DLG2_RAT
ID DLG2_RAT Reviewed; 852 AA.
AC Q63622; P70548; Q62939;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Disks large homolog 2;
DE AltName: Full=Channel-associated protein of synapse-110;
DE Short=Chapsyn-110 {ECO:0000303|PubMed:11997254};
DE AltName: Full=Postsynaptic density protein PSD-93;
GN Name=Dlg2; Synonyms=Dlgh2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8755482; DOI=10.1016/s0896-6273(00)80284-6;
RA Kim E., Cho K.-O., Rothschild A., Sheng M.;
RT "Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-
RT 110, a member of the PSD-95 family of proteins.";
RL Neuron 17:103-113(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RX PubMed=8625413; DOI=10.1016/s0092-8674(00)81053-3;
RA Brenman J.E., Chao D.S., Gee S.H., McGee A.W., Craven S.E.,
RA Santillano D.R., Wu Z., Huang F., Xia H., Peters M.F., Froehner S.C.,
RA Bredt D.S.;
RT "Interaction of nitric oxide synthase with the postsynaptic density protein
RT PSD-95 and alpha1-syntrophin mediated by PDZ domains.";
RL Cell 84:757-767(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Irie M., Hata Y., Takai Y.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
RX PubMed=15304517; DOI=10.1074/jbc.m407575200;
RA Leyland M.L., Dart C.;
RT "An alternatively spliced isoform of PSD-93/chapsyn 110 binds to the
RT inwardly rectifying potassium channel, Kir2.1.";
RL J. Biol. Chem. 279:43427-43436(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 5), SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH NOS1.
RX PubMed=8922396; DOI=10.1523/jneurosci.16-23-07407.1996;
RA Brenman J.E., Christopherson K.S., Craven S.E., McGee A.W., Bredt D.S.;
RT "Cloning and characterization of postsynaptic density 93, a nitric oxide
RT synthase interacting protein.";
RL J. Neurosci. 16:7407-7415(1996).
RN [6]
RP MUTAGENESIS OF CYS-5 AND CYS-7, AND PALMITOYLATION AT CYS-5 AND CYS-7.
RX PubMed=10779526; DOI=10.1074/jbc.m909919199;
RA El-Husseini A.E., Topinka J.R., Lehrer-Graiwer J.E., Firestein B.L.,
RA Craven S.E., Aoki C., Bredt D.S.;
RT "Ion channel clustering by membrane-associated guanylate kinases.
RT Differential regulation by N-terminal lipid and metal binding motifs.";
RL J. Biol. Chem. 275:23904-23910(2000).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=11095503; DOI=10.1097/00001756-200011090-00016;
RA Firestein B.L., Craven S.E., Bredt D.S.;
RT "Postsynaptic targeting of MAGUKs mediated by distinct N-terminal
RT domains.";
RL NeuroReport 11:3479-3484(2000).
RN [8]
RP INTERACTION WITH KCNJ4, AND SUBCELLULAR LOCATION.
RX PubMed=11997254; DOI=10.1152/ajpcell.00615.2001;
RA Inanobe A., Fujita A., Ito M., Tomoike H., Inageda K., Kurachi Y.;
RT "Inward rectifier K+ channel Kir2.3 is localized at the postsynaptic
RT membrane of excitatory synapses.";
RL Am. J. Physiol. 282:C1396-C1403(2002).
RN [9]
RP INTERACTION WITH LRFN1.
RX PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
RA Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K.,
RA Kim E.;
RT "SALM synaptic cell adhesion-like molecules regulate the differentiation of
RT excitatory synapses.";
RL Neuron 50:233-245(2006).
RN [10]
RP INTERACTION WITH FRMPD4.
RX PubMed=19118189; DOI=10.1523/jneurosci.3112-08.2008;
RA Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y., Kang G.B.,
RA Eom S.H., Kim H., Kim E.;
RT "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
RT regulates dendritic spine morphogenesis.";
RL J. Neurosci. 28:14546-14556(2008).
RN [11]
RP INTERACTION WITH ADAM22, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=20089912; DOI=10.1523/jneurosci.4661-09.2010;
RA Ogawa Y., Oses-Prieto J., Kim M.Y., Horresh I., Peles E., Burlingame A.L.,
RA Trimmer J.S., Meijer D., Rasband M.N.;
RT "ADAM22, a Kv1 channel-interacting protein, recruits membrane-associated
RT guanylate kinases to juxtaparanodes of myelinated axons.";
RL J. Neurosci. 30:1038-1048(2010).
RN [12]
RP INTERACTION WITH DGKI.
RX PubMed=21119615; DOI=10.1038/emboj.2010.286;
RA Yang J., Seo J., Nair R., Han S., Jang S., Kim K., Han K., Paik S.K.,
RA Choi J., Lee S., Bae Y.C., Topham M.K., Prescott S.M., Rhee J.S.,
RA Choi S.Y., Kim E.;
RT "DGKiota regulates presynaptic release during mGluR-dependent LTD.";
RL EMBO J. 30:165-180(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-365; SER-406;
RP SER-414; SER-528 AND SER-530, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Required for perception of chronic pain through NMDA receptor
CC signaling. Regulates surface expression of NMDA receptors in dorsal
CC horn neurons of the spinal cord. Interacts with the cytoplasmic tail of
CC NMDA receptor subunits as well as inward rectifying potassium channels.
CC Involved in regulation of synaptic stability at cholinergic synapses.
CC Part of the postsynaptic protein scaffold of excitatory synapses (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts through its PDZ domains with NETO1. Interacts with
CC NOS1/nNOS through second PDZ domain (PubMed:8922396). Interacts with
CC KCNJ2/Kir2.1 (via C-terminus) through one of its PDZ domains (By
CC similarity). Interacts with KCNJ4 (By similarity). Interacts with
CC FRMPD4 (via C-terminus) (PubMed:19118189). Interacts with LRFN1
CC (PubMed:16630835). Interacts with LRFN2 and LRFN4. Interacts with FASLG
CC (By similarity). Interacts with ADAM22 (PubMed:20089912). Interacts
CC with DGKI (via PDZ-binding motif) (PubMed:21119615).
CC {ECO:0000250|UniProtKB:Q15700, ECO:0000250|UniProtKB:Q91XM9,
CC ECO:0000269|PubMed:11997254, ECO:0000269|PubMed:16630835,
CC ECO:0000269|PubMed:19118189, ECO:0000269|PubMed:20089912,
CC ECO:0000269|PubMed:21119615, ECO:0000269|PubMed:8922396}.
CC -!- INTERACTION:
CC Q63622; F1MAB7: Dgki; NbExp=3; IntAct=EBI-396947, EBI-8523614;
CC Q63622; O08560: Dgkz; NbExp=4; IntAct=EBI-396947, EBI-8570505;
CC Q63622; P34926: Map1a; NbExp=4; IntAct=EBI-396947, EBI-631571;
CC Q63622; Q01814-1: ATP2B2; Xeno; NbExp=2; IntAct=EBI-396947, EBI-1174262;
CC Q63622; P23634-6: ATP2B4; Xeno; NbExp=2; IntAct=EBI-396947, EBI-1174437;
CC Q63622; P34998: CRHR1; Xeno; NbExp=2; IntAct=EBI-396947, EBI-3870393;
CC Q63622; O60333-3: KIF1B; Xeno; NbExp=3; IntAct=EBI-396947, EBI-465669;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10779526};
CC Lipid-anchor {ECO:0000269|PubMed:10779526}. Postsynaptic density
CC {ECO:0000269|PubMed:11095503}. Synapse. Cell projection, axon
CC {ECO:0000269|PubMed:20089912}. Membrane {ECO:0000269|PubMed:11997254,
CC ECO:0000269|PubMed:20089912}. Perikaryon {ECO:0000269|PubMed:11095503}.
CC Note=Concentrated in soma and postsynaptic density of a subset of
CC neurons (PubMed:11095503). {ECO:0000269|PubMed:11095503}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=PSD-93b;
CC IsoId=Q63622-1; Sequence=Displayed;
CC Name=2; Synonyms=PSD-93a;
CC IsoId=Q63622-2; Sequence=VSP_015528;
CC Name=3; Synonyms=PSD-93c;
CC IsoId=Q63622-3; Sequence=VSP_015527, VSP_015529, VSP_015530;
CC Name=4; Synonyms=PSD-93-delta;
CC IsoId=Q63622-4; Sequence=VSP_015526;
CC Name=5; Synonyms=PSD-93d;
CC IsoId=Q63622-5; Sequence=VSP_015525;
CC Name=6;
CC IsoId=Q63622-6; Sequence=VSP_015531, VSP_015533;
CC Name=7;
CC IsoId=Q63622-7; Sequence=VSP_015532;
CC -!- TISSUE SPECIFICITY: Detected in juxtaparanodal zones in the central
CC nervous system and at nerve terminal plexuses of basket cells in the
CC cerebellum (at protein level) (PubMed:20089912). Brain. High levels in
CC cerebellar Purkinje cells. Expressed in pyramidal cells of the Ammons's
CC horn and granular cells of the dentate gyrus in the hippocampus as well
CC as cerebral cortex and striatum. High levels in dorsal horn of spinal
CC cord. {ECO:0000269|PubMed:15304517, ECO:0000269|PubMed:20089912,
CC ECO:0000269|PubMed:8922396}.
CC -!- DEVELOPMENTAL STAGE: High levels in developing brain and spinal chord,
CC sensory neurons of dorsal root and trigeminal ganglia, myenteric
CC neurons of the intestine as well as in non-neuronal cells of adrenal,
CC thymus and submandibular glands of E15 embryos.
CC {ECO:0000269|PubMed:8922396}.
CC -!- PTM: Palmitoylation of isoform 1 and isoform 2 is not required for
CC targeting to postsynaptic density. {ECO:0000269|PubMed:10779526}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; U49049; AAB53243.1; -; mRNA.
DR EMBL; U50717; AAC52643.1; -; mRNA.
DR EMBL; U53368; AAB48562.1; -; mRNA.
DR PIR; T10811; T10811.
DR RefSeq; NP_071618.1; NM_022282.1. [Q63622-1]
DR PDB; 4H11; X-ray; 1.67 A; A/B=93-188.
DR PDBsum; 4H11; -.
DR AlphaFoldDB; Q63622; -.
DR SMR; Q63622; -.
DR BioGRID; 248965; 11.
DR CORUM; Q63622; -.
DR IntAct; Q63622; 18.
DR MINT; Q63622; -.
DR STRING; 10116.ENSRNOP00000052268; -.
DR iPTMnet; Q63622; -.
DR PhosphoSitePlus; Q63622; -.
DR SwissPalm; Q63622; -.
DR PaxDb; Q63622; -.
DR PRIDE; Q63622; -.
DR ABCD; Q63622; 3 sequenced antibodies.
DR Ensembl; ENSRNOT00000108774; ENSRNOP00000092409; ENSRNOG00000022635. [Q63622-7]
DR Ensembl; ENSRNOT00000110277; ENSRNOP00000097641; ENSRNOG00000022635. [Q63622-1]
DR GeneID; 64053; -.
DR KEGG; rno:64053; -.
DR UCSC; RGD:619895; rat. [Q63622-1]
DR CTD; 1740; -.
DR RGD; 619895; Dlg2.
DR eggNOG; KOG0708; Eukaryota.
DR GeneTree; ENSGT00940000155156; -.
DR InParanoid; Q63622; -.
DR OrthoDB; 807583at2759; -.
DR PRO; PR:Q63622; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0099031; C:anchored component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0043194; C:axon initial segment; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0044224; C:juxtaparanode region of axon; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; ISO:RGD.
DR GO; GO:0099641; P:anterograde axonal protein transport; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0035865; P:cellular response to potassium ion; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0045163; P:clustering of voltage-gated potassium channels; ISO:RGD.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0045161; P:neuronal ion channel clustering; IMP:RGD.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:RGD.
DR GO; GO:0043113; P:receptor clustering; IMP:RGD.
DR GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
DR GO; GO:0099642; P:retrograde axonal protein transport; ISO:RGD.
DR GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
DR CDD; cd12032; SH3_DLG2; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR016313; DLG1-like.
DR InterPro; IPR019590; DLG1_PEST_dom.
DR InterPro; IPR035759; DLG2_SH3.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR019583; PDZ_assoc.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF10608; MAGUK_N_PEST; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF10600; PDZ_assoc; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM01277; MAGUK_N_PEST; 1.
DR SMART; SM00228; PDZ; 3.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; Synapse.
FT CHAIN 1..852
FT /note="Disks large homolog 2"
FT /id="PRO_0000094555"
FT DOMAIN 98..184
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 193..279
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 421..501
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 536..606
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 662..837
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 58
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 505
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 732
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT MOD_RES 737
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT LIPID 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:10779526"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:10779526"
FT VAR_SEQ 1..246
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:8922396"
FT /id="VSP_015525"
FT VAR_SEQ 1..68
FT /note="MFFACYCALRTNVKKYRYQDEDGPHDHSLPRLTHEVRGPELVHVSEKNLSQI
FT ENVHGYVLQSHISPLK -> MNAYLTKQHSCSRGSDGMDAGRGVPTLIRDAHCACGWQR
FT NAQGLGYSSQTMPSSGPGGPASNRTKLVTLWDSVRKSPHKTSTKGKGNCGERCACPHGW
FT FSPAQ (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_015526"
FT VAR_SEQ 1..61
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8922396"
FT /id="VSP_015527"
FT VAR_SEQ 1..13
FT /note="MFFACYCALRTNV -> MICHCKVACTNNTLSLMFGC (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:8922396"
FT /id="VSP_015528"
FT VAR_SEQ 62..68
FT /note="SHISPLK -> MQHAFIP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8922396"
FT /id="VSP_015529"
FT VAR_SEQ 341..392
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8922396"
FT /id="VSP_015530"
FT VAR_SEQ 450..454
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:8625413"
FT /id="VSP_015531"
FT VAR_SEQ 626..641
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:8625413"
FT /id="VSP_015533"
FT VAR_SEQ 626..641
FT /note="GDIPGLGDDGYGTKTL -> GSFNDKRKKSFIFSRKFPFYKNKEQSEQETSD
FT PE (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_015532"
FT MUTAGEN 5
FT /note="C->S: Loss of palmitoylation and targeting to
FT postsynaptic density."
FT /evidence="ECO:0000269|PubMed:10779526"
FT MUTAGEN 7
FT /note="C->S: Loss of palmitoylation and targeting to
FT postsynaptic density."
FT /evidence="ECO:0000269|PubMed:10779526"
FT CONFLICT 181..182
FT /note="VR -> IL (in Ref. 2; AAC52643)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="I -> M (in Ref. 2; AAC52643)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="R -> K (in Ref. 2; AAC52643)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="D -> E (in Ref. 3; AAB48562)"
FT /evidence="ECO:0000305"
FT CONFLICT 464..465
FT /note="GD -> RK (in Ref. 2; AAC52643)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="D -> H (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="R -> P (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="A -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 484..486
FT /note="AAA -> LP (in Ref. 2; AAC52643)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="A -> S (in Ref. 2; AAC52643)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="H -> N (in Ref. 2; AAC52643)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="L -> Q (in Ref. 2; AAC52643)"
FT /evidence="ECO:0000305"
FT CONFLICT 627..630
FT /note="DIPG -> TSR (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="K -> A (in Ref. 3; AAB48562)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="F -> L (in Ref. 1; AAB53243)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="N -> Y (in Ref. 2; AAC52643)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="E -> V (in Ref. 1; AAB53243)"
FT /evidence="ECO:0000305"
FT CONFLICT 756
FT /note="L -> H (in Ref. 2; AAC52643)"
FT /evidence="ECO:0000305"
FT CONFLICT 791..792
FT /note="KR -> NG (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="T -> M (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:4H11"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:4H11"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4H11"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:4H11"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:4H11"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:4H11"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:4H11"
FT STRAND 175..184
FT /evidence="ECO:0007829|PDB:4H11"
SQ SEQUENCE 852 AA; 94934 MW; F8D414A8B9CF5B09 CRC64;
MFFACYCALR TNVKKYRYQD EDGPHDHSLP RLTHEVRGPE LVHVSEKNLS QIENVHGYVL
QSHISPLKAS PAPIIVNTDT LDTIPYVNGT EIEYEFEEIT LERGNSGLGF SIAGGTDNPH
IGDDPGIFIT KIIPGGAAAE DGRLRVNDCI LRVNEVDVSE VSHSKAVEAL KEAGSIVRLY
VRRRRPILET VVEIKLFKGP KGLGFSIAGG VGNQHIPGDN SIYVTKIIDG GAAQKDGRLQ
VGDRLLMVNN YSLEEVTHEE AVAILKNTSD VVYLKVGKPT TIYMTDPYGP PDITHSYSPP
MENHLLSGNN GTLEYKTSLP PISPGRYSPI PKHMLVEDDY TRPPEPVYST VNKLCDKPAS
PRHYSPVECD KSFLLSTPYP HYHLGLLPDS DMTSHSQHST ATRQPSVTLQ RAISLEGEPR
KVVLHKGSTG LGFNIVGGED GEGIFVSFIL AGGPADLSGE LQRGDQILSV NGIDLRGASH
EQAAAALKGA GQTVTIIAQY QPEDYARFEA KIHDLREQMM NHSMSSGSGS LRTNQKRSLY
VRAMFDYDKS KDSGLPSQGL SFKYGDILHV INASDDEWWQ ARRVILDGDS EEMGVIPSKR
RVERKERARL KTVKFNAKPG VIDSKGDIPG LGDDGYGTKT LRGQEDLILS YEPVTRQEIN
YTRPVIILGP MKDRINDDLI SEFPDKFGSC VPHTTRPKRD YEVDGRDYHF VISREQMEKD
IQEHKFIEAG QYNDNLYGTS VQSVRFVAER GKHCILDVSG NAIKRLQVAQ LYPIAIFIKP
KSLEPLMEMN KRLTEEQAKK TYDRAIKLEQ EFGEYFTAIV QGDTLEDIYN QCKLVIEEQS
GPFIWIPSKE KL
