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UniProtKB/Swiss-Prot entry P42263

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GRIA3_HUMAN
Primary accession number P42263
Secondary accession numbers Q4VXD5 Q4VXD6 Q9HDA0 Q9HDA1 Q9HDA2
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on October 11, 2005 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 95)
Name and origin of the protein
Protein name Glutamate receptor 3 [Precursor]
Synonyms GluR-3
GluR-C
GluR-K3
Glutamate receptor ionotropic, AMPA 3
AMPA-selective glutamate receptor 3
Gene name
Name: GRIA3
Synonyms: GLUR3, GLURC
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS FLIP AND FLOP), AND VARIANT LEU-525.
TISSUE=Hippocampus;
DOI=10.1016/0167-4781(94)90090-6; PubMed=7918660 [NCBI, ExPASy, EBI, Israel, Japan]
Rampersad V., Elliott C.E., Nutt S.L., Foldes R.L., Kamboj R.K.;
"Human glutamate receptor hGluR3 flip and flop isoforms: cloning and sequencing of the cDNAs and primary structure of the proteins.";
Biochim. Biophys. Acta 1219:563-566(1994).
[2]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
McLaughlin D.P., Kerwin R.W.;
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-525.
DOI=10.1002/(SICI)1096-8628(20000103)90:1<69::AID-AJMG12>3.3.CO;2-N; PubMed=10602120 [NCBI, ExPASy, EBI, Israel, Japan]
Amir R., Dahle E.J., Toriolo D., Zoghbi H.Y.;
"Candidate gene analysis in Rett syndrome and the identification of 21 SNPs in Xq.";
Am. J. Med. Genet. 90:69-71(2000).
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03440; PubMed=15772651 [NCBI, ExPASy, EBI, Israel, Japan]
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
 VARIANTS MRX94 GLN-450; SER-631; THR-706 AND ARG-833, AND CHARACTERIZATION OF VARIANTS MRX94 SER-631; THR-706 AND ARG-833.
DOI=10.1073/pnas.0708699104; PubMed=17989220 [NCBI, ExPASy, EBI, Israel, Japan]
Wu Y., Arai A.C., Rumbaugh G., Srivastava A.K., Turner G., Hayashi T., Suzuki E., Jiang Y., Zhang L., Rodriguez J., Boyle J., Tarpey P., Raymond F.L., Nevelsteen J., Froyen G., Stratton M., Futreal A., Gecz J., Stevenson R., Schwartz C.E., Valle D., Huganir R.L., Wang T.;
"Mutations in ionotropic AMPA receptor 3 alter channel properties and are associated with moderate cognitive impairment in humans.";
Proc. Natl. Acad. Sci. U.S.A. 104:18163-18168(2007).
Comments
  • FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist.
  • SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with PRKCABP, GRIP1 and GRIP2 (By similarity).
  • SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    NameFlop
    Isoform IDP42263-1
    This is the isoform sequence displayed in this entry.
    NameFlip
    Isoform IDP42263-2
    Features which should be applied to build the isoform sequence: VSP_000115, VSP_000116, VSP_000117, VSP_000118.
  • PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-621 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-847 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity).
  • DISEASE: Defects in GRIA3 are the cause of mental retardation X-linked type 94 (MRX94) [MIM:300699]. Mental retardation is characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. MRX94 patients have moderate mental retardation. Other variable features are macrocephaly, seizures, myoclonic jerks, autistic behavior, asthenic body habitus, distal muscle weakness and hyporeflexia.
  • MISCELLANEOUS: The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate.
  • SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10) family [view classification].
  • CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U10302; AAA67923.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U10301; AAA67922.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X82068; CAA57567.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166365; AAF97857.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166362; AAF97857.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166363; AAF97857.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166364; AAF97857.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF167332; AAF97858.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166366; AAF97858.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166367; AAF97858.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166368; AAF97858.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166369; AAF97858.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166370; AAF97858.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166371; AAF97858.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166372; AAF97858.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166373; AAF97858.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166375; AAF97858.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF167332; AAF97859.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166366; AAF97859.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166367; AAF97859.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166368; AAF97859.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166369; AAF97859.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166370; AAF97859.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166371; AAF97859.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166372; AAF97859.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166373; AAF97859.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF166374; AAF97859.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356213; CAI95643.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035426; CAI95643.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590139; CAI95643.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z83848; CAI95643.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z82899; CAI95643.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356213; CAI95644.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035426; CAI95644.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590139; CAI95644.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z83848; CAI95644.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z82899; CAI95644.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590139; CAI95164.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035426; CAI95164.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356213; CAI95164.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z83848; CAI95164.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z82899; CAI95164.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590139; CAI95165.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035426; CAI95165.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356213; CAI95165.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z83848; CAI95165.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z82899; CAI95165.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z83848; CAI95709.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590139; CAI95709.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356213; CAI95709.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035426; CAI95709.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z82899; CAI95709.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z83848; CAI95710.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590139; CAI95710.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356213; CAI95710.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035426; CAI95710.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z82899; CAI95710.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z82899; CAI95664.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z83848; CAI95664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590139; CAI95664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356213; CAI95664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035426; CAI95664.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z82899; CAI95665.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z83848; CAI95665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590139; CAI95665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356213; CAI95665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035426; CAI95665.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035426; CAI95683.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z83848; CAI95683.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z82899; CAI95683.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590139; CAI95683.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356213; CAI95683.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035426; CAI95684.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z83848; CAI95684.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z82899; CAI95684.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590139; CAI95684.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356213; CAI95684.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00219315; -.
IPI00298700; -.
PIR S49460; S49460.
S50128; S50128.
S53696; S53696.
UniGene Hs.377070
3D structure databases
HSSP P19491; 1FTK. [HSSP ENTRY / PDB]
SMR P42263; 422-536, 663-806.
ModBase P42263.
Protein family/group databases
TCDB 1.A.10.1.4; glutamate-gated ion channel (GIC) family of neurotransmitter receptors.
PTM databases
PhosphoSite P42263; -.
Organism-specific databases
GeneCards GC0XP122145; -.
HGNC HGNC:4573; GRIA3.
GenAtlas GRIA3.
HPA CAB007799; -.
MIM 300699; phenotype. [NCBI / EBI]
305915; gene. [NCBI / EBI]
Orphanet 98463; X-linked intellectual deficit.
PharmGKB PA28968; -.
Gene expression databases
ArrayExpress P42263; -.
Bgee P42263; -.
CleanEx HS_GRIA3; -.
GermOnline ENSG00000125675; Homo sapiens.
Ontologies
GO
GO:0030054; Cellular component: cell junction (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0045211; Cellular component: postsynaptic membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005234; Molecular function: extracellular-glutamate-gated ion channel activity (inferred from electronic annotation from InterPro).
GO:0004970; Molecular function: ionotropic glutamate receptor activity (inferred from electronic annotation from InterPro).
GO:0007215; Biological process: glutamate signaling pathway (traceable author statement from ProtInc).
GO:0006811; Biological process: ion transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001828; ANF_lig_bd_rcpt.
IPR019594; Glu_rcpt_Glu/Gly-bd.
IPR015683; Glutamate_receptor-rel.
IPR001320; Iontro_glu_rcpt.
IPR001508; NMDA_rcpt.
Graphical view of domain structure.
PANTHER PTHR18966; Glut_Rec_Related; 1.
Pfam PF01094; ANF_receptor; 1.
PF00060; Lig_chan; 1.
PF10613; Lig_chan-Glu_bd; 1.
Pfam graphical view of domain structure.
PRINTS PR00177; NMDARECEPTOR.
SMART SM00079; PBPe; 1.
SMART graphical view of domain structure.
Genome annotation databases
Ensembl ENSG00000125675; Homo sapiens. [Contig view]
Phylogenomic databases
HOVERGEN P42263; -.
OMA P42263; VYEMKVT.
Other
DrugBank DB00142; L-Glutamic Acid.
SOURCE GRIA3; Homo sapiens.
ProtoNet P42263.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cell junction; Cell membrane; Disease mutation; Glycoprotein; Ion transport; Ionic channel; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    28  28     Potential. 
CHAIN   29   894  866     Glutamate receptor 3. PRO_0000011536
TOPO_DOM   29   552  524     Extracellular (Potential). 
TRANSMEM   553   573  21     Potential. 
TOPO_DOM   574   635  62     Cytoplasmic (Potential). 
TRANSMEM   636   656  21     Potential. 
TOPO_DOM   657   823  167     Extracellular (Potential). 
TRANSMEM   824   844  21     Potential. 
TOPO_DOM   845   894  50     Cytoplasmic (Potential). 
REGION   508   510  3     Glutamate binding (By similarity). 
REGION   686   687  2     Glutamate binding (By similarity). 
BINDING   515   515        Glutamate (By similarity). 
BINDING   737   737        Glutamate (By similarity). 
MOD_RES   877   877        Phosphotyrosine (By similarity). 
MOD_RES   887   887        Phosphotyrosine (By similarity). 
LIPID   621   621        S-palmitoyl cysteine (By similarity). 
LIPID   847   847        S-palmitoyl cysteine (By similarity). 
CARBOHYD   63    63        N-linked (GlcNAc...) (Potential). 
CARBOHYD   266   266        N-linked (GlcNAc...) (Potential). 
CARBOHYD   380   380        N-linked (GlcNAc...) (Potential). 
CARBOHYD   415   415        N-linked (GlcNAc...) (Potential). 
CARBOHYD   422   422        N-linked (GlcNAc...) (Potential). 
VAR_SEQ   776   777        NA -> TP (in isoform Flip). VSP_000115
VAR_SEQ   786   786        N -> S (in isoform Flip). VSP_000116
VAR_SEQ   790   790        L -> I (in isoform Flip). VSP_000117
VAR_SEQ   807   811        SGGGD -> AKDSG (in isoform Flip). VSP_000118
VARIANT   450   450  1     R -> Q (in MRX94). VAR_043484 
VARIANT   525   525  1     F -> L (in dbSNP:rs1052538 [NCBI]). VAR_023579 
VARIANT   631   631  1     R -> S (in MRX94; homomers have minimal or no current; heteromers have altered desensitization kinetics). VAR_043485 
VARIANT   706   706  1     M -> T (in MRX94; homomers have minimal or no current; heteromers have altered desensitization kinetics). VAR_043486 
VARIANT   833   833  1     G -> R (in MRX94; reduced receptor expression possibly due to rapid degradation). VAR_043487 
CONFLICT   775   775        R -> G (in Ref. 1 and 2). 
Sequence information
Length: 894 AA [This is the length of the unprocessed precursor] Molecular weight: 101157 Da [This is the MW of the unprocessed precursor] CRC64: 178589A870E0D102 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MARQKKMGQS VLRAVFFLVL GLLGHSHGGF PNTISIGGLF MRNTVQEHSA FRFAVQLYNT 

        70         80         90        100        110        120 
NQNTTEKPFH LNYHVDHLDS SNSFSVTNAF CSQFSRGVYA IFGFYDQMSM NTLTSFCGAL 

       130        140        150        160        170        180 
HTSFVTPSFP TDADVQFVIQ MRPALKGAIL SLLGHYKWEK FVYLYDTERG FSILQAIMEA 

       190        200        210        220        230        240 
AVQNNWQVTA RSVGNIKDVQ EFRRIIEEMD RRQEKRYLID CEVERINTIL EQVVILGKHS 

       250        260        270        280        290        300 
RGYHYMLANL GFTDILLERV MHGGANITGF QIVNNENPMV QQFIQRWVRL DEREFPEAKN 

       310        320        330        340        350        360 
APLKYTSALT HDAILVIAEA FRYLRRQRVD VSRRGSAGDC LANPAVPWSQ GIDIERALKM 

       370        380        390        400        410        420 
VQVQGMTGNI QFDTYGRRTN YTIDVYEMKV SGSRKAGYWN EYERFVPFSD QQISNDSASS 

       430        440        450        460        470        480 
ENRTIVVTTI LESPYVMYKK NHEQLEGNER YEGYCVDLAY EIAKHVRIKY KLSIVGDGKY 

       490        500        510        520        530        540 
GARDPETKIW NGMVGELVYG RADIAVAPLT ITLVREEVID FSKPFMSLGI SIMIKKPQKS 

       550        560        570        580        590        600 
KPGVFSFLDP LAYEIWMCIV FAYIGVSVVL FLVSRFSPYE WHLEDNNEEP RDPQSPPDPP 

       610        620        630        640        650        660 
NEFGIFNSLW FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA NLAAFLTVER 

       670        680        690        700        710        720 
MVSPIESAED LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWSYMKSAE PSVFTKTTAD 

       730        740        750        760        770        780 
GVARVRKSKG KFAFLLESTM NEYIEQRKPC DTMKVGGNLD SKGYGVATPK GSALRNAVNL 

       790        800        810        820        830        840 
AVLKLNEQGL LDKLKNKWWY DKGECGSGGG DSKDKTSALS LSNVAGVFYI LVGGLGLAMM 

       850        860        870        880        890 
VALIEFCYKS RAESKRMKLT KNTQNFKPAP ATNTQNYATY REGYNVYGTE SVKI
P42263 in FASTA format

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