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Database: UniProt
Entry: P56476
LinkDB: P56476
Original site: P56476 
ID   GBRR2_MOUSE             Reviewed;         465 AA.
AC   P56476; Q6PEP0;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 4.
DT   16-APR-2014, entry version 117.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit rho-2;
DE   AltName: Full=GABA(A) receptor subunit rho-2;
DE   AltName: Full=GABA(C) receptor;
DE   Flags: Precursor;
GN   Name=Gabrr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Retina;
RA   Greka A., Koolen J.A., Lipton S.A., Zhang D.;
RT   "Molecular cloning of GABA rho subunits in the mouse retina.";
RL   Abstr. - Soc. Neurosci. 23:1262-1262(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Eye;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the
CC       vertebrate brain, mediates neuronal inhibition by binding to the
CC       GABA/benzodiazepine receptor and opening an integral chloride
CC       channel. Rho-2 GABA receptor could play a role in retinal
CC       neurotransmission (By similarity).
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A)
CC       receptor chains: alpha, beta, gamma, delta, and rho. Interacts
CC       with SQSTM1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein (By similarity). Cell
CC       membrane; Multi-pass membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1;
CC         IsoId=P56476-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P56476-2; Sequence=VSP_044374;
CC         Note=Isoform 2 could be translated from an upstream initiator
CC         ATG located in frame within the first coding exon. The
CC         probability of a signal peptide within this isoform is very low.
CC         No experimental confirmation available;
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       GABRR2 sub-subfamily.
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DR   EMBL; AF024621; AAB81965.1; -; mRNA.
DR   EMBL; CH466538; EDL05492.1; -; Genomic_DNA.
DR   EMBL; BC057957; AAH57957.2; -; mRNA.
DR   RefSeq; NP_032102.2; NM_008076.3.
DR   UniGene; Mm.6227; -.
DR   ProteinModelPortal; P56476; -.
DR   SMR; P56476; 62-465.
DR   PhosphoSite; P56476; -.
DR   PRIDE; P56476; -.
DR   Ensembl; ENSMUST00000024035; ENSMUSP00000024035; ENSMUSG00000023267. [P56476-2]
DR   Ensembl; ENSMUST00000108162; ENSMUSP00000103797; ENSMUSG00000023267. [P56476-1]
DR   GeneID; 14409; -.
DR   KEGG; mmu:14409; -.
DR   UCSC; uc008sfq.1; mouse. [P56476-1]
DR   CTD; 2570; -.
DR   MGI; MGI:95626; Gabrr2.
DR   eggNOG; NOG77438; -.
DR   GeneTree; ENSGT00630000089571; -.
DR   HOGENOM; HOG000231335; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; Q6PEP0; -.
DR   KO; K05190; -.
DR   OMA; DEHDFSM; -.
DR   OrthoDB; EOG712TVZ; -.
DR   TreeFam; TF315453; -.
DR   NextBio; 285985; -.
DR   PRO; PR:P56476; -.
DR   Bgee; P56476; -.
DR   Genevestigator; P56476; -.
DR   GO; GO:0030424; C:axon; TAS:MGI.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004890; F:GABA-A receptor activity; IMP:MGI.
DR   GO; GO:0006821; P:chloride transport; TAS:MGI.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IMP:MGI.
DR   GO; GO:0007601; P:visual perception; IMP:MGI.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR006028; GABAA_rcpt.
DR   InterPro; IPR008059; GABAAa_rho2_rcpt.
DR   InterPro; IPR008057; GABAAa_rho_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; PR00253; GABAARECEPTR.
DR   PRINTS; PR01670; GABAARRHO.
DR   PRINTS; PR01672; GABAARRHO2.
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   2: Evidence at transcript level;
KW   Alternative initiation; Cell junction; Cell membrane; Chloride;
KW   Chloride channel; Complete proteome; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Postsynaptic cell membrane;
KW   Reference proteome; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    465       Gamma-aminobutyric acid receptor subunit
FT                                rho-2.
FT                                /FTId=PRO_0000000489.
FT   TOPO_DOM     21    260       Extracellular (Probable).
FT   TRANSMEM    261    281       Helical; (Potential).
FT   TRANSMEM    294    314       Helical; (Potential).
FT   TRANSMEM    326    346       Helical; (Potential).
FT   TOPO_DOM    347    443       Cytoplasmic (Probable).
FT   TRANSMEM    444    464       Helical; (Potential).
FT   CARBOHYD    120    120       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    254    254       N-linked (GlcNAc...) (Potential).
FT   DISULFID    178    192       By similarity.
FT   VAR_SEQ       1      1       M -> MVKPGGILPIKSPCTAACCIIDMCRM (in
FT                                isoform 2).
FT                                /FTId=VSP_044374.
FT   CONFLICT     33     33       E -> D (in Ref. 1; AAB81965).
FT   CONFLICT     52     52       P -> A (in Ref. 1; AAB81965).
FT   CONFLICT     59     59       L -> F (in Ref. 1; AAB81965).
FT   CONFLICT     88     88       L -> V (in Ref. 1; AAB81965).
FT   CONFLICT    105    105       R -> K (in Ref. 1; AAB81965).
FT   CONFLICT    109    109       R -> K (in Ref. 1; AAB81965).
FT   CONFLICT    149    149       H -> Q (in Ref. 1; AAB81965).
FT   CONFLICT    357    357       R -> L (in Ref. 1; AAB81965).
FT   CONFLICT    366    366       M -> V (in Ref. 1; AAB81965).
FT   CONFLICT    372    372       S -> A (in Ref. 1; AAB81965).
FT   CONFLICT    394    394       R -> T (in Ref. 1; AAB81965).
FT   CONFLICT    400    400       E -> K (in Ref. 1; AAB81965).
FT   CONFLICT    421    421       R -> K (in Ref. 1; AAB81965).
FT   CONFLICT    429    429       Q -> R (in Ref. 1; AAB81965).
SQ   SEQUENCE   465 AA;  54231 MW;  B44B51B572468A20 CRC64;
     MPYLMRLALV LFCLMALVES RKPRRKRWTG LLETSKPSHL YKKNLDVTKM RPGKPRPLLR
     VEDHDFTMRP AFGGPAIPVG VDVQVESLDS ISEVDMDFTM TLYLRHYWRD ERLAFPSSSN
     KSMTFDGRLV KKIWVPDVFF VHSKRSFIHD TTTDNIMLRV FPDGHVLYSM RITVTAMCNM
     DFSHFPLDSQ TCSLELESYA YTDEDLMLYW KNGDESLKTD EKISLSQFLI QKFHTTSRLA
     FYSSTGWYNR LYINFTLRRH IFFFLLQTYF PATLMVMLSW VSFWIDHRAV PARVSLGIMT
     VLTMSTIITG VNASMPRVSY IRAVDIYLWV SFVFVFLSVL EYAAVNYLTT LQEQKERKFR
     EKLPCMCGML HSRTMMLDGS YSESEANSLA GYPRSHILPE EERPDNIVVH LALNSELTSS
     RKKGLLKGQM GLYIFQNTHA IDKYSRLIFP AFYIVFNLIY WSVFS
//
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