ID   GRID2_HUMAN             Reviewed;        1007 AA.
AC   O43424; E9PH24; Q4KKU8; Q4KKU9; Q4KKV0; Q59FZ1;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=Glutamate receptor ionotropic, delta-2;
DE            Short=GluD2;
DE            Short=GluR delta-2 subunit;
DE   Flags: Precursor;
GN   Name=GRID2; Synonyms=GLURD2;
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 1).
RC   TISSUE=Cerebellum;
RX   PubMed=9465309; DOI=10.1006/geno.1997.5108;
RA   Hu W., Zuo J., De Jager P.L., Heintz N.;
RT   "The human glutamate receptor delta 2 gene (GRID2) maps to chromosome
RT   4q22.";
RL   Genomics 47:143-145(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-68.
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 24-440, DISULFIDE BONDS,
RP   INTERACTION WITH CBLN1, MUTAGENESIS OF ASP-24; SER-25; ILE-26; THR-60;
RP   GLU-61; PHE-76; LEU-342; GLU-343; ASP-344; ARG-345; LYS-346; HIS-348;
RP   SER-349; MET-350; SER-352; GLN-364 AND LEU-434, SUBUNIT, FUNCTION, REGION,
RP   SITE, AND CHARACTERIZATION OF VARIANT SCAR18 THR-654.
RX   PubMed=27418511; DOI=10.1126/science.aae0104;
RA   Elegheert J., Kakegawa W., Clay J.E., Shanks N.F., Behiels E., Matsuda K.,
RA   Kohda K., Miura E., Rossmann M., Mitakidis N., Motohashi J., Chang V.T.,
RA   Siebold C., Greger I.H., Nakagawa T., Yuzaki M., Aricescu A.R.;
RT   "Structural basis for integration of GluD receptors within synaptic
RT   organizer complexes.";
RL   Science 353:295-299(2016).
RN   [6]
RP   INVOLVEMENT IN SCAR18.
RX   PubMed=23611888; DOI=10.1177/0883073813484967;
RA   Utine G.E., Haliloglu G., Salanci B., Cetinkaya A., Kiper P.O., Alanay Y.,
RA   Aktas D., Boduroglu K., Alikasifoglu M.;
RT   "A homozygous deletion in GRID2 causes a human phenotype with cerebellar
RT   ataxia and atrophy.";
RL   J. Child Neurol. 28:926-932(2013).
RN   [7]
RP   INVOLVEMENT IN SCAR18.
RX   PubMed=24078737; DOI=10.1212/wnl.0b013e3182a841a3;
RA   Hills L.B., Masri A., Konno K., Kakegawa W., Lam A.T., Lim-Melia E.,
RA   Chandy N., Hill R.S., Partlow J.N., Al-Saffar M., Nasir R., Stoler J.M.,
RA   Barkovich A.J., Watanabe M., Yuzaki M., Mochida G.H.;
RT   "Deletions in GRID2 lead to a recessive syndrome of cerebellar ataxia and
RT   tonic upgaze in humans.";
RL   Neurology 81:1378-1386(2013).
RN   [8]
RP   VARIANT [LARGE SCALE ANALYSIS] ASN-209.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [9]
RP   VARIANTS SCAR18 ASP-654; THR-654 AND VAL-656.
RX   PubMed=25841024; DOI=10.1212/wnl.0000000000001524;
RA   Coutelier M., Burglen L., Mundwiller E., Abada-Bendib M., Rodriguez D.,
RA   Chantot-Bastaraud S., Rougeot C., Cournelle M.A., Milh M., Toutain A.,
RA   Bacq D., Meyer V., Afenjar A., Deleuze J.F., Brice A., Heron D.,
RA   Stevanin G., Durr A.;
RT   "GRID2 mutations span from congenital to mild adult-onset cerebellar
RT   ataxia.";
RL   Neurology 84:1751-1759(2015).
CC   -!- FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory
CC       neurotransmitter at many synapses in the central nervous system. The
CC       postsynaptic actions of Glu are mediated by a variety of receptors that
CC       are named according to their selective agonists. Promotes
CC       synaptogenesis and mediates the D-Serine-dependent long term depression
CC       signals and AMPA receptor endocytosis of cerebellar parallel fiber-
CC       Purkinje cell (PF-PC) synapses through the beta-NRX1-CBLN1-GRID2 triad
CC       complex (PubMed:27418511). {ECO:0000269|PubMed:27418511}.
CC   -!- SUBUNIT: Tetramer; dimer of dimers (PubMed:27418511). Interacts with
CC       EML2, MAGI2 (via PDZ domains) and AP4M1 (By similarity). Interacts with
CC       BECN1, GOPC, GRID2IP, SHANK1 and SHANK2. Interacts with CBLN2, but not
CC       with CBLN4 (By similarity). Interacts with CBLN1 (via C1q domain); the
CC       interaction is CBLN1-NRX1 complex formation-dependent; CBLN1-binding is
CC       calcium-independent; CBLN1 hexamers anchor GRID2 N-terminal domain
CC       dimers to monomeric NRXN1 isoform beta; promotes synaptogenesis and
CC       mediates the D-Serine-dependent long term depression signals and AMPA
CC       receptor endocytosis (PubMed:27418511). {ECO:0000250|UniProtKB:Q61625,
CC       ECO:0000250|UniProtKB:Q63226, ECO:0000269|PubMed:27418511}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O43424-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O43424-2; Sequence=VSP_054704;
CC   -!- DOMAIN: The PDZ-binding motif mediates interaction with GOPC.
CC       {ECO:0000250}.
CC   -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 18 (SCAR18)
CC       [MIM:616204]: A form of spinocerebellar ataxia, a clinically and
CC       genetically heterogeneous group of cerebellar disorders. Patients show
CC       progressive incoordination of gait and often poor coordination of
CC       hands, speech and eye movements, due to degeneration of the cerebellum
CC       with variable involvement of the brainstem and spinal cord. SCAR18
CC       features include progressive cerebellar atrophy, delayed psychomotor
CC       development, severely impaired gait, ocular movement abnormalities, and
CC       intellectual disability. {ECO:0000269|PubMed:23611888,
CC       ECO:0000269|PubMed:24078737, ECO:0000269|PubMed:25841024,
CC       ECO:0000269|PubMed:27418511}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. GRID2 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD92555.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF009014; AAC39579.1; -; mRNA.
DR   EMBL; AB209318; BAD92555.1; ALT_INIT; mRNA.
DR   EMBL; AC020699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC022317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC093596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC093733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC095059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC096769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC104077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC105315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC105452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC108158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC110800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC112695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC115111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC115537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC099652; AAH99652.1; -; mRNA.
DR   EMBL; BC099653; AAH99653.1; -; mRNA.
DR   EMBL; BC099654; AAH99654.1; -; mRNA.
DR   CCDS; CCDS3637.1; -. [O43424-1]
DR   CCDS; CCDS68758.1; -. [O43424-2]
DR   RefSeq; NP_001273767.1; NM_001286838.1. [O43424-2]
DR   RefSeq; NP_001501.2; NM_001510.3. [O43424-1]
DR   PDB; 5KC8; X-ray; 1.75 A; A=24-440.
DR   PDB; 5KCA; X-ray; 3.10 A; A=24-440.
DR   PDBsum; 5KC8; -.
DR   PDBsum; 5KCA; -.
DR   AlphaFoldDB; O43424; -.
DR   SMR; O43424; -.
DR   BioGRID; 109152; 10.
DR   IntAct; O43424; 1.
DR   MINT; O43424; -.
DR   STRING; 9606.ENSP00000282020; -.
DR   ChEMBL; CHEMBL4524129; -.
DR   GlyCosmos; O43424; 4 sites, No reported glycans.
DR   GlyGen; O43424; 4 sites.
DR   iPTMnet; O43424; -.
DR   PhosphoSitePlus; O43424; -.
DR   BioMuta; GRID2; -.
DR   EPD; O43424; -.
DR   jPOST; O43424; -.
DR   MassIVE; O43424; -.
DR   MaxQB; O43424; -.
DR   PaxDb; 9606-ENSP00000282020; -.
DR   PeptideAtlas; O43424; -.
DR   ProteomicsDB; 20442; -.
DR   ProteomicsDB; 48936; -. [O43424-1]
DR   Pumba; O43424; -.
DR   Antibodypedia; 25698; 145 antibodies from 27 providers.
DR   DNASU; 2895; -.
DR   Ensembl; ENST00000282020.9; ENSP00000282020.4; ENSG00000152208.13. [O43424-1]
DR   Ensembl; ENST00000510992.5; ENSP00000421257.1; ENSG00000152208.13. [O43424-2]
DR   GeneID; 2895; -.
DR   KEGG; hsa:2895; -.
DR   MANE-Select; ENST00000282020.9; ENSP00000282020.4; NM_001510.4; NP_001501.2.
DR   UCSC; uc011cdt.4; human. [O43424-1]
DR   AGR; HGNC:4576; -.
DR   CTD; 2895; -.
DR   DisGeNET; 2895; -.
DR   GeneCards; GRID2; -.
DR   HGNC; HGNC:4576; GRID2.
DR   HPA; ENSG00000152208; Group enriched (brain, testis).
DR   MalaCards; GRID2; -.
DR   MIM; 602368; gene.
DR   MIM; 616204; phenotype.
DR   neXtProt; NX_O43424; -.
DR   OpenTargets; ENSG00000152208; -.
DR   Orphanet; 363432; Autosomal recessive congenital cerebellar ataxia due to GRID2 deficiency.
DR   PharmGKB; PA28971; -.
DR   VEuPathDB; HostDB:ENSG00000152208; -.
DR   eggNOG; KOG1052; Eukaryota.
DR   GeneTree; ENSGT00940000155192; -.
DR   InParanoid; O43424; -.
DR   OMA; EXISNLY; -.
DR   OrthoDB; 511851at2759; -.
DR   PhylomeDB; O43424; -.
DR   TreeFam; TF352434; -.
DR   PathwayCommons; O43424; -.
DR   SignaLink; O43424; -.
DR   SIGNOR; O43424; -.
DR   BioGRID-ORCS; 2895; 6 hits in 1151 CRISPR screens.
DR   ChiTaRS; GRID2; human.
DR   GeneWiki; GRID2; -.
DR   GenomeRNAi; 2895; -.
DR   Pharos; O43424; Tbio.
DR   PRO; PR:O43424; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; O43424; Protein.
DR   Bgee; ENSG00000152208; Expressed in right testis and 77 other cell types or tissues.
DR   ExpressionAtlas; O43424; baseline and differential.
DR   GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0008328; C:ionotropic glutamate receptor complex; ISS:BHF-UCL.
DR   GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR   GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; ISS:BHF-UCL.
DR   GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0030165; F:PDZ domain binding; ISS:BHF-UCL.
DR   GO; GO:0097110; F:scaffold protein binding; ISS:BHF-UCL.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0021707; P:cerebellar granule cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; ISS:BHF-UCL.
DR   GO; GO:1904861; P:excitatory synapse assembly; IMP:UniProtKB.
DR   GO; GO:0007215; P:glutamate receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:BHF-UCL.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:1900454; P:positive regulation of long-term synaptic depression; IMP:UniProtKB.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IMP:UniProtKB.
DR   GO; GO:0060134; P:prepulse inhibition; ISS:BHF-UCL.
DR   GO; GO:0008104; P:protein localization; ISS:BHF-UCL.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:BHF-UCL.
DR   GO; GO:0010975; P:regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:0099151; P:regulation of postsynaptic density assembly; IEA:Ensembl.
DR   GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; ISS:BHF-UCL.
DR   CDD; cd06391; PBP1_iGluR_delta_2; 1.
DR   CDD; cd13731; PBP2_iGluR_delta_2; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR001508; Iono_Glu_rcpt_met.
DR   InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR   InterPro; IPR001320; Iontro_rcpt_C.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   PANTHER; PTHR18966:SF109; GLUTAMATE RECEPTOR IONOTROPIC, DELTA-2; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
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; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   Genevisible; O43424; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW   Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW   Membrane; Neurodegeneration; Phosphoprotein; Postsynaptic cell membrane;
KW   Receptor; Reference proteome; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..1007
FT                   /note="Glutamate receptor ionotropic, delta-2"
FT                   /id="PRO_0000011564"
FT   TOPO_DOM        24..566
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        567..587
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        588..635
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        636..656
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        657..830
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        831..851
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        852..1007
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          24..345
FT                   /note="Interaction with CBLN1 homotrimer"
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   REGION          921..991
FT                   /note="Interaction with AP4M1"
FT                   /evidence="ECO:0000250|UniProtKB:Q63226"
FT   MOTIF           1005..1007
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000250"
FT   SITE            76
FT                   /note="Essential for dimerization"
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MOD_RES         883
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61625"
FT   MOD_RES         886
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61625"
FT   MOD_RES         890
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61625"
FT   MOD_RES         1006
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63226"
FT   CARBOHYD        293
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        713
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        716
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..355
FT                   /evidence="ECO:0000269|PubMed:27418511,
FT                   ECO:0007744|PDB:5KC8, ECO:0007744|PDB:5KCA"
FT   DISULFID        99..131
FT                   /evidence="ECO:0000269|PubMed:27418511,
FT                   ECO:0007744|PDB:5KC8, ECO:0007744|PDB:5KCA"
FT   DISULFID        298..310
FT                   /evidence="ECO:0000269|PubMed:27418511,
FT                   ECO:0007744|PDB:5KC8, ECO:0007744|PDB:5KCA"
FT   VAR_SEQ         82..176
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054704"
FT   VARIANT         68
FT                   /note="T -> M (in dbSNP:rs34144324)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_055016"
FT   VARIANT         209
FT                   /note="T -> N (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035697"
FT   VARIANT         398
FT                   /note="F -> S (in dbSNP:rs34796082)"
FT                   /id="VAR_055017"
FT   VARIANT         490
FT                   /note="V -> I (in dbSNP:rs10034345)"
FT                   /id="VAR_055018"
FT   VARIANT         654
FT                   /note="A -> D (in SCAR18)"
FT                   /evidence="ECO:0000269|PubMed:25841024"
FT                   /id="VAR_074166"
FT   VARIANT         654
FT                   /note="A -> T (in SCAR18; constitutively open the
FT                   extracellular-glutamate-gated ion channel)"
FT                   /evidence="ECO:0000269|PubMed:25841024,
FT                   ECO:0000269|PubMed:27418511"
FT                   /id="VAR_074167"
FT   VARIANT         656
FT                   /note="L -> V (in SCAR18)"
FT                   /evidence="ECO:0000269|PubMed:25841024"
FT                   /id="VAR_074168"
FT   MUTAGEN         24
FT                   /note="D->A: Reduces binding to CBLN1; when associated with
FT                   D76. Abolishes CBLN1 binding; when associated with A-26;
FT                   A-61; D-76 and A-345. Abolishes synapse assembly; when
FT                   associated with A-26; A-61 and A-345. Abolishes cerebellar
FT                   parallel fiber-Purkinje cell synapse formation; when
FT                   associated with A-26; A-61 and A-345. Abolishes
FT                   D-Serine-dependent long term synaptic depression at PF-PC
FT                   synapses; when associated with A-26; A-61 and A-345."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         25
FT                   /note="S->A: Reduces binding to CBLN1; when associated with
FT                   D76."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         26
FT                   /note="I->A: Reduces binding to CBLN1; when associated with
FT                   D76. Abolishes CBLN1 binding; when associated with A-24;
FT                   A-61; D-76 and A-345. Abolishes synapse assembly; when
FT                   associated with A-24; A-61 and A-345. Abolishes cerebellar
FT                   parallel fiber-Purkinje cell synapse formation; when
FT                   associated with A-24; A-61 and A-345. Abolishes
FT                   D-Serine-dependent long term synaptic depression at PF-PC
FT                   synapses; when associated with A-24; A-61 and A-345."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         60
FT                   /note="T->A: No effect on CBLN1 interaction; when
FT                   associated with D76."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         61
FT                   /note="E->A: Reduces binding to CBLN1; when associated with
FT                   D76. Abolishes CBLN1 binding; when associated with A-24;
FT                   A-26; D-76 and A-345. Abolishes synapse assembly; when
FT                   associated with A-24; A-26 and A-345. Abolishes cerebellar
FT                   parallel fiber-Purkinje cell synapse formation; when
FT                   associated with A-24; A-26 and A-345. Abolishes
FT                   D-Serine-dependent long term synaptic depression at PF-PC
FT                   synapses; when associated with A-24; A-26 and A-345."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         76
FT                   /note="F->D: Monomeric form. Does not dimerize. Weakly
FT                   interacts with C1q domain of CBLN1. Forms intermediate
FT                   synapse. Abolishes cerebellar parallel fiber-Purkinje cell
FT                   synapse formation. Abolishes D-Serine?dependent long term
FT                   synaptic depression at PF-PC synapses. Does not recover
FT                   motor coordination in experiment of transfection in
FT                   Grid2-null mice."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         342
FT                   /note="L->A: Reduces binding to CBLN1; when associated with
FT                   D76."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         343
FT                   /note="E->A: No effect on CBLN1 interaction; when
FT                   associated with D76. No effect on CBLN1 binding; when
FT                   associated with D-76; A-346; A-349 and A-350. No effect on
FT                   synapse assembly; when associated with A-346; A-349 and
FT                   A-350. No effect on cerebellar parallel fiber-Purkinje cell
FT                   synapse formation; when associated with A-346; A-349 and
FT                   A-350. Does not affect D-Serine?dependent long term
FT                   synaptic depression at PF-PC synapses; when associated with
FT                   A-346; A-349 and A-350. Does not affect motor coordination;
FT                   when associated with A-346; A-349 and A-350."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         344
FT                   /note="D->A: No effect on CBLN1 interaction; when
FT                   associated with D76."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         345
FT                   /note="R->A: Reduces binding to CBLN1; when associated with
FT                   D76. Abolishes CBLN1 binding; when associated with A-24;
FT                   A-26; A-61 and D-76. Abolishes synapse assembly; when
FT                   associated with A-24; A-26 and A-61. Abolishes cerebellar
FT                   parallel fiber-Purkinje cell synapse formation; when
FT                   associated with A-24; A-26 and A-61. Abolishes
FT                   D-Serine-dependent long term synaptic depression at PF-PC
FT                   synapses; when associated with A-24; A-26 and A-61."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         346
FT                   /note="K->A: No effect on CBLN1 interaction; when
FT                   associated with D76. No effect on CBLN1 binding; when
FT                   associated with D-76; A-343; A-349 and A-350. No effect on
FT                   synapse assembly; when associated with A-343; A-349 and
FT                   A-350. No effect on cerebellar parallel fiber-Purkinje cell
FT                   synapse formation; when associated with A-343; A-349 and
FT                   A-350. Does not affect D-Serine?dependent long term
FT                   synaptic depression at PF-PC synapses; when associated with
FT                   A-343; A-349 and A-350. Does not affect motor coordination;
FT                   when associated with A-343; A-349 and A-350."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         348
FT                   /note="H->A: Reduces binding to CBLN1; when associated with
FT                   D76."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         349
FT                   /note="S->A: No effect on CBLN1 interaction; when
FT                   associated with D76. No effect on CBLN1 binding; when
FT                   associated with D-76; A-343; A-346 and A-350. No effect on
FT                   synapse assembly; when associated with A-343; A-346 and
FT                   A-350. No effect on cerebellar parallel fiber-Purkinje cell
FT                   synapse formation; when associated with A-343; A-346 and
FT                   A-350. Does not affect D-Serine?dependent long term
FT                   synaptic depression at PF-PC synapses; when associated with
FT                   A-343; A-346 and A-350. Does not affect motor coordination;
FT                   when associated with A-343; A-346 and A-350."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         350
FT                   /note="M->A: No effect on CBLN1 interaction; when
FT                   associated with D76. No effect on CBLN1 binding; when
FT                   associated with D-76; A-343; A-346 and A-349. No effect on
FT                   synapse assembly; when associated with A-343; A-346 and
FT                   A-349. No effect on cerebellar parallel fiber-Purkinje cell
FT                   synapse formation; when associated with A-343; A-346 and
FT                   A-349. Does not affect D-Serine?dependent long term
FT                   synaptic depression at PF-PC synapses; when associated with
FT                   A-343; A-346 and A-349. Does not affect motor coordination;
FT                   when associated with A-343; A-346 and A-349."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         352
FT                   /note="S->A: Reduces binding to CBLN1; when associated with
FT                   D76."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         364
FT                   /note="Q->A: No effect on CBLN1 interaction; when
FT                   associated with D76."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   MUTAGEN         434
FT                   /note="L->ELSNGTDGAS: Impairs the ability of the LBD to
FT                   induce pore closure. No effect on synapse assembly. No
FT                   effect on cerebellar parallel fiber-Purkinje cell synapse
FT                   formation. Abolishes D-Serine?dependent long term synaptic
FT                   depression at PF-PC synapses. Does not affect motor
FT                   coordination."
FT                   /evidence="ECO:0000269|PubMed:27418511"
FT   CONFLICT        6
FT                   /note="F -> L (in Ref. 1; AAC39579 and 4;
FT                   AAH99652/AAH99653/AAH99654)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        8
FT                   /note="L -> F (in Ref. 4; AAH99652)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        290
FT                   /note="V -> I (in Ref. 1; AAC39579)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        462
FT                   /note="G -> C (in Ref. 1; AAC39579)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        557
FT                   /note="D -> E (in Ref. 4; AAH99652)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        752
FT                   /note="N -> Y (in Ref. 1; AAC39579)"
FT                   /evidence="ECO:0000305"
FT   STRAND          27..34
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           38..53
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           75..88
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          93..97
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           99..112
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          116..120
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:5KCA"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           152..162
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          167..172
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           178..181
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           182..190
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          194..199
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           204..214
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           217..226
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          229..234
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           236..248
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          257..261
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           267..276
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          279..287
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           294..297
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          298..300
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           307..310
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           315..318
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           322..343
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          355..357
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   HELIX           366..374
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          377..380
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          383..386
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          397..402
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          414..420
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   TURN            421..423
FT                   /evidence="ECO:0007829|PDB:5KC8"
FT   STRAND          424..427
FT                   /evidence="ECO:0007829|PDB:5KC8"
SQ   SEQUENCE   1007 AA;  113356 MW;  8EF938AB7F1D6D26 CRC64;
     MEVFPFLLVL SVWWSRTWDS ANADSIIHIG AIFDESAKKD DEVFRTAVGD LNQNEEILQT
     EKITFSVTFV DGNNPFQAVQ EACELMNQGI LALVSSIGCT SAGSLQSLAD AMHIPHLFIQ
     RSTAGTPRSG CGLTRSNRND DYTLSVRPPV YLHDVILRVV TEYAWQKFII FYDSEYDIRG
     IQEFLDKVSQ QGMDVALQKV ENNINKMITT LFDTMRIEEL NRYRDTLRRA ILVMNPATAK
     SFITEVVETN LVAFDCHWII INEEINDVDV QELVRRSIGR LTIIRQTFPV PQNISQRCFR
     GNHRISSTLC DPKDPFAQNM EISNLYIYDT VLLLANAFHK KLEDRKWHSM ASLSCIRKNS
     KPWQGGRSML ETIKKGGVSG LTGELEFGEN GGNPNVHFEI LGTNYGEELG RGVRKLGCWN
     PVTGLNGSLT DKKLENNMRG VVLRVVTVLE EPFVMVSENV LGKPKKYQGF SIDVLDALSN
     YLGFNYEIYV APDHKYGSPQ EDGTWNGLVG ELVFKRADIG ISALTITPDR ENVVDFTTRY
     MDYSVGVLLR RAEKTVDMFA CLAPFDLSLW ACIAGTVLLV GLLVYLLNWL NPPRLQMGSM
     TSTTLYNSMW FVYGSFVQQG GEVPYTTLAT RMMMGAWWLF ALIVISSYTA NLAAFLTITR
     IESSIQSLQD LSKQTEIPYG TVLDSAVYEH VRMKGLNPFE RDSMYSQMWR MINRSNGSEN
     NVLESQAGIQ KVKYGNYAFV WDAAVLEYVA INDPDCSFYT IGNTVADRGY GIALQHGSPY
     RDVFSQRILE LQQNGDMDIL KHKWWPKNGQ CDLYSSVDTK QKGGALDIKS FAGVFCILAA
     GIVLSCFIAM LETWWNKRKG SRVPSKEDDK EIDLEHLHRR VNSLCTDDDS PHKQFSTSSI
     DLTPLDIDTL PTRQALEQIS DFRNTHITTT TFIPEQIQTL SRTLSAKAAS GFTFGNVPEH
     RTGPFRHRAP NGGFFRSPIK TMSSIPYQPT PTLGLNLGND PDRGTSI
//