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 13-FEB-2019, entry version 171. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RP 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., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA 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., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA 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., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 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 RT project: 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, RP REGION, 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., RA Matsuda K., Kohda K., Miura E., Rossmann M., Mitakidis N., RA Motohashi J., Chang V.T., Siebold C., Greger I.H., Nakagawa T., RA 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., RA Alanay Y., Aktas D., Boduroglu K., Alikasifoglu M.; RT "A homozygous deletion in GRID2 causes a human phenotype with RT cerebellar 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., RA Stoler J.M., Barkovich A.J., Watanabe M., Yuzaki M., Mochida G.H.; RT "Deletions in GRID2 lead to a recessive syndrome of cerebellar ataxia RT and 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., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT 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., RA Rodriguez D., Chantot-Bastaraud S., Rougeot C., Cournelle M.A., RA Milh M., Toutain A., Bacq D., Meyer V., Afenjar A., Deleuze J.F., RA Brice A., Heron D., 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 CC excitatory neurotransmitter at many synapses in the central CC nervous system. The postsynaptic actions of Glu are mediated by a CC variety of receptors that are named according to their selective CC agonists. Promotes synaptogenesis and mediates the D-Serine- CC dependent long term depression signals and AMPA receptor CC endocytosis of cerebellar parallel fiber-Purkinje cell (PF-PC) CC synapses through the beta-NRX1-CBLN1-GRID2 triad complex CC (PubMed:27418511). {ECO:0000269|PubMed:27418511}. CC -!- SUBUNIT: Tetramer; dimer of dimers (PubMed:27418511). Interacts CC with EML2, MAGI2 (via PDZ domains) and AP4M1 (By similarity). CC Interacts with BECN1, GOPC, GRID2IP, SHANK1 and SHANK2. Interacts CC with CBLN2, but not with CBLN4 (By similarity). Interacts with CC CBLN1 (via C1q domain); the interaction is CBLN1-NRX1 complex CC formation-dependent; CBLN1-binding is calcium-independent; CBLN1 CC hexamers anchor GRID2 N-terminal domain dimers to monomeric NRXN1 CC isoform beta; promotes synaptogenesis and mediates the D-Serine- CC dependent long term depression signals and AMPA receptor CC 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 CC membrane protein {ECO:0000250}. Cell junction, synapse, CC postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane CC 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]: Spinocerebellar ataxia defines a clinically and CC genetically heterogeneous group of cerebellar disorders. Patients CC show progressive incoordination of gait and often poor CC coordination of hands, speech and eye movements, due to CC degeneration of the cerebellum with variable involvement of the CC brainstem and spinal cord. SCAR18 features include progressive CC cerebellar atrophy, delayed psychomotor development, severely CC impaired gait, ocular movement abnormalities, and intellectual CC 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 CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC CC 1.A.10.1) family. GRID2 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD92555.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; 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 UniGene; Hs.162727; -. DR UniGene; Hs.480281; -. 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 ProteinModelPortal; O43424; -. DR SMR; O43424; -. DR BioGrid; 109152; 7. DR MINT; O43424; -. DR STRING; 9606.ENSP00000282020; -. DR DrugBank; DB00142; L-Glutamic Acid. DR iPTMnet; O43424; -. DR PhosphoSitePlus; O43424; -. DR BioMuta; GRID2; -. DR EPD; O43424; -. DR jPOST; O43424; -. DR MaxQB; O43424; -. DR PaxDb; O43424; -. DR PeptideAtlas; O43424; -. DR PRIDE; O43424; -. DR ProteomicsDB; 48936; -. DR Ensembl; ENST00000282020; ENSP00000282020; ENSG00000152208. [O43424-1] DR Ensembl; ENST00000510992; ENSP00000421257; ENSG00000152208. [O43424-2] DR GeneID; 2895; -. DR KEGG; hsa:2895; -. DR UCSC; uc011cdt.4; human. [O43424-1] DR CTD; 2895; -. DR DisGeNET; 2895; -. DR EuPathDB; HostDB:ENSG00000152208.11; -. DR GeneCards; GRID2; -. DR H-InvDB; HIX0031353; -. DR HGNC; HGNC:4576; GRID2. DR HPA; HPA056253; -. DR HPA; HPA058538; -. 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 eggNOG; ENOG410ISR9; Eukaryota. DR eggNOG; ENOG410YYDD; LUCA. DR GeneTree; ENSGT00940000155192; -. DR HOGENOM; HOG000264260; -. DR HOVERGEN; HBG051840; -. DR InParanoid; O43424; -. DR KO; K05207; -. DR OMA; LQQSGDM; -. DR OrthoDB; 122304at2759; -. DR PhylomeDB; O43424; -. DR TreeFam; TF352434; -. DR ChiTaRS; GRID2; human. DR GeneWiki; GRID2; -. DR GenomeRNAi; 2895; -. DR PRO; PR:O43424; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; ENSG00000152208; Expressed in 65 organ(s), highest expression level in cerebellar vermis. DR ExpressionAtlas; O43424; baseline and differential. DR Genevisible; O43424; HS. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0099061; C:integral component of postsynaptic density membrane; 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:0045211; C:postsynaptic 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:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro. 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 ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central. DR GO; GO:0034613; P:cellular protein localization; ISS:BHF-UCL. 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: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:0035249; P:synaptic transmission, glutamatergic; ISS:BHF-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; Cell junction; Cell membrane; KW Complete proteome; Disulfide bond; Glycoprotein; Ion channel; KW Ion transport; Ligand-gated ion channel; Membrane; Neurodegeneration; KW Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Receptor; KW Reference proteome; Signal; Synapse; Transmembrane; KW Transmembrane helix; Transport. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 1007 Glutamate receptor ionotropic, delta-2. FT /FTId=PRO_0000011564. FT TOPO_DOM 24 566 Extracellular. {ECO:0000255}. FT TRANSMEM 567 587 Helical. {ECO:0000255}. FT TOPO_DOM 588 635 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 636 656 Helical. {ECO:0000255}. FT TOPO_DOM 657 830 Extracellular. {ECO:0000255}. FT TRANSMEM 831 851 Helical. {ECO:0000255}. FT TOPO_DOM 852 1007 Cytoplasmic. {ECO:0000255}. FT REGION 24 345 Interaction with CBLN1 homotrimer. FT {ECO:0000269|PubMed:27418511}. FT REGION 921 991 Interaction with AP4M1. FT {ECO:0000250|UniProtKB:Q63226}. FT MOTIF 1005 1007 PDZ-binding. {ECO:0000250}. FT SITE 76 76 Essential for dimerization. FT {ECO:0000269|PubMed:27418511}. FT MOD_RES 883 883 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61625}. FT MOD_RES 886 886 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q61625}. FT MOD_RES 890 890 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61625}. FT MOD_RES 1006 1006 Phosphoserine. FT {ECO:0000250|UniProtKB:Q63226}. FT CARBOHYD 293 293 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 426 426 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 83 355 {ECO:0000244|PDB:5KC8, FT ECO:0000244|PDB:5KCA, FT ECO:0000269|PubMed:27418511}. FT DISULFID 99 131 {ECO:0000244|PDB:5KC8, FT ECO:0000244|PDB:5KCA, FT ECO:0000269|PubMed:27418511}. FT DISULFID 298 310 {ECO:0000244|PDB:5KC8, FT ECO:0000244|PDB:5KCA, FT ECO:0000269|PubMed:27418511}. FT VAR_SEQ 82 176 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_054704. FT VARIANT 68 68 T -> M (in dbSNP:rs34144324). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_055016. FT VARIANT 209 209 T -> N (in a colorectal cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_035697. FT VARIANT 398 398 F -> S (in dbSNP:rs34796082). FT /FTId=VAR_055017. FT VARIANT 490 490 V -> I (in dbSNP:rs10034345). FT /FTId=VAR_055018. FT VARIANT 654 654 A -> D (in SCAR18). FT {ECO:0000269|PubMed:25841024}. FT /FTId=VAR_074166. FT VARIANT 654 654 A -> T (in SCAR18; constitutively open FT the extracellular-glutamate-gated ion FT channel). {ECO:0000269|PubMed:25841024, FT ECO:0000269|PubMed:27418511}. FT /FTId=VAR_074167. FT VARIANT 656 656 L -> V (in SCAR18). FT {ECO:0000269|PubMed:25841024}. FT /FTId=VAR_074168. FT MUTAGEN 24 24 D->A: Reduces binding to CBLN1; when FT associated with D76. Abolishes CBLN1 FT binding; when associated with A-26; A-61; FT D-76 and A-345. Abolishes synapse FT assembly; when associated with A-26; A-61 FT and A-345. Abolishes cerebellar parallel FT fiber-Purkinje cell synapse formation; FT when associated with A-26; A-61 and A- FT 345. Abolishes D-Serine-dependent long FT term synaptic depression at PF-PC FT synapses; when associated with A-26; A-61 FT and A-345. {ECO:0000269|PubMed:27418511}. FT MUTAGEN 25 25 S->A: Reduces binding to CBLN1; when FT associated with D76. FT {ECO:0000269|PubMed:27418511}. FT MUTAGEN 26 26 I->A: Reduces binding to CBLN1; when FT associated with D76. Abolishes CBLN1 FT binding; when associated with A-24; A-61; FT D-76 and A-345. Abolishes synapse FT assembly; when associated with A-24; A-61 FT and A-345. Abolishes cerebellar parallel FT fiber-Purkinje cell synapse formation; FT when associated with A-24; A-61 and A- FT 345. Abolishes D-Serine-dependent long FT term synaptic depression at PF-PC FT synapses; when associated with A-24; A-61 FT and A-345. {ECO:0000269|PubMed:27418511}. FT MUTAGEN 60 60 T->A: No effect on CBLN1 interaction; FT when associated with D76. FT {ECO:0000269|PubMed:27418511}. FT MUTAGEN 61 61 E->A: Reduces binding to CBLN1; when FT associated with D76. Abolishes CBLN1 FT binding; when associated with A-24; A-26; FT D-76 and A-345. Abolishes synapse FT assembly; when associated with A-24; A-26 FT and A-345. Abolishes cerebellar parallel FT fiber-Purkinje cell synapse formation; FT when associated with A-24; A-26 and A- FT 345. Abolishes D-Serine-dependent long FT term synaptic depression at PF-PC FT synapses; when associated with A-24; A-26 FT and A-345. {ECO:0000269|PubMed:27418511}. FT MUTAGEN 76 76 F->D: Monomeric form. Does not dimerize. FT Weakly interacts with C1q domain of FT CBLN1. Forms intermediate synapse. FT Abolishes cerebellar parallel fiber- FT Purkinje cell synapse formation. FT Abolishes D-Serine?dependent long term FT synaptic depression at PF-PC synapses. FT Does not recover motor coordination in FT experiment of tranfection in Grid2-null FT mice. {ECO:0000269|PubMed:27418511}. FT MUTAGEN 342 342 L->A: Reduces binding to CBLN1; when FT associated with D76. FT {ECO:0000269|PubMed:27418511}. FT MUTAGEN 343 343 E->A: No effect on CBLN1 interaction; FT when associated with D76. No effect on FT CBLN1 binding; when associated with D-76; FT A-346; A-349 and A-350. No effect on FT synapse assembly; when associated with A- FT 346; A-349 and A-350. No effect on FT cerebellar parallel fiber-Purkinje cell FT synapse formation; when associated with FT A-346; A-349 and A-350. Does not affect FT D-Serine?dependent long term synaptic FT depression at PF-PC synapses; when FT associated with A-346; A-349 and A-350. FT Does not affect motor coordination; when FT associated with A-346; A-349 and A-350. FT {ECO:0000269|PubMed:27418511}. FT MUTAGEN 344 344 D->A: No effect on CBLN1 interaction; FT when associated with D76. FT {ECO:0000269|PubMed:27418511}. FT MUTAGEN 345 345 R->A: Reduces binding to CBLN1; when FT associated with D76. Abolishes CBLN1 FT binding; when associated with A-24; A-26; FT A-61 and D-76. Abolishes synapse FT assembly; when associated with A-24; A-26 FT and A-61. Abolishes cerebellar parallel FT fiber-Purkinje cell synapse formation; FT when associated with A-24; A-26 and A-61. FT Abolishes D-Serine-dependent long term FT synaptic depression at PF-PC synapses; FT when associated with A-24; A-26 and A-61. FT {ECO:0000269|PubMed:27418511}. FT MUTAGEN 346 346 K->A: No effect on CBLN1 interaction; FT when associated with D76. No effect on FT CBLN1 binding; when associated with D-76; FT A-343; A-349 and A-350. No effect on FT synapse assembly; when associated with A- FT 343; A-349 and A-350. No effect on FT cerebellar parallel fiber-Purkinje cell FT synapse formation; when associated with FT A-343; A-349 and A-350. Does not affect FT D-Serine?dependent long term synaptic FT depression at PF-PC synapses; when FT associated with A-343; A-349 and A-350. FT Does not affect motor coordination; when FT associated with A-343; A-349 and A-350. FT {ECO:0000269|PubMed:27418511}. FT MUTAGEN 348 348 H->A: Reduces binding to CBLN1; when FT associated with D76. FT {ECO:0000269|PubMed:27418511}. FT MUTAGEN 349 349 S->A: No effect on CBLN1 interaction; FT when associated with D76. No effect on FT CBLN1 binding; when associated with D-76; FT A-343; A-346 and A-350. No effect on FT synapse assembly; when associated with A- FT 343; A-346 and A-350. No effect on FT cerebellar parallel fiber-Purkinje cell FT synapse formation; when associated with FT A-343; A-346 and A-350. Does not affect FT D-Serine?dependent long term synaptic FT depression at PF-PC synapses; when FT associated with A-343; A-346 and A-350. FT Does not affect motor coordination; when FT associated with A-343; A-346 and A-350. FT {ECO:0000269|PubMed:27418511}. FT MUTAGEN 350 350 M->A: No effect on CBLN1 interaction; FT when associated with D76. No effect on FT CBLN1 binding; when associated with D-76; FT A-343; A-346 and A-349. No effect on FT synapse assembly; when associated with A- FT 343; A-346 and A-349. No effect on FT cerebellar parallel fiber-Purkinje cell FT synapse formation; when associated with FT A-343; A-346 and A-349. Does not affect FT D-Serine?dependent long term synaptic FT depression at PF-PC synapses; when FT associated with A-343; A-346 and A-349. FT Does not affect motor coordination; when FT associated with A-343; A-346 and A-349. FT {ECO:0000269|PubMed:27418511}. FT MUTAGEN 352 352 S->A: Reduces binding to CBLN1; when FT associated with D76. FT {ECO:0000269|PubMed:27418511}. FT MUTAGEN 364 364 Q->A: No effect on CBLN1 interaction; FT when associated with D76. FT {ECO:0000269|PubMed:27418511}. FT MUTAGEN 434 434 L->ELSNGTDGAS: Impairs the ability of the FT LBD to induce pore closure. No effect on FT synapse assembly. No effect on cerebellar FT parallel fiber-Purkinje cell synapse FT formation. Abolishes D-Serine?dependent FT long term synaptic depression at PF-PC FT synapses. Does not affect motor FT coordination. FT {ECO:0000269|PubMed:27418511}. FT CONFLICT 6 6 F -> L (in Ref. 1; AAC39579 and 4; FT AAH99652/AAH99653/AAH99654). FT {ECO:0000305}. FT CONFLICT 8 8 L -> F (in Ref. 4; AAH99652). FT {ECO:0000305}. FT CONFLICT 290 290 V -> I (in Ref. 1; AAC39579). FT {ECO:0000305}. FT CONFLICT 462 462 G -> C (in Ref. 1; AAC39579). FT {ECO:0000305}. FT CONFLICT 557 557 D -> E (in Ref. 4; AAH99652). FT {ECO:0000305}. FT CONFLICT 752 752 N -> Y (in Ref. 1; AAC39579). FT {ECO:0000305}. FT STRAND 27 34 {ECO:0000244|PDB:5KC8}. FT HELIX 38 53 {ECO:0000244|PDB:5KC8}. FT STRAND 63 70 {ECO:0000244|PDB:5KC8}. FT HELIX 75 88 {ECO:0000244|PDB:5KC8}. FT STRAND 93 97 {ECO:0000244|PDB:5KC8}. FT HELIX 99 112 {ECO:0000244|PDB:5KC8}. FT STRAND 116 120 {ECO:0000244|PDB:5KC8}. FT STRAND 137 139 {ECO:0000244|PDB:5KCA}. FT STRAND 143 145 {ECO:0000244|PDB:5KC8}. FT HELIX 152 162 {ECO:0000244|PDB:5KC8}. FT STRAND 167 172 {ECO:0000244|PDB:5KC8}. FT HELIX 178 181 {ECO:0000244|PDB:5KC8}. FT HELIX 182 190 {ECO:0000244|PDB:5KC8}. FT STRAND 194 199 {ECO:0000244|PDB:5KC8}. FT HELIX 204 214 {ECO:0000244|PDB:5KC8}. FT HELIX 217 226 {ECO:0000244|PDB:5KC8}. FT STRAND 229 234 {ECO:0000244|PDB:5KC8}. FT HELIX 236 248 {ECO:0000244|PDB:5KC8}. FT STRAND 257 261 {ECO:0000244|PDB:5KC8}. FT HELIX 267 276 {ECO:0000244|PDB:5KC8}. FT STRAND 279 287 {ECO:0000244|PDB:5KC8}. FT HELIX 294 297 {ECO:0000244|PDB:5KC8}. FT STRAND 298 300 {ECO:0000244|PDB:5KC8}. FT HELIX 307 310 {ECO:0000244|PDB:5KC8}. FT HELIX 315 318 {ECO:0000244|PDB:5KC8}. FT HELIX 322 343 {ECO:0000244|PDB:5KC8}. FT STRAND 355 357 {ECO:0000244|PDB:5KC8}. FT HELIX 366 374 {ECO:0000244|PDB:5KC8}. FT STRAND 377 380 {ECO:0000244|PDB:5KC8}. FT STRAND 383 386 {ECO:0000244|PDB:5KC8}. FT STRAND 397 402 {ECO:0000244|PDB:5KC8}. FT STRAND 414 420 {ECO:0000244|PDB:5KC8}. FT TURN 421 423 {ECO:0000244|PDB:5KC8}. FT STRAND 424 427 {ECO:0000244|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 //