GenomeNet

Database: UniProt
Entry: P63079
LinkDB: P63079
Original site: P63079 
ID   GBRB3_RAT               Reviewed;         473 AA.
AC   P63079; P15433;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   01-OCT-2014, entry version 90.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit beta-3;
DE   AltName: Full=GABA(A) receptor subunit beta-3;
DE   Flags: Precursor;
GN   Name=Gabrb3; Synonyms=Gabrb-3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   SUBUNIT.
RC   TISSUE=Brain;
RX   PubMed=2548852;
RA   Ymer S., Schofield P.R., Draguhn A., Werner P., Koehler M.,
RA   Seeburg P.H.;
RT   "GABAA receptor beta subunit heterogeneity: functional expression of
RT   cloned cDNAs.";
RL   EMBO J. 8:1665-1670(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   SUBUNIT.
RX   PubMed=2540033; DOI=10.1016/0014-5793(89)80271-6;
RA   Lolait S.J., O'Carroll A.-M., Kusano K., Muller J.-M.,
RA   Brownstein M.J., Mahan L.C.;
RT   "Cloning and expression of a novel rat GABAA receptor.";
RL   FEBS Lett. 246:145-148(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8382702;
RA   Kirkness E.F., Fraser C.M.;
RT   "A strong promoter element is located between alternative exons of a
RT   gene encoding the human gamma-aminobutyric acid-type A receptor beta 3
RT   subunit (GABRB3).";
RL   J. Biol. Chem. 268:4420-4428(1993).
RN   [4]
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=9092594;
RA   Tretter V., Ehya N., Fuchs K., Sieghart W.;
RT   "Stoichiometry and assembly of a recombinant GABAA receptor subtype.";
RL   J. Neurosci. 17:2728-2737(1997).
RN   [5]
RP   INTERACTION WITH UBQLN1.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RX   PubMed=11528422; DOI=10.1038/nn0901-908;
RA   Bedford F.K., Kittler J.T., Muller E., Thomas P., Uren J.M., Merlo D.,
RA   Wisden W., Triller A., Smart T.G., Moss S.J.;
RT   "GABA(A) receptor cell surface number and subunit stability are
RT   regulated by the ubiquitin-like protein Plic-1.";
RL   Nat. Neurosci. 4:908-916(2001).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC   -!- FUNCTION: Component of the heteropentameric receptor for GABA, the
CC       major inhibitory neurotransmitter in the vertebrate brain.
CC       Functions also as histamine receptor and mediates cellular
CC       responses to histamine. Functions as receptor for diazepines and
CC       various anesthetics, such as pentobarbital; these are bound at a
CC       separate allosteric effector binding site. Functions as ligand-
CC       gated chloride channel. {ECO:0000269|PubMed:2540033,
CC       ECO:0000269|PubMed:2548852}.
CC   -!- SUBUNIT: Can form functional homopentamers (in vitro) (By
CC       similarity). Binds UBQLN1. Heteropentamer, formed by a combination
CC       of alpha, beta, gamma, delta and rho chains. {ECO:0000250,
CC       ECO:0000269|PubMed:2540033, ECO:0000269|PubMed:2548852,
CC       ECO:0000269|PubMed:9092594}.
CC   -!- INTERACTION:
CC       Q7TSU1:Arfgef2; NbExp=3; IntAct=EBI-6257937, EBI-6257913;
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily.
CC       GABRB3 sub-subfamily. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X15468; CAA33495.1; -; mRNA.
DR   EMBL; L04310; AAA41180.1; -; Genomic_DNA.
DR   PIR; S04466; S04466.
DR   RefSeq; NP_058761.1; NM_017065.1.
DR   UniGene; Rn.233948; -.
DR   ProteinModelPortal; P63079; -.
DR   SMR; P63079; 47-346.
DR   DIP; DIP-60770N; -.
DR   IntAct; P63079; 2.
DR   STRING; 10116.ENSRNOP00000061969; -.
DR   BindingDB; P63079; -.
DR   ChEMBL; CHEMBL2111374; -.
DR   GuidetoPHARMACOLOGY; 412; -.
DR   PaxDb; P63079; -.
DR   PRIDE; P63079; -.
DR   GeneID; 24922; -.
DR   KEGG; rno:24922; -.
DR   UCSC; RGD:2651; rat.
DR   CTD; 2562; -.
DR   RGD; 2651; Gabrb3.
DR   eggNOG; NOG77438; -.
DR   HOGENOM; HOG000231335; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; P63079; -.
DR   KO; K05181; -.
DR   PhylomeDB; P63079; -.
DR   NextBio; 285953; -.
DR   PRO; PR:P63079; -.
DR   Genevestigator; P63079; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:1902711; C:GABA-A receptor complex; ISS:UniProtKB.
DR   GO; GO:0060077; C:inhibitory synapse; IDA:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR   GO; GO:0035612; F:AP-2 adaptor complex binding; IPI:RGD.
DR   GO; GO:0005254; F:chloride channel activity; IDA:RGD.
DR   GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004890; F:GABA-A receptor activity; IDA:RGD.
DR   GO; GO:0022851; F:GABA-gated chloride ion channel activity; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB.
DR   GO; GO:1902476; P:chloride transmembrane transport; IDA:GOC.
DR   GO; GO:0034220; P:ion transmembrane transport; ISS:GOC.
DR   GO; GO:0060021; P:palate development; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IDA:GOC.
DR   GO; GO:0051932; P:synaptic transmission, GABAergic; IDA:RGD.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR006028; GABAA/Glycine_rcpt.
DR   InterPro; IPR002289; GABAAb_rcpt.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   PANTHER; PTHR18945; PTHR18945; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR01160; GABAARBETA.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Chloride; Chloride channel;
KW   Complete proteome; Disulfide bond; Glycoprotein; Ion channel;
KW   Ion transport; Ligand-gated ion channel; Membrane;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
KW   Synapse; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26    473       Gamma-aminobutyric acid receptor subunit
FT                                beta-3.
FT                                /FTId=PRO_0000000464.
FT   TOPO_DOM     26    245       Extracellular. {ECO:0000250}.
FT   TRANSMEM    246    267       Helical. {ECO:0000250}.
FT   TOPO_DOM    268    270       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    271    293       Helical. {ECO:0000250}.
FT   TOPO_DOM    294    304       Extracellular. {ECO:0000250}.
FT   TRANSMEM    305    327       Helical. {ECO:0000250}.
FT   TOPO_DOM    328    450       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    451    472       Helical. {ECO:0000250}.
FT   REGION      120    122       Agonist binding. {ECO:0000250}.
FT   REGION      180    182       Agonist binding. {ECO:0000250}.
FT   REGION      290    311       Allosteric effector binding.
FT                                {ECO:0000250}.
FT   BINDING     225    225       Agonist. {ECO:0000250}.
FT   CARBOHYD     33     33       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    105    105       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    174    174       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    161    175       {ECO:0000250}.
FT   CONFLICT    256    256       L -> M (in Ref. 1; CAA33495).
FT                                {ECO:0000305}.
SQ   SEQUENCE   473 AA;  54166 MW;  6A5ABD8A9143FE45 CRC64;
     MWGFAGGRLF GIFSAPVLVA VVCCAQSVND PGNMSFVKET VDKLLKGYDI RLRPDFGGPP
     VCVGMNIDIA SIDMVSEVNM DYTLTMYFQQ YWRDKRLAYS GIPLNLTLDN RVADQLWVPD
     TYFLNDKKSF VHGVTVKNRM IRLHPDGTVL YGLRITTTAA CMMDLRRYPL DEQNCTLEIE
     SYGYTTDDIE FYWRGGDKAV TGVERIELPQ FSIVEHRLVS RNVVFATGAY PRLSLSFRLK
     RNIGYFILQT YMPSILITIL SWVSFWINYD ASAARVALGI TTVLTMTTIN THLRETLPKI
     PYVKAIDMYL MGCFVFVFLA LLEYAFVNYI FFGRGPQRQK KLAEKTAKAK NDRSKSEINR
     VDAHGNILLA PMDVHNEMNE VAGSVGDTRN SAISFDNSGI QYRKQSMPKE GHGRYMGDRS
     IPHKKTHLRR RSSQLKIKIP DLTDVNAIDR WSRIVFPFTF SLFNLVYWLY YVN
//
DBGET integrated database retrieval system