTSPLSFH RKCSLWAPGR PFLTLVLLVS
     IKQVTGSLLE ETTRKWAQYK QACLRDLLKE PSGIFCNGTF DQYVCWPHSS PGNVSVPCPS
     YLPWWSEESS GRAYRHCLAQ GTWQTIENAT DIWQDDSECS ENHSFKQNVD RYALLSTLQL
     MYTVGYSFSL ISLFLALTLL LFLRKLHCTR NYIHMNLFAS FILRTLAVLV KDVVFYNSYS
     KRPDNENGWM SYLSEMSTSC RSVQVLLHYF VGANYLWLLV EGLYLHTLLE PTVLPERRLW
     PRYLLLGWAF PVLFVVPWGF ARAHLENTGC WTTNGNKKIW WIIRGPMMLC VTVNFFIFLK
     ILKLLISKLK AHQMCFRDYK YRLAKSTLVL IPLLGVHEIL FSFITDDQVE GFAKLIRLFI
     QLTLSSFHGF LVALQYGFAN GEVKAELRKY WVRFLLARHS GCRACVLGKD FRFLGKCPKK
     LSEGDGAEKL RKLQPSLNSG RLLHLAMRGL GELGAQPQQD HARWPRGSSL SECSEGDVTM
     ANTMEEILEE SEI
 
 
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