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   24-JAN-2024, entry version 175.
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   GlyCosmos; P56476; 2 sites, No reported glycans.
DR   GlyGen; P56476; 2 sites.
DR   PhosphoSitePlus; P56476; -.
DR   PaxDb; 10090-ENSMUSP00000024035; -.
DR   Antibodypedia; 18718; 142 antibodies from 23 providers.
DR   DNASU; 14409; -.
DR   Ensembl; ENSMUST00000024035.9; ENSMUSP00000024035.3; ENSMUSG00000023267.11. [P56476-2]
DR   Ensembl; ENSMUST00000108162.8; ENSMUSP00000103797.2; ENSMUSG00000023267.11. [P56476-1]
DR   GeneID; 14409; -.
DR   KEGG; mmu:14409; -.
DR   UCSC; uc008sfq.1; mouse. [P56476-2]
DR   AGR; MGI:95626; -.
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; 4265336at2759; -.
DR   TreeFam; TF315453; -.
DR   Reactome; R-MMU-977443; GABA receptor activation.
DR   BioGRID-ORCS; 14409; 5 hits in 80 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 51 other cell types or tissues.
DR   ExpressionAtlas; P56476; baseline and differential.
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: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: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 monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; ISO:MGI.
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:0007601; P:visual perception; IMP:MGI.
DR   CDD; cd19005; LGIC_ECD_GABAAR_rho; 1.
DR   CDD; cd19059; LGIC_TM_GABAAR_rho; 1.
DR   Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR   Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 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   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945:SF197; GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT RHO-2; 1.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 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; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR   SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
DR   Genevisible; P56476; MM.
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
//