GRIA2_HUMAN
ID GRIA2_HUMAN Reviewed; 883 AA.
AC P42262; A8MT92; I6L997; Q96FP6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Glutamate receptor 2 {ECO:0000305};
DE Short=GluR-2;
DE AltName: Full=AMPA-selective glutamate receptor 2;
DE AltName: Full=GluR-B;
DE AltName: Full=GluR-K2;
DE AltName: Full=Glutamate receptor ionotropic, AMPA 2;
DE Short=GluA2;
DE Flags: Precursor;
GN Name=GRIA2 {ECO:0000312|HGNC:HGNC:4572}; Synonyms=GLUR2;
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 FLIP), AND RNA EDITING OF POSITION 607.
RC TISSUE=Brain;
RX PubMed=8003671; DOI=10.1097/00001756-199401120-00018;
RA Sun W., Ferrer-Montiel A.V., Montal M.;
RT "Primary structure and functional expression of the AMPA/kainate receptor
RT subunit 2 from human brain.";
RL NeuroReport 5:441-444(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS FLOP AND 4), AND RNA
RP EDITING OF POSITIONS 607 AND 608.
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 [4]
RP RNA EDITING OF POSITION 607.
RX PubMed=7523595; DOI=10.1046/j.1471-4159.1994.63051596.x;
RA Paschen W., Hedreen J.C., Ross C.A.;
RT "RNA editing of the glutamate receptor subunits GluR2 and GluR6 in human
RT brain tissue.";
RL J. Neurochem. 63:1596-1602(1994).
RN [5]
RP IDENTIFICATION (ISOFORM 3).
RX PubMed=14687553; DOI=10.1016/s0896-6273(03)00722-0;
RA Kolleker A., Zhu J.J., Schupp B.J., Qin Y., Mack V., Borchardt T.,
RA Koehr G., Malinow R., Seeburg P.H., Osten P.;
RT "Glutamatergic plasticity by synaptic delivery of GluR-B(long)-containing
RT AMPA receptors.";
RL Neuron 40:1199-1212(2003).
RN [6]
RP INTERACTION WITH PICK1.
RX PubMed=15247289; DOI=10.1074/jbc.m404499200;
RA Dev K.K., Nakanishi S., Henley J.M.;
RT "The PDZ domain of PICK1 differentially accepts protein kinase C-alpha and
RT GluR2 as interacting ligands.";
RL J. Biol. Chem. 279:41393-41397(2004).
RN [7]
RP UBIQUITINATION.
RX PubMed=23129617; DOI=10.1073/pnas.1217477109;
RA Lussier M.P., Herring B.E., Nasu-Nishimura Y., Neutzner A., Karbowski M.,
RA Youle R.J., Nicoll R.A., Roche K.W.;
RT "Ubiquitin ligase RNF167 regulates AMPA receptor-mediated synaptic
RT transmission.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:19426-19431(2012).
RN [8]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23739980; DOI=10.1523/jneurosci.2626-12.2013;
RA Salussolia C.L., Gan Q., Kazi R., Singh P., Allopenna J., Furukawa H.,
RA Wollmuth L.P.;
RT "A eukaryotic specific transmembrane segment is required for
RT tetramerization in AMPA receptors.";
RL J. Neurosci. 33:9840-9845(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 25-412, SUBUNIT, DISULFIDE BOND,
RP AND GLYCOSYLATION AT ASN-370.
RX PubMed=19651138; DOI=10.1016/j.jmb.2009.07.082;
RA Clayton A., Siebold C., Gilbert R.J., Sutton G.C., Harlos K.,
RA McIlhinney R.A., Jones E.Y., Aricescu A.R.;
RT "Crystal structure of the GluR2 amino-terminal domain provides insights
RT into the architecture and assembly of ionotropic glutamate receptors.";
RL J. Mol. Biol. 392:1125-1132(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 413-795 IN COMPLEX WITH GLUTAMATE
RP AND SYNTHETIC INHIBITOR, AND FUNCTION.
RX PubMed=20614889; DOI=10.1021/jm1005429;
RA Ward S.E., Harries M., Aldegheri L., Andreotti D., Ballantine S., Bax B.D.,
RA Harris A.J., Harker A.J., Lund J., Melarange R., Mingardi A.,
RA Mookherjee C., Mosley J., Neve M., Oliosi B., Profeta R., Smith K.J.,
RA Smith P.W., Spada S., Thewlis K.M., Yusaf S.P.;
RT "Discovery of N-[(2S)-5-(6-fluoro-3-pyridinyl)-2,3-dihydro-1H-inden-2-yl]-
RT 2-propanesulfonamide, a novel clinical AMPA receptor positive modulator.";
RL J. Med. Chem. 53:5801-5812(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 413-796 IN COMPLEX WITH GLUTAMATE
RP AND SYNTHETIC INHIBITOR, AND DISULFIDE BOND.
RX PubMed=21531559; DOI=10.1016/j.bmcl.2011.04.017;
RA Koller M., Lingenhoehl K., Schmutz M., Vranesic I.T., Kallen J.,
RA Auberson Y.P., Carcache D.A., Mattes H., Ofner S., Orain D., Urwyler S.;
RT "Quinazolinedione sulfonamides: a novel class of competitive AMPA receptor
RT antagonists with oral activity.";
RL Bioorg. Med. Chem. Lett. 21:3358-3361(2011).
RN [12]
RP VARIANTS NEDLIB GLU-47; GLY-302; 323-ARG--ILE-883 DEL; 528-PRO--LYS-530
RP DEL; THR-528; GLU-607; ARG-609; ASN-611; SER-639; LEU-644; ASN-646;
RP LEU-647; ASP-776; LEU-788; VAL-792; VAL-807 AND SER-812, INVOLVEMENT IN
RP NEDLIB, CHARACTERIZATION OF VARIANTS NEDLIB GLU-47; GLY-302; GLU-607;
RP ARG-609; SER-639; LEU-644 AND ASN-646, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31300657; DOI=10.1038/s41467-019-10910-w;
RG SYNAPS Study Group;
RA Salpietro V., Dixon C.L., Guo H., Bello O.D., Vandrovcova J., Efthymiou S.,
RA Maroofian R., Heimer G., Burglen L., Valence S., Torti E., Hacke M.,
RA Rankin J., Tariq H., Colin E., Procaccio V., Striano P., Mankad K.,
RA Lieb A., Chen S., Pisani L., Bettencourt C., Maennikkoe R., Manole A.,
RA Brusco A., Grosso E., Ferrero G.B., Armstrong-Moron J., Gueden S.,
RA Bar-Yosef O., Tzadok M., Monaghan K.G., Santiago-Sim T., Person R.E.,
RA Cho M.T., Willaert R., Yoo Y., Chae J.H., Quan Y., Wu H., Wang T.,
RA Bernier R.A., Xia K., Blesson A., Jain M., Motazacker M.M., Jaeger B.,
RA Schneider A.L., Boysen K., Muir A.M., Myers C.T., Gavrilova R.H.,
RA Gunderson L., Schultz-Rogers L., Klee E.W., Dyment D., Osmond M.,
RA Parellada M., Llorente C., Gonzalez-Penas J., Carracedo A.,
RA Van Haeringen A., Ruivenkamp C., Nava C., Heron D., Nardello R.,
RA Iacomino M., Minetti C., Skabar A., Fabretto A., Raspall-Chaure M.,
RA Chez M., Tsai A., Fassi E., Shinawi M., Constantino J.N., De Zorzi R.,
RA Fortuna S., Kok F., Keren B., Bonneau D., Choi M., Benzeev B., Zara F.,
RA Mefford H.C., Scheffer I.E., Clayton-Smith J., Macaya A., Rothman J.E.,
RA Eichler E.E., Kullmann D.M., Houlden H.;
RT "AMPA receptor GluA2 subunit defects are a cause of neurodevelopmental
RT disorders.";
RL Nat. Commun. 10:3094-3094(2019).
CC -!- FUNCTION: Receptor for glutamate that functions as ligand-gated ion
CC channel in the central nervous system (PubMed:31300657). It plays an
CC important role in excitatory synaptic transmission. L-glutamate acts as
CC an excitatory neurotransmitter at many synapses in the central nervous
CC system. Binding of the excitatory neurotransmitter L-glutamate induces
CC a conformation change, leading to the opening of the cation channel,
CC and thereby converts the chemical signal to an electrical impulse. The
CC receptor then desensitizes rapidly and enters a transient inactive
CC state, characterized by the presence of bound agonist. In the presence
CC of CACNG4 or CACNG7 or CACNG8, shows resensitization which is
CC characterized by a delayed accumulation of current flux upon continued
CC application of glutamate. Through complex formation with NSG1, GRIP1
CC and STX12 controls the intracellular fate of AMPAR and the endosomal
CC sorting of the GRIA2 subunit toward recycling and membrane targeting
CC (By similarity). {ECO:0000250|UniProtKB:P19491,
CC ECO:0000269|PubMed:20614889, ECO:0000269|PubMed:31300657}.
CC -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC receptor subunits. Tetramers may be formed by the dimerization of
CC dimers. May interact with MPP4. Forms a ternary complex with GRIP1 and
CC CSPG4. Interacts with ATAD1 in an ATP-dependent manner. ATAD1-catalyzed
CC ATP hydrolysis disrupts binding to ATAD1 and to GRIP1 and leads to
CC AMPAR complex disassembly. Interacts with GRIP2. Isoform 1, but not
CC isoform 3, interacts with PICK1/PRKCABP. Interacts with GRIA1 and
CC SYNDIG1. Interacts with LRFN1 (By similarity). Found in a complex with
CC GRIA1, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5,
CC CACNG7 and CACNG8. Interacts with CACNG5 (By similarity). Interacts
CC with SNX27 (via PDZ domain); the interaction is required for recycling
CC to the plasma membrane when endocytosed and prevent degradation in
CC lysosomes. Interacts with OLFM2 (By similarity). Interacts with AP4B1,
CC AP4E1 and AP4M1; probably indirect it mediates the somatodendritic
CC localization of GRIA2 in neurons (By similarity). Forms a complex with
CC NSG1, GRIP1 and STX12; controls the intracellular fate of AMPAR and the
CC endosomal sorting of the GRIA2 subunit toward recycling and membrane
CC targeting (By similarity). Interacts with IQSEC1; the interaction is
CC required for ARF6 activation (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P19491, ECO:0000250|UniProtKB:P23819}.
CC -!- INTERACTION:
CC P42262; P46459: NSF; NbExp=2; IntAct=EBI-3909876, EBI-712251;
CC P42262; Q9EP80: Pick1; Xeno; NbExp=2; IntAct=EBI-3909876, EBI-77728;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23739980,
CC ECO:0000269|PubMed:31300657}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23739980}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Postsynaptic
CC cell membrane {ECO:0000269|PubMed:23739980}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:23739980}. Postsynaptic density membrane
CC {ECO:0000250|UniProtKB:P23819}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23819}. Note=Interaction with CACNG2, CNIH2 and
CC CNIH3 promotes cell surface expression (By similarity). Displays a
CC somatodendritic localization and is excluded from axons in neurons (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P23819}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Flop;
CC IsoId=P42262-1; Sequence=Displayed;
CC Name=Flip;
CC IsoId=P42262-2; Sequence=VSP_053350;
CC Name=3; Synonyms=Long;
CC IsoId=P42262-3; Sequence=VSP_029309;
CC Name=4;
CC IsoId=P42262-4; Sequence=VSP_055920, VSP_053350;
CC -!- DOMAIN: The M4 transmembrane segment mediates tetramerization and is
CC required for cell surface expression.
CC -!- PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-610
CC palmitoylation leads to Golgi retention and decreased cell surface
CC expression. In contrast, Cys-836 palmitoylation does not affect cell
CC surface expression but regulates stimulation-dependent endocytosis (By
CC similarity). {ECO:0000250|UniProtKB:P23819}.
CC -!- PTM: Phosphorylation at Tyr-876 is required forc interaction with
CC IQSEC1 and ARF6 activation. {ECO:0000250|UniProtKB:P19491}.
CC -!- PTM: Ubiquitinated by RNF167, leading to its degradation.
CC {ECO:0000269|PubMed:23129617}.
CC -!- RNA EDITING: Modified_positions=607 {ECO:0000269|PubMed:7523595};
CC Note=Partially edited. Fully edited in the brain. Heteromerically
CC expressed edited GLUR2 (R) receptor complexes are impermeable to
CC calcium, whereas the unedited (Q) forms are highly permeable to
CC divalent ions. {ECO:0000269|PubMed:7523595};
CC -!- DISEASE: Neurodevelopmental disorder with language impairment and
CC behavioral abnormalities (NEDLIB) [MIM:618917]: A neurodevelopmental
CC disorder characterized by global developmental delay, impaired
CC intellectual development, poor or absent speech, and behavioral
CC abnormalities, such as autism spectrum disorder, repetitive behaviors,
CC and hyperactivity. Some patients develop seizures and manifest
CC developmental regression. {ECO:0000269|PubMed:31300657}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: The postsynaptic actions of Glu are mediated by a
CC variety of receptors that are named according to their selective
CC agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRIA2 subfamily. {ECO:0000305}.
CC -!- CAUTION: This entry describes variant p.Q607E that is due to a change
CC CAG to GAG at nucleotide level (PubMed:31300657). The cytosine (C) to
CC guanidine (G) change occurs immediately 5' to the adenosine (A) that is
CC edited to inosine (I) by ADAR2. This nucleotide substitution would
CC result in p.R607G in the edited version of the protein. However, ADAR2
CC recognition assays predict that the mutant codon (GAG) is edited 90%
CC less than the normal codon (CAG). {ECO:0000269|PubMed:31300657}.
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; L20814; AAA58631.1; -; mRNA.
DR EMBL; AC079233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010574; AAH10574.1; -; mRNA.
DR EMBL; BC028736; AAH28736.2; -; mRNA.
DR CCDS; CCDS3797.1; -. [P42262-2]
DR CCDS; CCDS43274.1; -. [P42262-1]
DR CCDS; CCDS43275.1; -. [P42262-4]
DR PIR; I58181; I58181.
DR RefSeq; NP_000817.2; NM_000826.3. [P42262-2]
DR RefSeq; NP_001077088.1; NM_001083619.1. [P42262-1]
DR RefSeq; NP_001077089.1; NM_001083620.1. [P42262-4]
DR RefSeq; XP_016863605.1; XM_017008116.1.
DR RefSeq; XP_016863606.1; XM_017008117.1.
DR PDB; 2WJW; X-ray; 1.80 A; A=25-412.
DR PDB; 2WJX; X-ray; 4.10 A; A/B/C=25-412.
DR PDB; 2XHD; X-ray; 1.80 A; A/B=413-527, A/B=653-796.
DR PDB; 3R7X; X-ray; 2.10 A; A/B=413-527, A/B=653-796.
DR PDB; 3RN8; X-ray; 1.70 A; A/B/C=413-527, A/B/C=653-812.
DR PDB; 3RNN; X-ray; 1.75 A; A/B/C=413-527, A/B/C=653-812.
DR PDB; 3UA8; X-ray; 1.90 A; A=413-527, A=653-796.
DR PDB; 5H8S; X-ray; 1.70 A; A/B/C=413-527, A/B/C=653-796.
DR PDB; 5YBF; X-ray; 1.50 A; A/B/C/D/E/F=413-527, A/B/C/D/E/F=653-796.
DR PDB; 5YBG; X-ray; 1.52 A; A/B/C/D/E/F=413-527, A/B/C/D/E/F=653-796.
DR PDB; 5ZG0; X-ray; 1.58 A; A/B/C/D/E/F=413-526, A/B/C/D/E/F=653-796.
DR PDB; 5ZG1; X-ray; 1.32 A; A/B=413-526, A/B=653-796.
DR PDB; 5ZG2; X-ray; 1.25 A; A/B=413-526, A/B=653-796.
DR PDB; 5ZG3; X-ray; 1.65 A; A/B/C/D/E/F=413-527, A/B/C/D/E/F=653-796.
DR PDB; 7F3O; X-ray; 1.44 A; A/B/C/D/E/F=413-527, A/B/C/D/E/F=653-796.
DR PDBsum; 2WJW; -.
DR PDBsum; 2WJX; -.
DR PDBsum; 2XHD; -.
DR PDBsum; 3R7X; -.
DR PDBsum; 3RN8; -.
DR PDBsum; 3RNN; -.
DR PDBsum; 3UA8; -.
DR PDBsum; 5H8S; -.
DR PDBsum; 5YBF; -.
DR PDBsum; 5YBG; -.
DR PDBsum; 5ZG0; -.
DR PDBsum; 5ZG1; -.
DR PDBsum; 5ZG2; -.
DR PDBsum; 5ZG3; -.
DR PDBsum; 7F3O; -.
DR AlphaFoldDB; P42262; -.
DR SMR; P42262; -.
DR BioGRID; 109148; 37.
DR CORUM; P42262; -.
DR DIP; DIP-42852N; -.
DR IntAct; P42262; 20.
DR MINT; P42262; -.
DR STRING; 9606.ENSP00000296526; -.
DR BindingDB; P42262; -.
DR ChEMBL; CHEMBL4016; -.
DR DrugBank; DB03319; (2S)-2-Ammonio-3-[5-(2-methyl-2-propanyl)-3-oxido-1,2-oxazol-4-yl]propanoate.
DR DrugBank; DB08305; (3R)-3-cyclopentyl-6-methyl-7-[(4-methylpiperazin-1-yl)sulfonyl]-3,4-dihydro-2H-1,2-benzothiazine 1,1-dioxide.
DR DrugBank; DB08304; (3R)-3-cyclopentyl-7-[(4-methylpiperazin-1-yl)sulfonyl]-3,4-dihydro-2H-1,2-benzothiazine 1,1-dioxide.
DR DrugBank; DB08303; (3S)-3-cyclopentyl-6-methyl-7-[(4-methylpiperazin-1-yl)sulfonyl]-3,4-dihydro-2H-1,2,4-benzothiadiazine 1,1-dioxide.
DR DrugBank; DB03240; (S)-2-Amino-3-(1,3,5,7-Pentahydro-2,4-Dioxo-Cyclopenta[E]Pyrimidin-1-Yl) Proionic Acid.
DR DrugBank; DB02057; (S)-AMPA.
DR DrugBank; DB01664; (S)-DES-ME-AMPA.
DR DrugBank; DB07598; 2,3,6A,7,8,9-HEXAHYDRO-11H-[1,4]DIOXINO[2,3-G]PYRROLO[2,1-B][1,3]BENZOXAZIN-11-ONE.
DR DrugBank; DB04152; 2-Amino-3-(3-Hydroxy-7,8-Dihydro-6h-Cyclohepta[D]-4-Isoxazolyl)Propionic Acid.
DR DrugBank; DB02347; 2-Amino-3-(5-Tert-Butyl-3-(Phosphonomethoxy)-4-Isoxazolyl)Propionic Acid.
DR DrugBank; DB01351; Amobarbital.
DR DrugBank; DB04599; Aniracetam.
DR DrugBank; DB01352; Aprobarbital.
DR DrugBank; DB01483; Barbital.
DR DrugBank; DB04000; Bromo-Willardiine.
DR DrugBank; DB00237; Butabarbital.
DR DrugBank; DB00241; Butalbital.
DR DrugBank; DB01353; Butobarbital.
DR DrugBank; DB05047; CX-717.
DR DrugBank; DB01496; Dihydro-2-thioxo-5-((5-(2-(trifluoromethyl)phenyl)-2-furanyl)methyl)-4,6(1H,5H)-pyrimidinedione.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB03759; FG-9041.
DR DrugBank; DB13146; Fluciclovine (18F).
DR DrugBank; DB02966; Fluoro-Willardiine.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB01354; Heptabarbital.
DR DrugBank; DB01355; Hexobarbital.
DR DrugBank; DB02818; Iodo-Willardiine.
DR DrugBank; DB00463; Metharbital.
DR DrugBank; DB00849; Methylphenobarbital.
DR DrugBank; DB07455; N,N'-[biphenyl-4,4'-diyldi(2R)propane-2,1-diyl]dimethanesulfonamide.
DR DrugBank; DB00312; Pentobarbital.
DR DrugBank; DB01174; Phenobarbital.
DR DrugBank; DB00794; Primidone.
DR DrugBank; DB01346; Quinidine barbiturate.
DR DrugBank; DB02999; Quisqualic acid.
DR DrugBank; DB00418; Secobarbital.
DR DrugBank; DB04982; Talampanel.
DR DrugBank; DB00306; Talbutal.
DR DrugBank; DB04798; THIO-ATPA.
DR DrugBank; DB00599; Thiopental.
DR DrugBank; DB04129; Willardiine.
DR DrugCentral; P42262; -.
DR GuidetoPHARMACOLOGY; 445; -.
DR TCDB; 1.A.10.1.13; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; P42262; 4 sites.
DR iPTMnet; P42262; -.
DR PhosphoSitePlus; P42262; -.
DR SwissPalm; P42262; -.
DR BioMuta; GRIA2; -.
DR DMDM; 23831146; -.
DR EPD; P42262; -.
DR MassIVE; P42262; -.
DR PaxDb; P42262; -.
DR PeptideAtlas; P42262; -.
DR PRIDE; P42262; -.
DR ProteomicsDB; 2007; -.
DR ProteomicsDB; 55498; -. [P42262-1]
DR ProteomicsDB; 55499; -. [P42262-2]
DR ProteomicsDB; 55500; -. [P42262-3]
DR ABCD; P42262; 1 sequenced antibody.
DR Antibodypedia; 1529; 670 antibodies from 47 providers.
DR DNASU; 2891; -.
DR Ensembl; ENST00000264426.14; ENSP00000264426.9; ENSG00000120251.21. [P42262-1]
DR Ensembl; ENST00000296526.12; ENSP00000296526.7; ENSG00000120251.21. [P42262-2]
DR Ensembl; ENST00000393815.6; ENSP00000377403.2; ENSG00000120251.21. [P42262-4]
DR Ensembl; ENST00000507898.5; ENSP00000426845.1; ENSG00000120251.21. [P42262-4]
DR Ensembl; ENST00000645636.1; ENSP00000495569.1; ENSG00000120251.21. [P42262-3]
DR GeneID; 2891; -.
DR KEGG; hsa:2891; -.
DR MANE-Select; ENST00000264426.14; ENSP00000264426.9; NM_001083619.3; NP_001077088.2.
DR UCSC; uc003ipk.5; human. [P42262-1]
DR CTD; 2891; -.
DR DisGeNET; 2891; -.
DR GeneCards; GRIA2; -.
DR HGNC; HGNC:4572; GRIA2.
DR HPA; ENSG00000120251; Tissue enhanced (brain, retina).
DR MalaCards; GRIA2; -.
DR MIM; 138247; gene.
DR MIM; 618917; phenotype.
DR neXtProt; NX_P42262; -.
DR OpenTargets; ENSG00000120251; -.
DR PharmGKB; PA28967; -.
DR VEuPathDB; HostDB:ENSG00000120251; -.
DR eggNOG; KOG1054; Eukaryota.
DR GeneTree; ENSGT00940000156950; -.
DR HOGENOM; CLU_007257_1_2_1; -.
DR InParanoid; P42262; -.
DR OMA; THYIMAN; -.
DR OrthoDB; 1459745at2759; -.
DR PhylomeDB; P42262; -.
DR TreeFam; TF315232; -.
DR PathwayCommons; P42262; -.
DR Reactome; R-HSA-399710; Activation of AMPA receptors.
DR Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-HSA-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-HSA-9022699; MECP2 regulates neuronal receptors and channels.
DR Reactome; R-HSA-9620244; Long-term potentiation.
DR SignaLink; P42262; -.
DR SIGNOR; P42262; -.
DR BioGRID-ORCS; 2891; 9 hits in 1071 CRISPR screens.
DR ChiTaRS; GRIA2; human.
DR EvolutionaryTrace; P42262; -.
DR GeneWiki; GRIA2; -.
DR GenomeRNAi; 2891; -.
DR Pharos; P42262; Tclin.
DR PRO; PR:P42262; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P42262; protein.
DR Bgee; ENSG00000120251; Expressed in frontal pole and 152 other tissues.
DR ExpressionAtlas; P42262; baseline and differential.
DR Genevisible; P42262; HS.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; ISS:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032279; C:asymmetric synapse; ISS:ARUK-UCL.
DR GO; GO:0030425; C:dendrite; ISS:ARUK-UCL.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0060076; C:excitatory synapse; NAS:ARUK-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; TAS:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; TAS:ARUK-UCL.
DR GO; GO:0014069; C:postsynaptic density; ISS:ARUK-UCL.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098843; C:postsynaptic endocytic zone; NAS:ARUK-UCL.
DR GO; GO:0004971; F:AMPA glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; ISS:ARUK-UCL.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; TAS:ARUK-UCL.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autism spectrum disorder;
KW Cell membrane; Disease variant; Disulfide bond; Endoplasmic reticulum;
KW Epilepsy; Glycoprotein; Intellectual disability; Ion channel;
KW Ion transport; Ligand-gated ion channel; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW RNA editing; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..883
FT /note="Glutamate receptor 2"
FT /id="PRO_0000011532"
FT TOPO_DOM 25..543
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 565..591
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 592..607
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 608..610
FT /evidence="ECO:0000250"
FT TOPO_DOM 611..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 638..812
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 813..833
FT /note="Helical; Name=M4"
FT TOPO_DOM 834..883
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 867..877
FT /note="Required for interaction with IQSEC1"
FT /evidence="ECO:0000250|UniProtKB:P19491"
FT BINDING 471
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:20614889,
FT ECO:0000269|PubMed:21531559"
FT BINDING 499..501
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 506
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:20614889,
FT ECO:0000269|PubMed:21531559"
FT BINDING 675..676
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 726
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:20614889,
FT ECO:0000269|PubMed:21531559"
FT MOD_RES 683
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P19491"
FT MOD_RES 717
FT /note="Phosphoserine; by PKG"
FT /evidence="ECO:0000250|UniProtKB:P19491"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23819"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23819"
FT MOD_RES 876
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P23819"
FT MOD_RES 880
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23819"
FT LIPID 610
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 836
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19651138"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..330
FT DISULFID 739..794
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055920"
FT VAR_SEQ 765..800
FT /note="NAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGD -> TPVNLAVLKLSE
FT QGVLDKLKNKWWYDKGECGAKDSG (in isoform Flip and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8003671"
FT /id="VSP_053350"
FT VAR_SEQ 848..883
FT /note="VAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI -> MTLNDAMRNKAR
FT LSITGSTGENGRVMTPEFPKAVHAVPYVSPGMGMNVSVTDLS (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_029309"
FT VARIANT 47
FT /note="G -> E (in NEDLIB; unknown pathological
FT significance; decreased localization to cell membrane)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084679"
FT VARIANT 302
FT /note="D -> G (in NEDLIB; severe decrease of ionotropic
FT glutamate receptor activity)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084680"
FT VARIANT 323..883
FT /note="Missing (in NEDLIB)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084681"
FT VARIANT 528..530
FT /note="Missing (in NEDLIB; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084682"
FT VARIANT 528
FT /note="P -> T (in NEDLIB)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084683"
FT VARIANT 607
FT /note="Q -> E (in NEDLIB; homomeric channels show increased
FT ionotropic glutamate receptor activity; decreased
FT localization to cell membrane)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084684"
FT VARIANT 607
FT /note="Q -> R (in RNA edited version; dbSNP:rs17850674)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8003671"
FT /id="VAR_000303"
FT VARIANT 608
FT /note="Q -> R (in dbSNP:rs17850675)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037055"
FT VARIANT 609
FT /note="G -> R (in NEDLIB; loss of ionotropic glutamate
FT receptor activity; no effect on localization to cell
FT membrane)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084685"
FT VARIANT 611
FT /note="D -> N (in NEDLIB; dbSNP:rs1553956958)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084686"
FT VARIANT 639
FT /note="A -> S (in NEDLIB; reduced ionotropic glutamate
FT receptor activity; decreased localization to cell membrane;
FT dbSNP:rs1579377564)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084687"
FT VARIANT 644
FT /note="F -> L (in NEDLIB; reduced ionotropic glutamate
FT receptor activity)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084688"
FT VARIANT 646
FT /note="T -> N (in NEDLIB; reduced ionotropic glutamate
FT receptor activity)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084689"
FT VARIANT 647
FT /note="V -> L (in NEDLIB)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084690"
FT VARIANT 776
FT /note="E -> D (in NEDLIB)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084691"
FT VARIANT 788
FT /note="W -> L (in NEDLIB)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084692"
FT VARIANT 792
FT /note="G -> V (in NEDLIB)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084693"
FT VARIANT 807
FT /note="A -> V (in NEDLIB)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084694"
FT VARIANT 812
FT /note="N -> S (in NEDLIB)"
FT /evidence="ECO:0000269|PubMed:31300657"
FT /id="VAR_084695"
FT CONFLICT 140
FT /note="I -> V (in Ref. 3; AAH10574)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="G -> E (in Ref. 1; AAA58631)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="T -> I (in Ref. 3; AAH28736)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="R -> G (in Ref. 1; AAA58631)"
FT /evidence="ECO:0000305"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:2WJW"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:2WJW"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2WJW"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2WJW"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2WJW"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:2WJW"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:2WJW"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:2WJW"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:2WJW"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:2WJW"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2WJW"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:2WJW"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:2WJW"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:2WJW"
FT HELIX 295..316
FT /evidence="ECO:0007829|PDB:2WJW"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 382..390
FT /evidence="ECO:0007829|PDB:2WJW"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:2WJW"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:5ZG2"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:5ZG2"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:5ZG2"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:5ZG2"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:5ZG2"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:5ZG2"
FT HELIX 445..457
FT /evidence="ECO:0007829|PDB:5ZG2"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:5ZG2"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:5ZG2"
FT HELIX 483..489
FT /evidence="ECO:0007829|PDB:5ZG2"
FT STRAND 494..501
FT /evidence="ECO:0007829|PDB:5ZG2"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:5ZG2"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:5ZG2"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:5ZG2"
FT STRAND 521..526
FT /evidence="ECO:0007829|PDB:5ZG2"
FT HELIX 657..661
FT /evidence="ECO:0007829|PDB:5ZG2"
FT STRAND 664..669
FT /evidence="ECO:0007829|PDB:5ZG2"
FT STRAND 671..674
FT /evidence="ECO:0007829|PDB:5ZG2"
FT HELIX 675..682
FT /evidence="ECO:0007829|PDB:5ZG2"
FT HELIX 686..697
FT /evidence="ECO:0007829|PDB:5ZG2"
FT STRAND 704..706
FT /evidence="ECO:0007829|PDB:5ZG2"
FT HELIX 707..716
FT /evidence="ECO:0007829|PDB:5ZG2"
FT TURN 717..719
FT /evidence="ECO:0007829|PDB:5ZG2"
FT STRAND 721..726
FT /evidence="ECO:0007829|PDB:5ZG2"
FT HELIX 727..734
FT /evidence="ECO:0007829|PDB:5ZG2"
FT STRAND 741..745
FT /evidence="ECO:0007829|PDB:5ZG2"
FT STRAND 751..758
FT /evidence="ECO:0007829|PDB:5ZG2"
FT HELIX 764..776
FT /evidence="ECO:0007829|PDB:5ZG2"
FT HELIX 779..788
FT /evidence="ECO:0007829|PDB:5ZG2"
FT TURN 789..791
FT /evidence="ECO:0007829|PDB:5ZG2"
SQ SEQUENCE 883 AA; 98821 MW; 6DAB96C76D1D8448 CRC64;
MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP
HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG
THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV
GNINNDKKDE MYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL
GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT TTIKYTSALT
YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI
KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT
ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI
WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD
PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF
SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL
SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK
YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLRNAVNLA VLKLNEQGLL
DKLKNKWWYD KGECGSGGGD SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR
AEAKRMKVAK NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI
