GBRR2_MOUSE
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 03-AUG-2022, entry version 167.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate
CC brain, mediates neuronal inhibition by binding to the
CC GABA/benzodiazepine receptor and opening an integral chloride channel.
CC Rho-2 GABA receptor could play a role in retinal neurotransmission (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC chains: alpha, beta, gamma, delta, and rho. Interacts with SQSTM1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
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 -!- MISCELLANEOUS: [Isoform 2]: Isoform 2 could be translated from an
CC upstream initiator ATG located in frame within the first coding exon.
CC The probability of a signal peptide within this isoform is very low.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRR2 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; AF024621; AAB81965.1; -; mRNA.
DR EMBL; CH466538; EDL05492.1; -; Genomic_DNA.
DR EMBL; BC057957; AAH57957.2; -; mRNA.
DR CCDS; CCDS18020.1; -. [P56476-2]
DR RefSeq; NP_032102.2; NM_008076.3. [P56476-2]
DR AlphaFoldDB; P56476; -.
DR SMR; P56476; -.
DR STRING; 10090.ENSMUSP00000024035; -.
DR GlyGen; P56476; 2 sites.
DR PhosphoSitePlus; P56476; -.
DR PaxDb; P56476; -.
DR PRIDE; P56476; -.
DR Antibodypedia; 18718; 123 antibodies from 23 providers.
DR DNASU; 14409; -.
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. [P56476-2]
DR CTD; 2570; -.
DR MGI; MGI:95626; Gabrr2.
DR VEuPathDB; HostDB:ENSMUSG00000023267; -.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000156864; -.
DR HOGENOM; CLU_010920_0_1_1; -.
DR InParanoid; P56476; -.
DR OMA; KFPCVCG; -.
DR OrthoDB; 640805at2759; -.
DR TreeFam; TF315453; -.
DR Reactome; R-MMU-977443; GABA receptor activation.
DR BioGRID-ORCS; 14409; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Gabrr2; mouse.
DR PRO; PR:P56476; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P56476; protein.
DR Bgee; ENSMUSG00000023267; Expressed in retinal neural layer and 49 other tissues.
DR ExpressionAtlas; P56476; baseline and differential.
DR Genevisible; P56476; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; TAS:MGI.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:1902711; C:GABA-A receptor complex; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0004890; F:GABA-A receptor activity; IMP:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0006821; P:chloride transport; TAS:MGI.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IMP:MGI.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR008059; GABAAa_rho2_rcpt.
DR InterPro; IPR008057; GABAAa_rho_rcpt.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
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 membrane; Chloride; Chloride channel;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Postsynaptic cell membrane; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..465
FT /note="Gamma-aminobutyric acid receptor subunit rho-2"
FT /id="PRO_0000000489"
FT TOPO_DOM 21..260
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 178..192
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MVKPGGILPIKSPCTAACCIIDMCRM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044374"
FT CONFLICT 33
FT /note="E -> D (in Ref. 1; AAB81965)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="P -> A (in Ref. 1; AAB81965)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="L -> F (in Ref. 1; AAB81965)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="L -> V (in Ref. 1; AAB81965)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="R -> K (in Ref. 1; AAB81965)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="R -> K (in Ref. 1; AAB81965)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="H -> Q (in Ref. 1; AAB81965)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="R -> L (in Ref. 1; AAB81965)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="M -> V (in Ref. 1; AAB81965)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="S -> A (in Ref. 1; AAB81965)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="R -> T (in Ref. 1; AAB81965)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="E -> K (in Ref. 1; AAB81965)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="R -> K (in Ref. 1; AAB81965)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="Q -> R (in Ref. 1; AAB81965)"
FT /evidence="ECO:0000305"
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
