NMD3A_HUMAN
ID NMD3A_HUMAN Reviewed; 1115 AA.
AC Q8TCU5; B3DLF9; Q5VTR3; Q8TF29; Q8WXI6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 3A;
DE Short=GluN3A;
DE AltName: Full=N-methyl-D-aspartate receptor subtype 3A;
DE Short=NMDAR3A;
DE Short=NR3A;
DE AltName: Full=NMDAR-L;
DE Flags: Precursor;
GN Name=GRIN3A; Synonyms=KIAA1973;
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], AND VARIANT ARG-487.
RC TISSUE=Brain;
RX PubMed=11735224; DOI=10.1006/geno.2001.6666;
RA Andersson O., Stenqvist A., Attersand A., von Euler G.;
RT "Nucleotide sequence, genomic organization, and chromosomal localization of
RT genes encoding the human NMDA receptor subunits NR3A and NR3B.";
RL Genomics 78:178-184(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MET-362; ARG-487 AND ASN-835, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11880201; DOI=10.1016/s0304-3940(01)02524-1;
RA Eriksson M., Nilsson A., Froelich-Fabre S., Aakesson E., Dunker J.,
RA Seiger A., Folkesson R., Benedikz E., Sundstroem E.;
RT "Cloning and expression of the human NMDA receptor subunit NR3A.";
RL Neurosci. Lett. 321:177-181(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-1041.
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-1041.
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=14684485; DOI=10.1196/annals.1300.049;
RA Mueller H.T., Meador-Woodruff J.H.;
RT "Expression of the NR3A subunit of the NMDA receptor in human fetal
RT brain.";
RL Ann. N. Y. Acad. Sci. 1003:448-451(2003).
RN [7]
RP INTERACTION WITH PPP2CB.
RX PubMed=11588171; DOI=10.1523/jneurosci.21-20-07985.2001;
RA Chan S.F., Sucher N.J.;
RT "An NMDA receptor signaling complex with protein phosphatase 2A.";
RL J. Neurosci. 21:7985-7992(2001).
RN [8]
RP VARIANTS ILE-72; GLY-111; SER-116; 227-GLU--SER-1115 DEL; TRP-337; ARG-373;
RP THR-375; PRO-434; PHE-493; 508-GLN--SER-1115 DEL; SER-565; ASN-586;
RP LEU-641; SER-793; MET-921; HIS-956 AND ASN-1028.
RX PubMed=22833210; DOI=10.1038/tp.2011.52;
RG S2D team;
RA Tarabeux J., Kebir O., Gauthier J., Hamdan F.F., Xiong L., Piton A.,
RA Spiegelman D., Henrion E., Millet B., Fathalli F., Joober R.,
RA Rapoport J.L., DeLisi L.E., Fombonne E., Mottron L., Forget-Dubois N.,
RA Boivin M., Michaud J.L., Drapeau P., Lafreniere R.G., Rouleau G.A.,
RA Krebs M.O.;
RT "Rare mutations in N-methyl-D-aspartate glutamate receptors in autism
RT spectrum disorders and schizophrenia.";
RL Transl. Psychiatry 1:E55-E55(2011).
CC -!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with
CC reduced single-channel conductance, low calcium permeability and low
CC voltage-dependent sensitivity to magnesium. Mediated by glycine. During
CC the development of neural circuits, plays a role in the synaptic
CC refinement period, restricting spine maturation and growth. By
CC competing with GIT1 interaction with ARHGEF7/beta-PIX, may reduce
CC GIT1/ARHGEF7-regulated local activation of RAC1, hence affecting
CC signaling and limiting the maturation and growth of inactive synapses.
CC May also play a role in PPP2CB-NMDAR mediated signaling mechanism.
CC {ECO:0000250|UniProtKB:Q9R1M7}.
CC -!- SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon
CC subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A
CC or GRIN3B). Does not form functional homomeric channels. Found in a
CC complex with GRIN1, GRIN2A or GRIN2B and PPP2CB (By similarity).
CC Probably interacts with PPP2CB. No complex with PPP2CB is detected when
CC NMDARs are stimulated by NMDA (PubMed:11588171). Interacts (via C-
CC terminus) with GIT1, but not with GRIA1/GluA1, nor with
CC synaptophysin/SYP; this interaction competes with GIT1 interaction with
CC ARHGEF7/beta-PIX (By similarity). {ECO:0000250|UniProtKB:Q9R1M7,
CC ECO:0000269|PubMed:11588171}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9R1M7};
CC Multi-pass membrane protein {ECO:0000250}. Postsynaptic cell membrane
CC {ECO:0000250}. Postsynaptic density {ECO:0000250}. Note=Enriched in
CC postsynaptic plasma membrane and postsynaptic densities. Requires the
CC presence of GRIN1 to be targeted at the plasma membrane (By
CC similarity). {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain.
CC {ECO:0000269|PubMed:14684485}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. NR3A/GRIN3A subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85559.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF416558; AAL40734.1; -; mRNA.
DR EMBL; AJ416950; CAC95229.2; -; mRNA.
DR EMBL; AB075853; BAB85559.1; ALT_INIT; mRNA.
DR EMBL; AL591377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC167432; AAI67432.1; -; mRNA.
DR CCDS; CCDS6758.1; -.
DR RefSeq; NP_597702.2; NM_133445.2.
DR AlphaFoldDB; Q8TCU5; -.
DR SMR; Q8TCU5; -.
DR BioGRID; 125508; 6.
DR CORUM; Q8TCU5; -.
DR STRING; 9606.ENSP00000355155; -.
DR ChEMBL; CHEMBL4787; -.
DR DrugBank; DB00659; Acamprosate.
DR DrugBank; DB06151; Acetylcysteine.
DR DrugBank; DB00915; Amantadine.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB00289; Atomoxetine.
DR DrugBank; DB00514; Dextromethorphan.
DR DrugBank; DB00843; Donepezil.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB11823; Esketamine.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB13146; Fluciclovine (18F).
DR DrugBank; DB06741; Gavestinel.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00874; Guaifenesin.
DR DrugBank; DB01159; Halothane.
DR DrugBank; DB01221; Ketamine.
DR DrugBank; DB06738; Ketobemidone.
DR DrugBank; DB09409; Magnesium acetate tetrahydrate.
DR DrugBank; DB09481; Magnesium carbonate.
DR DrugBank; DB01043; Memantine.
DR DrugBank; DB00333; Methadone.
DR DrugBank; DB04896; Milnacipran.
DR DrugBank; DB04926; Neramexane.
DR DrugBank; DB01173; Orphenadrine.
DR DrugBank; DB00312; Pentobarbital.
DR DrugBank; DB03575; Phencyclidine.
DR DrugBank; DB01174; Phenobarbital.
DR DrugBank; DB01708; Prasterone.
DR DrugBank; DB00721; Procaine.
DR DrugBank; DB00392; Profenamine.
DR DrugBank; DB01549; Rolicyclidine.
DR DrugBank; DB00418; Secobarbital.
DR DrugBank; DB01520; Tenocyclidine.
DR DrugBank; DB00193; Tramadol.
DR DrugCentral; Q8TCU5; -.
DR GlyGen; Q8TCU5; 11 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TCU5; -.
DR PhosphoSitePlus; Q8TCU5; -.
DR BioMuta; GRIN3A; -.
DR DMDM; 212276445; -.
DR MassIVE; Q8TCU5; -.
DR PaxDb; Q8TCU5; -.
DR PeptideAtlas; Q8TCU5; -.
DR PRIDE; Q8TCU5; -.
DR ProteomicsDB; 74174; -.
DR Antibodypedia; 54489; 29 antibodies from 10 providers.
DR DNASU; 116443; -.
DR Ensembl; ENST00000361820.6; ENSP00000355155.3; ENSG00000198785.7.
DR GeneID; 116443; -.
DR KEGG; hsa:116443; -.
DR MANE-Select; ENST00000361820.6; ENSP00000355155.3; NM_133445.3; NP_597702.2.
DR UCSC; uc004bbp.3; human.
DR CTD; 116443; -.
DR DisGeNET; 116443; -.
DR GeneCards; GRIN3A; -.
DR HGNC; HGNC:16767; GRIN3A.
DR HPA; ENSG00000198785; Tissue enhanced (brain).
DR MIM; 606650; gene.
DR neXtProt; NX_Q8TCU5; -.
DR OpenTargets; ENSG00000198785; -.
DR PharmGKB; PA28983; -.
DR VEuPathDB; HostDB:ENSG00000198785; -.
DR eggNOG; KOG1053; Eukaryota.
DR GeneTree; ENSGT00940000158571; -.
DR HOGENOM; CLU_002039_0_0_1; -.
DR InParanoid; Q8TCU5; -.
DR OMA; VGNSQHA; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q8TCU5; -.
DR TreeFam; TF314731; -.
DR PathwayCommons; Q8TCU5; -.
DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors.
DR SignaLink; Q8TCU5; -.
DR BioGRID-ORCS; 116443; 12 hits in 1070 CRISPR screens.
DR ChiTaRS; GRIN3A; human.
DR GeneWiki; GRIN3A; -.
DR GenomeRNAi; 116443; -.
DR Pharos; Q8TCU5; Tclin.
DR PRO; PR:Q8TCU5; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8TCU5; protein.
DR Bgee; ENSG00000198785; Expressed in Brodmann (1909) area 46 and 117 other tissues.
DR Genevisible; Q8TCU5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IEA:Ensembl.
DR GO; GO:0016594; F:glycine binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0042165; F:neurotransmitter binding; IEA:Ensembl.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IEA:Ensembl.
DR GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0061000; P:negative regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0060134; P:prepulse inhibition; IEA:Ensembl.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IDA:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:Ensembl.
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 Calcium; Cell membrane; Coiled coil; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Magnesium; Membrane;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1115
FT /note="Glutamate receptor ionotropic, NMDA 3A"
FT /id="PRO_0000011568"
FT TOPO_DOM 24..674
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 675..695
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 696..748
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 770..930
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 931..951
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 952..1115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 59..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..987
FT /note="PPP2CB binding site"
FT /evidence="ECO:0000250"
FT REGION 1062..1095
FT /note="GIT1-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9R1M7"
FT COILED 1058..1109
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 72
FT /note="S -> I (in dbSNP:rs558734093)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079892"
FT VARIANT 111
FT /note="R -> G (found in a patient with autism spectrum
FT disorder; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079893"
FT VARIANT 116
FT /note="G -> S (in dbSNP:rs111415222)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079894"
FT VARIANT 227..1115
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079895"
FT VARIANT 337
FT /note="R -> W (in dbSNP:rs773593066)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079896"
FT VARIANT 362
FT /note="V -> M (in dbSNP:rs10989591)"
FT /evidence="ECO:0000269|PubMed:11880201"
FT /id="VAR_019672"
FT VARIANT 373
FT /note="G -> R (found in a patient with autism spectrum
FT disorder; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079897"
FT VARIANT 375
FT /note="I -> T (in dbSNP:rs144427058)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079898"
FT VARIANT 434
FT /note="S -> P (in dbSNP:rs776062103)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079899"
FT VARIANT 480
FT /note="R -> H (in dbSNP:rs34755188)"
FT /id="VAR_047150"
FT VARIANT 487
FT /note="G -> R (in dbSNP:rs10989589)"
FT /evidence="ECO:0000269|PubMed:11735224,
FT ECO:0000269|PubMed:11880201"
FT /id="VAR_019673"
FT VARIANT 493
FT /note="Y -> F (in dbSNP:rs773322226)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079900"
FT VARIANT 508..1115
FT /note="Missing (probable disease-associated variant found
FT in a patient with schizophrenia)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079901"
FT VARIANT 565
FT /note="N -> S (in dbSNP:rs371244839)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079902"
FT VARIANT 586
FT /note="K -> N (in dbSNP:rs142284927)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079903"
FT VARIANT 641
FT /note="V -> L (found in a patient with autism spectrum
FT disorder; unknown pathological significance;
FT dbSNP:rs1360008284)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079904"
FT VARIANT 793
FT /note="R -> S (in dbSNP:rs144770241)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079905"
FT VARIANT 835
FT /note="D -> N (in dbSNP:rs10989563)"
FT /evidence="ECO:0000269|PubMed:11880201"
FT /id="VAR_019674"
FT VARIANT 921
FT /note="T -> M (in dbSNP:rs144712629)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079906"
FT VARIANT 956
FT /note="Y -> H (in dbSNP:rs141253502)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079907"
FT VARIANT 1028
FT /note="I -> N (found in a patient with schizophrenia;
FT unknown pathological significance; dbSNP:rs755464674)"
FT /evidence="ECO:0000269|PubMed:22833210"
FT /id="VAR_079908"
FT VARIANT 1041
FT /note="R -> Q (in dbSNP:rs3739722)"
FT /evidence="ECO:0000269|PubMed:11853319,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_019675"
FT CONFLICT 559
FT /note="S -> N (in Ref. 1; AAL40734)"
FT /evidence="ECO:0000305"
FT CONFLICT 977
FT /note="Q -> R (in Ref. 1; AAL40734)"
FT /evidence="ECO:0000305"
FT CONFLICT 1073
FT /note="N -> I (in Ref. 1; AAL40734)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1115 AA; 125465 MW; 0FEEC995F6AAF940 CRC64;
MRRLSLWWLL SRVCLLLPPP CALVLAGVPS SSSHPQPCQI LKRIGHAVRV GAVHLQPWTT
APRAASRAPD DSRAGAQRDE PEPGTRRSPA PSPGARWLGS TLHGRGPPGS RKPGEGARAE
ALWPRDALLF AVDNLNRVEG LLPYNLSLEV VMAIEAGLGD LPLLPFSSPS SPWSSDPFSF
LQSVCHTVVV QGVSALLAFP QSQGEMMELD LVSLVLHIPV ISIVRHEFPR ESQNPLHLQL
SLENSLSSDA DVTVSILTMN NWYNFSLLLC QEDWNITDFL LLTQNNSKFH LGSIINITAN
LPSTQDLLSF LQIQLESIKN STPTVVMFGC DMESIRRIFE ITTQFGVMPP ELRWVLGDSQ
NVEELRTEGL PLGLIAHGKT TQSVFEHYVQ DAMELVARAV ATATMIQPEL ALIPSTMNCM
EVETTNLTSG QYLSRFLANT TFRGLSGSIR VKGSTIVSSE NNFFIWNLQH DPMGKPMWTR
LGSWQGGKIV MDYGIWPEQA QRHKTHFQHP SKLHLRVVTL IEHPFVFTRE VDDEGLCPAG
QLCLDPMTND SSTLDSLFSS LHSSNDTVPI KFKKCCYGYC IDLLEKIAED MNFDFDLYIV
GDGKYGAWKN GHWTGLVGDL LRGTAHMAVT SFSINTARSQ VIDFTSPFFS TSLGILVRTR
DTAAPIGAFM WPLHWTMWLG IFVALHITAV FLTLYEWKSP FGLTPKGRNR SKVFSFSSAL
NICYALLFGR TVAIKPPKCW TGRFLMNLWA IFCMFCLSTY TANLAAVMVG EKIYEELSGI
HDPKLHHPSQ GFRFGTVRES SAEDYVRQSF PEMHEYMRRY NVPATPDGVE YLKNDPEKLD
AFIMDKALLD YEVSIDADCK LLTVGKPFAI EGYGIGLPPN SPLTANISEL ISQYKSHGFM
DMLHDKWYRV VPCGKRSFAV TETLQMGIKH FSGLFVLLCI GFGLSILTTI GEHIVYRLLL
PRIKNKSKLQ YWLHTSQRLH RAINTSFIEE KQQHFKTKRV EKRSNVGPRQ LTVWNTSNLS
HDNRRKYIFS DEEGQNQLGI RIHQDIPLPP RRRELPALRT TNGKADSLNV SRNSVMQELS
ELEKQIQVIR QELQLAVSRK TELEEYQRTS RTCES
