GBRA3_RAT
ID GBRA3_RAT Reviewed; 493 AA.
AC P20236; F1LNZ5;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-3;
DE AltName: Full=GABA(A) receptor subunit alpha-3;
DE Flags: Precursor;
GN Name=Gabra3; Synonyms=Gabra-3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=2153588; DOI=10.1016/0014-5793(90)80118-3;
RA Malherbe P., Sigel E., Baur R., Persohn E., Richards J.G., Moehler H.;
RT "Functional expression and sites of gene transcription of a novel alpha
RT subunit of the GABAA receptor in rat brain.";
RL FEBS Lett. 260:261-265(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1966765; DOI=10.1101/sqb.1990.055.01.006;
RA Seeburg P.H., Wisden W., Verdoorn T., Pritchett D., Werner P., Herb A.,
RA Lueddens H., Sprengel R., Sakmann B.;
RT "The GABAA receptor family: molecular and functional diversity.";
RL Cold Spring Harb. Symp. Quant. Biol. 55:29-40(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-163, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
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 -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC chains: alpha, beta, gamma, delta, and rho. Binds UBQLN1 (By
CC similarity). Interacts with GPHN (By similarity).
CC {ECO:0000250|UniProtKB:P26049, ECO:0000250|UniProtKB:P34903}.
CC -!- INTERACTION:
CC P20236; Q03555-6: Gphn; NbExp=5; IntAct=EBI-5273284, EBI-5273276;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in most brain regions.
CC {ECO:0000269|PubMed:2153588}.
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. GABRA3 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X51991; CAA36247.1; -; mRNA.
DR EMBL; L08492; AAC42031.1; -; Genomic_DNA.
DR EMBL; AABR07042312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07042313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07042314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07042315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07042316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07042317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07042318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A34130; A34130.
DR RefSeq; NP_058765.3; NM_017069.3.
DR RefSeq; XP_017457405.1; XM_017601916.1.
DR PDB; 4TK1; X-ray; 2.70 A; C/D=396-406.
DR PDB; 4TK2; X-ray; 4.10 A; C/D=396-406.
DR PDB; 4TK3; X-ray; 2.70 A; C/D=396-406.
DR PDB; 4TK4; X-ray; 3.60 A; C/D=396-406.
DR PDB; 4U90; X-ray; 2.00 A; D/E=396-404.
DR PDB; 6HSN; X-ray; 1.55 A; D/E=396-405.
DR PDBsum; 4TK1; -.
DR PDBsum; 4TK2; -.
DR PDBsum; 4TK3; -.
DR PDBsum; 4TK4; -.
DR PDBsum; 4U90; -.
DR PDBsum; 6HSN; -.
DR AlphaFoldDB; P20236; -.
DR SMR; P20236; -.
DR ComplexPortal; CPX-409; GABA-A receptor, alpha-3/beta-3/gamma-2.
DR CORUM; P20236; -.
DR IntAct; P20236; 1.
DR STRING; 10116.ENSRNOP00000050712; -.
DR BindingDB; P20236; -.
DR ChEMBL; CHEMBL328; -.
DR DrugCentral; P20236; -.
DR GlyGen; P20236; 4 sites, 9 N-linked glycans (1 site).
DR iPTMnet; P20236; -.
DR PhosphoSitePlus; P20236; -.
DR PaxDb; P20236; -.
DR PRIDE; P20236; -.
DR GeneID; 24947; -.
DR KEGG; rno:24947; -.
DR CTD; 2556; -.
DR RGD; 2648; Gabra3.
DR VEuPathDB; HostDB:ENSRNOG00000056558; -.
DR eggNOG; KOG3642; Eukaryota.
DR HOGENOM; CLU_010920_2_1_1; -.
DR InParanoid; P20236; -.
DR OMA; LTKKANN; -.
DR OrthoDB; 1057372at2759; -.
DR PhylomeDB; P20236; -.
DR TreeFam; TF315453; -.
DR Reactome; R-RNO-977443; GABA receptor activation.
DR PRO; PR:P20236; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000056558; Expressed in frontal cortex and 4 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR GO; GO:1902711; C:GABA-A receptor complex; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0004890; F:GABA-A receptor activity; IDA:RGD.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; IBA:GO_Central.
DR GO; GO:0005237; F:inhibitory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:RGD.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IBA:GO_Central.
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:0060078; P:regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IBA:GO_Central.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR001390; GABAAa_rcpt.
DR InterPro; IPR005433; GABBAa3_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; PR01079; GABAARALPHA.
DR PRINTS; PR01616; GABAARALPHA3.
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 3D-structure; Cell membrane; Chloride; Chloride channel; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..493
FT /note="Gamma-aminobutyric acid receptor subunit alpha-3"
FT /id="PRO_0000000439"
FT TOPO_DOM 29..276
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 277..298
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 304..325
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 338..359
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 360..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 459..480
FT /note="Helical"
FT /evidence="ECO:0000305"
FT REGION 27..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26049"
FT MOD_RES 428
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26049"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26049"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26049"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 191..205
FT /evidence="ECO:0000250"
FT CONFLICT 160
FT /note="V -> M (in Ref. 2; AAC42031)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="S -> T (in Ref. 2; AAC42031)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="I -> M (in Ref. 1; CAA36247 and 2; AAC42031)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="K -> L (in Ref. 1; CAA36247)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 55430 MW; 4A685D5E05D76B41 CRC64;
MITTQMWHFY VTRVGLLLLI SILPGTTGQG ESRRQEPGDF VKQDIGGLSP KHAPDIPDDS
TDNITIFTRI LDRLLDGYDN RLRPGLGDAV TEVKTDIYVT SFGPVSDTDM EYTIDVFFRQ
TWHDERLKFD GPMKILPLNN LLASKIWTPD TFFHNGKKSV AHNMTTPNKL LRLVDNGTLL
YTMRLTIHAE CPMHLEDFPM DVHACPLKFG SYAYTKAEVI YSWTLGKNKS VEVAQDGSRL
NQYDLLGHVV GTEIIRSSTG EYVVMTTHFH LKRKIGYFVI QTYLPCIMTV ILSQVSFWLN
RESVPARTVF GVTTVLTMTT LSISARNSLP KVAYATAMDW FIAVCYAFVF SALIEFATVN
YFTKRSWAWE GKKVPEALEM KKKTPAAPTK KTSTTFNIVG TTYPINLAKD TEFSTISKAA
AAPSASSTPT VIASPKTTYV QDSPAETKTY NSVSKVDKIS RIIFPVLFAI FNLVYWATYV
NRESAIKGMI RKQ
