GLRA2_HUMAN
ID GLRA2_HUMAN Reviewed; 452 AA.
AC P23416; A8K0J6; B2R6I8; B7Z4F5; J3KQ59; Q53YX7; Q6ICQ0; Q99862;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Glycine receptor subunit alpha-2;
DE Flags: Precursor;
GN Name=GLRA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2*), FUNCTION, SUBCELLULAR
RP LOCATION, AND ACTIVITY REGULATION.
RX PubMed=2155780; DOI=10.1002/j.1460-2075.1990.tb08172.x;
RA Grenningloh G., Schmieden V., Schofield P.R., Seeburg P.H., Siddique T.,
RA Mohandas T.K., Becker C.-M., Betz H.;
RT "Alpha subunit variants of the human glycine receptor: primary structures,
RT functional expression and chromosomal localization of the corresponding
RT genes.";
RL EMBO J. 9:771-776(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9674912;
RX DOI=10.1002/(sici)1096-8628(19980630)78:2<176::aid-ajmg16>3.0.co;2-k;
RA Cummings C.J., Dahle E.J.R., Zoghbi H.Y.;
RT "Analysis of the genomic structure of the human glycine receptor alpha-2
RT subunit gene and exclusion of this gene as a candidate for Rett syndrome.";
RL Am. J. Med. Genet. 78:176-178(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-2B AND ALPHA-2*), FUNCTION,
RP SUBCELLULAR LOCATION, SUBUNIT, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15302677; DOI=10.1038/sj.bjp.0705875;
RA Miller P.S., Harvey R.J., Smart T.G.;
RT "Differential agonist sensitivity of glycine receptor alpha2 subunit splice
RT variants.";
RL Br. J. Pharmacol. 143:19-26(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-2B).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA-2*; ALPHA-2B AND 3).
RC TISSUE=Brain, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-2*).
RC TISSUE=Brain;
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).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-360.
RX PubMed=8973915; DOI=10.1101/gr.6.12.1200;
RA Monani U.R., Burghes A.H.M.;
RT "Structure of the human alpha 2 subunit gene of the glycine receptor: use
RT of vectorette and Alu-exon PCR.";
RL Genome Res. 6:1200-1206(1996).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GLRB, AND ACTIVITY
RP REGULATION.
RX PubMed=16144831; DOI=10.1074/jbc.m508303200;
RA Miller P.S., Da Silva H.M., Smart T.G.;
RT "Molecular basis for zinc potentiation at strychnine-sensitive glycine
RT receptors.";
RL J. Biol. Chem. 280:37877-37884(2005).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=23895467; DOI=10.1111/acer.12192;
RA McCracken L.M., Trudell J.R., McCracken M.L., Harris R.A.;
RT "Zinc-dependent modulation of alpha2- and alpha3-glycine receptor subunits
RT by ethanol.";
RL Alcohol. Clin. Exp. Res. 37:2002-2010(2013).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25445488; DOI=10.1016/j.neuropharm.2014.10.026;
RA Zhang Y., Dixon C.L., Keramidas A., Lynch J.W.;
RT "Functional reconstitution of glycinergic synapses incorporating defined
RT glycine receptor subunit combinations.";
RL Neuropharmacology 89:391-397(2015).
CC -!- FUNCTION: Glycine receptors are ligand-gated chloride channels. Channel
CC opening is triggered by extracellular glycine (PubMed:2155780,
CC PubMed:15302677, PubMed:16144831, PubMed:23895467, PubMed:25445488).
CC Channel opening is also triggered by taurine and beta-alanine
CC (PubMed:15302677). Plays a role in the down-regulation of neuronal
CC excitability. Contributes to the generation of inhibitory postsynaptic
CC currents (PubMed:25445488). Plays a role in cellular responses to
CC ethanol (PubMed:23895467). {ECO:0000269|PubMed:15302677,
CC ECO:0000269|PubMed:16144831, ECO:0000269|PubMed:2155780,
CC ECO:0000269|PubMed:23895467, ECO:0000269|PubMed:25445488}.
CC -!- ACTIVITY REGULATION: Inhibited by strychnine (PubMed:2155780,
CC PubMed:15302677). Inhibited by picrotoxin (PubMed:15302677). Channel
CC activity is potentiated by 10-100 uM Zn(2+) (PubMed:15302677,
CC PubMed:16144831, PubMed:23895467). Channel activity is marginally
CC increased by 50 mM ethanol; it is strongly increased by a combination
CC of 0.5 uM Zn(2+) and 50 mM ethanol (PubMed:23895467). Channel activity
CC is inhibited by 100-1000 uM Zn(2+) (PubMed:15302677).
CC {ECO:0000269|PubMed:15302677, ECO:0000269|PubMed:16144831,
CC ECO:0000269|PubMed:2155780, ECO:0000269|PubMed:23895467}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=For isoform Alpha-2* homopentamers, a concentration of about 66
CC uM glycine results in half-maximal channel conductance. For isoform
CC Alpha-2B homopentamers, a concentration of about 34 uM glycine
CC results in half-maximal channel conductance.;
CC -!- SUBUNIT: Homopentamer (in vitro). Interacts with GLRB
CC (PubMed:16144831). Heteropentamer composed of GLRA2 and GLRB. Both
CC homopentamers and heteropentamers form functional ion channels, but
CC their characteristics are subtly different (PubMed:15302677).
CC {ECO:0000269|PubMed:16144831, ECO:0000305|PubMed:15302677}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q7TNC8}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23415}. Synapse {ECO:0000250|UniProtKB:Q7TNC8}.
CC Cell membrane {ECO:0000269|PubMed:15302677,
CC ECO:0000269|PubMed:16144831, ECO:0000269|PubMed:2155780,
CC ECO:0000269|PubMed:23895467, ECO:0000269|PubMed:25445488}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P23415}. Cell projection
CC {ECO:0000250|UniProtKB:Q7TNC8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Alpha-2*;
CC IsoId=P23416-1; Sequence=Displayed;
CC Name=Alpha-2B;
CC IsoId=P23416-2; Sequence=VSP_000082;
CC Name=3;
CC IsoId=P23416-3; Sequence=VSP_045465;
CC -!- MISCELLANEOUS: The alpha subunit binds strychnine.
CC {ECO:0000269|PubMed:2155780}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Glycine receptor (TC 1.A.9.3) subfamily. GLRA2 sub-subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X52008; CAA36257.1; -; mRNA.
DR EMBL; AF053495; AAC35290.1; -; Genomic_DNA.
DR EMBL; AF053487; AAC35290.1; JOINED; Genomic_DNA.
DR EMBL; AF053488; AAC35290.1; JOINED; Genomic_DNA.
DR EMBL; AF053489; AAC35290.1; JOINED; Genomic_DNA.
DR EMBL; AF053490; AAC35290.1; JOINED; Genomic_DNA.
DR EMBL; AF053491; AAC35290.1; JOINED; Genomic_DNA.
DR EMBL; AF053492; AAC35290.1; JOINED; Genomic_DNA.
DR EMBL; AF053493; AAC35290.1; JOINED; Genomic_DNA.
DR EMBL; AF053494; AAC35290.1; JOINED; Genomic_DNA.
DR EMBL; AY437083; AAR87842.1; -; mRNA.
DR EMBL; AY437084; AAR87843.1; -; mRNA.
DR EMBL; CR450343; CAG29339.1; -; mRNA.
DR EMBL; AK289561; BAF82250.1; -; mRNA.
DR EMBL; AK297304; BAH12541.1; -; mRNA.
DR EMBL; AK312591; BAG35485.1; -; mRNA.
DR EMBL; AC003658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC003683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98859.1; -; Genomic_DNA.
DR EMBL; CH471074; EAW98860.1; -; Genomic_DNA.
DR EMBL; BC032864; AAH32864.1; -; mRNA.
DR EMBL; U77731; AAB38272.1; -; Genomic_DNA.
DR EMBL; U77724; AAB38272.1; JOINED; Genomic_DNA.
DR EMBL; U77725; AAB38272.1; JOINED; Genomic_DNA.
DR EMBL; U77726; AAB38272.1; JOINED; Genomic_DNA.
DR EMBL; U77727; AAB38272.1; JOINED; Genomic_DNA.
DR EMBL; U77728; AAB38272.1; JOINED; Genomic_DNA.
DR EMBL; U77729; AAB38272.1; JOINED; Genomic_DNA.
DR EMBL; U77730; AAB38272.1; JOINED; Genomic_DNA.
DR EMBL; U77731; AAB38273.1; -; Genomic_DNA.
DR EMBL; U77724; AAB38273.1; JOINED; Genomic_DNA.
DR EMBL; U77725; AAB38273.1; JOINED; Genomic_DNA.
DR EMBL; U77726; AAB38273.1; JOINED; Genomic_DNA.
DR EMBL; U77727; AAB38273.1; JOINED; Genomic_DNA.
DR EMBL; U77728; AAB38273.1; JOINED; Genomic_DNA.
DR EMBL; U77729; AAB38273.1; JOINED; Genomic_DNA.
DR EMBL; U77730; AAB38273.1; JOINED; Genomic_DNA.
DR CCDS; CCDS14160.1; -. [P23416-1]
DR CCDS; CCDS48085.1; -. [P23416-2]
DR CCDS; CCDS55371.1; -. [P23416-3]
DR PIR; S12381; S12381.
DR RefSeq; NP_001112357.1; NM_001118885.1. [P23416-1]
DR RefSeq; NP_001112358.1; NM_001118886.1. [P23416-2]
DR RefSeq; NP_001165413.1; NM_001171942.1. [P23416-3]
DR RefSeq; NP_002054.1; NM_002063.3. [P23416-1]
DR RefSeq; XP_016884916.1; XM_017029427.1. [P23416-2]
DR RefSeq; XP_016884917.1; XM_017029428.1. [P23416-3]
DR RefSeq; XP_016884918.1; XM_017029429.1. [P23416-3]
DR PDB; 5BKF; EM; 3.60 A; A/B/C/D=28-343, A/B/C/D=409-452.
DR PDB; 5BKG; EM; 3.80 A; A/B/C/D=28-343, A/B/C/D=409-452.
DR PDB; 7KUY; EM; 3.60 A; A/B/C/D=28-343, A/B/C/D=409-452.
DR PDB; 7L31; EM; 3.80 A; A/B/C/D=28-343, A/B/C/D=409-452.
DR PDBsum; 5BKF; -.
DR PDBsum; 5BKG; -.
DR PDBsum; 7KUY; -.
DR PDBsum; 7L31; -.
DR AlphaFoldDB; P23416; -.
DR SMR; P23416; -.
DR BioGRID; 109004; 30.
DR IntAct; P23416; 20.
DR STRING; 9606.ENSP00000218075; -.
DR BindingDB; P23416; -.
DR ChEMBL; CHEMBL5871; -.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB00145; Glycine.
DR DrugBank; DB00431; Lindane.
DR DrugBank; DB01043; Memantine.
DR DrugBank; DB00466; Picrotoxin.
DR DrugBank; DB01956; Taurine.
DR DrugCentral; P23416; -.
DR GuidetoPHARMACOLOGY; 424; -.
DR TCDB; 1.A.9.3.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR GlyGen; P23416; 2 sites.
DR iPTMnet; P23416; -.
DR PhosphoSitePlus; P23416; -.
DR BioMuta; GLRA2; -.
DR DMDM; 121578; -.
DR MassIVE; P23416; -.
DR PaxDb; P23416; -.
DR PeptideAtlas; P23416; -.
DR PRIDE; P23416; -.
DR ProteomicsDB; 54091; -. [P23416-1]
DR ProteomicsDB; 54092; -. [P23416-2]
DR Antibodypedia; 54675; 53 antibodies from 17 providers.
DR DNASU; 2742; -.
DR Ensembl; ENST00000218075.9; ENSP00000218075.4; ENSG00000101958.14. [P23416-1]
DR Ensembl; ENST00000355020.8; ENSP00000347123.4; ENSG00000101958.14. [P23416-2]
DR Ensembl; ENST00000443437.6; ENSP00000387756.2; ENSG00000101958.14. [P23416-3]
DR GeneID; 2742; -.
DR KEGG; hsa:2742; -.
DR MANE-Select; ENST00000218075.9; ENSP00000218075.4; NM_002063.4; NP_002054.1.
DR UCSC; uc004cwe.5; human. [P23416-1]
DR CTD; 2742; -.
DR DisGeNET; 2742; -.
DR GeneCards; GLRA2; -.
DR HGNC; HGNC:4327; GLRA2.
DR HPA; ENSG00000101958; Tissue enhanced (brain, intestine, retina).
DR MIM; 305990; gene.
DR neXtProt; NX_P23416; -.
DR OpenTargets; ENSG00000101958; -.
DR PharmGKB; PA28728; -.
DR VEuPathDB; HostDB:ENSG00000101958; -.
DR eggNOG; KOG3644; Eukaryota.
DR GeneTree; ENSGT00940000158730; -.
DR HOGENOM; CLU_010920_1_2_1; -.
DR InParanoid; P23416; -.
DR OMA; ENMFLRI; -.
DR OrthoDB; 614790at2759; -.
DR PhylomeDB; P23416; -.
DR TreeFam; TF315453; -.
DR PathwayCommons; P23416; -.
DR Reactome; R-HSA-112314; Neurotransmitter receptors and postsynaptic signal transmission.
DR SignaLink; P23416; -.
DR SIGNOR; P23416; -.
DR BioGRID-ORCS; 2742; 20 hits in 694 CRISPR screens.
DR ChiTaRS; GLRA2; human.
DR GeneWiki; GLRA2; -.
DR GenomeRNAi; 2742; -.
DR Pharos; P23416; Tchem.
DR PRO; PR:P23416; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P23416; protein.
DR Bgee; ENSG00000101958; Expressed in cortical plate and 57 other tissues.
DR ExpressionAtlas; P23416; baseline and differential.
DR Genevisible; P23416; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0098690; C:glycinergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0016934; F:extracellularly glycine-gated chloride channel activity; IDA:UniProtKB.
DR GO; GO:0016594; F:glycine binding; IDA:UniProtKB.
DR GO; GO:0022852; F:glycine-gated chloride ion channel activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
DR GO; GO:0071361; P:cellular response to ethanol; IDA:UniProtKB.
DR GO; GO:0071294; P:cellular response to zinc ion; IDA:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IDA:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0043200; P:response to amino acid; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0060012; P:synaptic transmission, glycinergic; 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; IPR008127; Glycine_rcpt_A.
DR InterPro; IPR008129; Glycine_rcpt_A2.
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 PANTHER; PTHR18945:SF28; PTHR18945:SF28; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00253; GABAARECEPTR.
DR PRINTS; PR01673; GLYRALPHA.
DR PRINTS; PR01675; GLYRALPHA2.
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; Alternative splicing; Cell membrane; Cell projection;
KW Chloride; Chloride channel; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Metal-binding;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport; Zinc.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..452
FT /note="Glycine receptor subunit alpha-2"
FT /id="PRO_0000000416"
FT TOPO_DOM 28..256
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 257..278
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TOPO_DOM 279..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 284..304
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TOPO_DOM 305..315
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 316..336
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TOPO_DOM 337..420
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 421..441
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TOPO_DOM 442..452
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT BINDING 236..241
FT /ligand="strychnine"
FT /ligand_id="ChEBI:CHEBI:90700"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT SITE 295
FT /note="Important for obstruction of the ion pore in the
FT closed conformation"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 172..186
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT DISULFID 232..243
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT VAR_SEQ 1..89
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045465"
FT VAR_SEQ 85..86
FT /note="VT -> IA (in isoform Alpha-2B)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15302677, ECO:0000303|Ref.4"
FT /id="VSP_000082"
FT CONFLICT 389
FT /note="V -> A (in Ref. 5; BAH12541)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 52002 MW; 9EE74B3F49A555EA CRC64;
MNRQLVNILT ALFAFFLETN HFRTAFCKDH DSRSGKQPSQ TLSPSDFLDK LMGRTSGYDA
RIRPNFKGPP VNVTCNIFIN SFGSVTETTM DYRVNIFLRQ QWNDSRLAYS EYPDDSLDLD
PSMLDSIWKP DLFFANEKGA NFHDVTTDNK LLRISKNGKV LYSIRLTLTL SCPMDLKNFP
MDVQTCTMQL ESFGYTMNDL IFEWLSDGPV QVAEGLTLPQ FILKEEKELG YCTKHYNTGK
FTCIEVKFHL ERQMGYYLIQ MYIPSLLIVI LSWVSFWINM DAAPARVALG ITTVLTMTTQ
SSGSRASLPK VSYVKAIDIW MAVCLLFVFA ALLEYAAVNF VSRQHKEFLR LRRRQKRQNK
EEDVTRESRF NFSGYGMGHC LQVKDGTAVK ATPANPLPQP PKDGDAIKKK FVDRAKRIDT
ISRAAFPLAF LIFNIFYWIT YKIIRHEDVH KK
