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Database: UniProt
Entry: Q62696
LinkDB: Q62696
Original site: Q62696 
ID   DLG1_RAT                Reviewed;         911 AA.
AC   Q62696;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   29-OCT-2014, entry version 143.
DE   RecName: Full=Disks large homolog 1;
DE   AltName: Full=Synapse-associated protein 97;
DE            Short=SAP-97;
DE            Short=SAP97;
GN   Name=Dlg1; Synonyms=Dlgh1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Brain;
RX   PubMed=7891172;
RA   Mueller B.M., Kistner U., Veh R.W., Cases-Langhoff C., Becker B.,
RA   Gundelfinger E.D., Garner C.C.;
RT   "Molecular characterization and spatial distribution of SAP97, a novel
RT   presynaptic protein homologous to SAP90 and the Drosophila discs-large
RT   tumor suppressor protein.";
RL   J. Neurosci. 15:2354-2366(1995).
RN   [2]
RP   INTERACTION WITH DLGAP1; DLGAP2; DLGAP3 AND DLGAP4.
RX   PubMed=9115257; DOI=10.1074/jbc.272.18.11943;
RA   Takeuchi M., Hata Y., Hirao K., Toyoda A., Irie M., Takai Y.;
RT   "SAPAPs. A family of PSD-95/SAP90-associated proteins localized at
RT   postsynaptic density.";
RL   J. Biol. Chem. 272:11943-11951(1997).
RN   [3]
RP   INTERACTION WITH GRIA1.
RX   PubMed=9677374; DOI=10.1074/jbc.273.31.19518;
RA   Leonard A.S., Davare M.A., Horne M.C., Garner C.C., Hell J.W.;
RT   "SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-
RT   4-propionic acid receptor GluR1 subunit.";
RL   J. Biol. Chem. 273:19518-19524(1998).
RN   [4]
RP   INTERACTION WITH MAP1A.
RX   PubMed=9786987;
RA   Brenman J.E., Topinka J.R., Cooper E.C., McGee A.W., Rosen J.,
RA   Milroy T., Ralston H.J., Bredt D.S.;
RT   "Localization of postsynaptic density-93 to dendritic microtubules and
RT   interaction with microtubule-associated protein 1A.";
RL   J. Neurosci. 18:8805-8813(1998).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10629225; DOI=10.1083/jcb.148.1.147;
RA   Tiffany A.M., Manganas L.N., Kim E., Hsueh Y.P., Sheng M.,
RA   Trimmer J.S.;
RT   "PSD-95 and SAP97 exhibit distinct mechanisms for regulating K(+)
RT   channel surface expression and clustering.";
RL   J. Cell Biol. 148:147-158(2000).
RN   [6]
RP   INTERACTION WITH CASK, AND SUBCELLULAR LOCATION.
RX   PubMed=11865057; DOI=10.1128/MCB.22.6.1778-1791.2002;
RA   Lee S., Fan S., Makarova O., Straight S., Margolis B.;
RT   "A novel and conserved protein-protein interaction domain of mammalian
RT   Lin-2/CASK binds and recruits SAP97 to the lateral surface of
RT   epithelia.";
RL   Mol. Cell. Biol. 22:1778-1791(2002).
RN   [7]
RP   INDUCTION BY BDNF.
RX   PubMed=14597197; DOI=10.1016/j.ydbio.2003.07.008;
RA   Jourdi H., Iwakura Y., Narisawa-Saito M., Ibaraki K., Xiong H.,
RA   Watanabe M., Hayashi Y., Takei N., Nawa H.;
RT   "Brain-derived neurotrophic factor signal enhances and maintains the
RT   expression of AMPA receptor-associated PDZ proteins in developing
RT   cortical neurons.";
RL   Dev. Biol. 263:216-230(2003).
RN   [8]
RP   MUTAGENESIS OF SER-232, PHOSPHORYLATION AT SER-232, AND INTERACTION
RP   WITH GRIN2A.
RX   PubMed=12933808; DOI=10.1074/jbc.M303576200;
RA   Gardoni F., Mauceri D., Fiorentini C., Bellone C., Missale C.,
RA   Cattabeni F., Di Luca M.;
RT   "CaMKII-dependent phosphorylation regulates SAP97/NR2A interaction.";
RL   J. Biol. Chem. 278:44745-44752(2003).
RN   [9]
RP   INTERACTION WITH CASK; LIN7A; LIN7B; LIN7C; APBA1 AND KCNJ12, AND
RP   FUNCTION.
RX   PubMed=14960569; DOI=10.1074/jbc.M400284200;
RA   Leonoudakis D., Conti L.R., Radeke C.M., McGuire L.M.,
RA   Vandenberg C.A.;
RT   "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and
RT   Mint1 is associated with inward rectifier Kir2 potassium channels.";
RL   J. Biol. Chem. 279:19051-19063(2004).
RN   [10]
RP   MUTAGENESIS OF SER-39, PHOSPHORYLATION AT SER-39, SUBCELLULAR
RP   LOCATION, AND FUNCTION.
RX   PubMed=15044483; DOI=10.1074/jbc.M402796200;
RA   Mauceri D., Cattabeni F., Di Luca M., Gardoni F.;
RT   "Calcium/calmodulin-dependent protein kinase II phosphorylation drives
RT   synapse-associated protein 97 into spines.";
RL   J. Biol. Chem. 279:23813-23821(2004).
RN   [11]
RP   FUNCTION.
RX   PubMed=15504326; DOI=10.1016/j.neuron.2004.10.012;
RA   Nakagawa T., Futai K., Lashuel H.A., Lo I., Okamoto K., Walz T.,
RA   Hayashi Y., Sheng M.;
RT   "Quaternary structure, protein dynamics, and synaptic function of
RT   SAP97 controlled by L27 domain interactions.";
RL   Neuron 44:453-467(2004).
RN   [12]
RP   INTERACTION WITH PTEN.
RX   PubMed=15951562; DOI=10.1074/jbc.M504761200;
RA   Valiente M., Andres-Pons A., Gomar B., Torres J., Gil A., Tapparel C.,
RA   Antonarakis S.E., Pulido R.;
RT   "Binding of PTEN to specific PDZ domains contributes to PTEN protein
RT   stability and phosphorylation by microtubule-associated
RT   serine/threonine kinases.";
RL   J. Biol. Chem. 280:28936-28943(2005).
RN   [13]
RP   INTERACTION WITH LRFN2.
RX   PubMed=16495444; DOI=10.1523/JNEUROSCI.3799-05.2006;
RA   Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K.,
RA   Wenthold R.J.;
RT   "A novel family of adhesion-like molecules that interacts with the
RT   NMDA receptor.";
RL   J. Neurosci. 26:2174-2183(2006).
RN   [14]
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.,
RA   Kaang B.-K., Kim E.;
RT   "SALM synaptic cell adhesion-like molecules regulate the
RT   differentiation of excitatory synapses.";
RL   Neuron 50:233-245(2006).
RN   [15]
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.,
RA   Kang G.B., 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   [16]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH KCND2; KCND3 AND CAMK2.
RX   PubMed=19213956; DOI=10.1161/CIRCRESAHA.108.191007;
RA   El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H.,
RA   Coulombe A., Jeromin A., Hatem S.N.;
RT   "Kv4 potassium channels form a tripartite complex with the anchoring
RT   protein SAP97 and CaMKII in cardiac myocytes.";
RL   Circ. Res. 104:758-769(2009).
CC   -!- FUNCTION: Essential multidomain scaffolding protein required for
CC       normal development (By similarity). Recruits channels, receptors
CC       and signaling molecules to discrete plasma membrane domains in
CC       polarized cells. Regulates the excitability of cardiac myocytes by
CC       modulating the functional expression of Kv4 channels. Functional
CC       regulator of Kv1.5 channel (By similarity). May play a role in
CC       adherens junction assembly, signal transduction, cell
CC       proliferation, synaptogenesis and lymphocyte activation.
CC       {ECO:0000250, ECO:0000269|PubMed:14960569,
CC       ECO:0000269|PubMed:15044483, ECO:0000269|PubMed:15504326,
CC       ECO:0000269|PubMed:19213956}.
CC   -!- SUBUNIT: Homotetramer (Probable). Interacts with KCNF1 (By
CC       similarity). Interacts with CAMK2. Interacts through its PDZ
CC       domains with GRIN2A, KCNA1, KCNA2, KCNA3, KCNA4, KCNA5, KCND2,
CC       KCND3, GRIA1, GPR124 and GPR125. Interacts with cytoskeleton-
CC       associated proteins EPB41 and EZR. Found in a complex with KCNA5
CC       and CAV3. Found in a complex with APC and CTNNB1. Interacts with
CC       CDH1 through binding to PIK3R1. Forms multiprotein complexes with
CC       CASK, LIN7A, LIN7B, LIN7C, APBA1, and KCNJ12. Interacts through
CC       its guanylate kinase-like domain with KIF13B. Interacts with TOPK.
CC       Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A
CC       or LIN7C). May interact with HTR2A and TJAP1 (By similarity).
CC       Interacts through its guanylate kinase-like domain with DLGAP1,
CC       DLGAP2, DLGAP3, DLGAP4 and MAP1A. Interacts with LRFN1 and LRFN2.
CC       Interacts with LRFN4 and SFPQ (By similarity). Interacts with
CC       PTEN. Interacts with FRMPD4 (via C-terminus). {ECO:0000250,
CC       ECO:0000269|PubMed:11865057, ECO:0000269|PubMed:12933808,
CC       ECO:0000269|PubMed:14960569, ECO:0000269|PubMed:15951562,
CC       ECO:0000269|PubMed:16495444, ECO:0000269|PubMed:16630835,
CC       ECO:0000269|PubMed:19118189, ECO:0000269|PubMed:19213956,
CC       ECO:0000269|PubMed:9115257, ECO:0000269|PubMed:9677374,
CC       ECO:0000269|PubMed:9786987, ECO:0000305}.
CC   -!- INTERACTION:
CC       Q9Y297:BTRC (xeno); NbExp=3; IntAct=EBI-389325, EBI-307461;
CC       Q810C5:Dgki; NbExp=3; IntAct=EBI-389325, EBI-8523614;
CC       O08560:Dgkz; NbExp=4; IntAct=EBI-389325, EBI-8570505;
CC       P31016:Dlg4; NbExp=2; IntAct=EBI-389325, EBI-375655;
CC       O14490:DLGAP1 (xeno); NbExp=2; IntAct=EBI-389325, EBI-1753207;
CC       P89079:E4 (xeno); NbExp=4; IntAct=EBI-389325, EBI-7401124;
CC       Q8VDU0:Gpsm2 (xeno); NbExp=7; IntAct=EBI-389325, EBI-7575403;
CC       Q460M5:Lrfn2; NbExp=2; IntAct=EBI-389325, EBI-877185;
CC       P34926:Map1a; NbExp=2; IntAct=EBI-389325, EBI-631571;
CC       P60484:PTEN (xeno); NbExp=2; IntAct=EBI-389325, EBI-696162;
CC       B1AYL1:Scn7a (xeno); NbExp=3; IntAct=EBI-389325, EBI-8068354;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}. Basolateral cell membrane {ECO:0000250}.
CC       Endoplasmic reticulum membrane {ECO:0000250}. Cell junction,
CC       synapse, postsynaptic cell membrane, postsynaptic density
CC       {ECO:0000250}. Cell junction, synapse. Cell membrane, sarcolemma.
CC       Note=Colocalizes with EPB41 at regions of intercellular contacts.
CC       Basolateral in epithelial cells. May also associate with
CC       endoplasmic reticulum membranes. Mainly found in neurons soma,
CC       moderately found at postsynaptic densities (By similarity).
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Strongly expressed in
CC       epithelial cells, in the small intestine it is only detected in
CC       the vili. Expressed in brain, heart (at protein level), muscle,
CC       lung and liver. In the brain it was detected in olfactory bulbs,
CC       cerebral cortex, hippocampus, and spinal cord (at protein level).
CC       {ECO:0000269|PubMed:19213956, ECO:0000269|PubMed:7891172}.
CC   -!- INDUCTION: By BDNF. {ECO:0000269|PubMed:14597197}.
CC   -!- DOMAIN: The PDZ domains may also mediate association to membranes
CC       by binding to EPB41 and GPR124 together with the L27 domain that
CC       binds CASK and DLG2. {ECO:0000250}.
CC   -!- DOMAIN: The L27 domain may regulate DLG1 self-association. The N-
CC       terminal alternatively spliced region is capable of binding
CC       several SH3 domains and also moderates the level of protein
CC       oligomerization (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated by MAPK12 (By similarity). Phosphorylation of
CC       Ser-39 modulates transport to the plasma membrane and
CC       phosphorylation of Ser-232 regulates association with GRIN2A.
CC       {ECO:0000250, ECO:0000269|PubMed:12933808,
CC       ECO:0000269|PubMed:15044483}.
CC   -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00100}.
CC   -!- SIMILARITY: Contains 1 L27 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00365}.
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00143}.
CC   -!- SIMILARITY: Contains 1 SH3 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00192}.
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DR   EMBL; U14950; AAA79976.1; -; mRNA.
DR   PIR; I56552; I56552.
DR   RefSeq; NP_036920.1; NM_012788.1.
DR   UniGene; Rn.89331; -.
DR   PDB; 1RSO; NMR; -; A/C=4-63.
DR   PDB; 1ZOK; NMR; -; A=221-313.
DR   PDB; 2AWU; X-ray; 2.44 A; A/B=314-409.
DR   PDB; 2AWW; X-ray; 2.21 A; A/B=314-409.
DR   PDB; 2AWX; X-ray; 1.80 A; A/B=314-409.
DR   PDB; 2G2L; X-ray; 2.35 A; A/B=314-409.
DR   PDB; 2I0I; X-ray; 2.80 A; A/B/C=459-543.
DR   PDB; 2I0L; X-ray; 2.31 A; A/B=318-401.
DR   PDB; 3UAT; X-ray; 2.70 A; A=578-911.
DR   PDBsum; 1RSO; -.
DR   PDBsum; 1ZOK; -.
DR   PDBsum; 2AWU; -.
DR   PDBsum; 2AWW; -.
DR   PDBsum; 2AWX; -.
DR   PDBsum; 2G2L; -.
DR   PDBsum; 2I0I; -.
DR   PDBsum; 2I0L; -.
DR   PDBsum; 3UAT; -.
DR   ProteinModelPortal; Q62696; -.
DR   SMR; Q62696; 4-63, 221-313, 318-400, 462-542, 583-911.
DR   BioGrid; 247292; 16.
DR   DIP; DIP-31527N; -.
DR   IntAct; Q62696; 27.
DR   MINT; MINT-93379; -.
DR   STRING; 10116.ENSRNOP00000055673; -.
DR   PhosphoSite; Q62696; -.
DR   PaxDb; Q62696; -.
DR   PRIDE; Q62696; -.
DR   GeneID; 25252; -.
DR   KEGG; rno:25252; -.
DR   UCSC; RGD:2505; rat.
DR   CTD; 1739; -.
DR   RGD; 2505; Dlg1.
DR   eggNOG; COG0194; -.
DR   HOGENOM; HOG000232102; -.
DR   HOVERGEN; HBG107814; -.
DR   InParanoid; Q62696; -.
DR   KO; K12076; -.
DR   PhylomeDB; Q62696; -.
DR   EvolutionaryTrace; Q62696; -.
DR   NextBio; 605875; -.
DR   PRO; PR:Q62696; -.
DR   Genevestigator; Q62696; -.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:RGD.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0014069; C:postsynaptic density; TAS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; TAS:RGD.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
DR   GO; GO:0030315; C:T-tubule; IDA:RGD.
DR   GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR   GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR   GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEP:RGD.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0001935; P:endothelial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0043268; P:positive regulation of potassium ion transport; IMP:RGD.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:RGD.
DR   GO; GO:0016337; P:single organismal cell-cell adhesion; ISS:UniProtKB.
DR   Gene3D; 2.30.42.10; -; 3.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR016313; DLG1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR015143; L27_1.
DR   InterPro; IPR019590; MAGUK_PEST_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR019583; PDZ_assoc.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR23119; PTHR23119; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF09058; L27_1; 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; SM00569; L27; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SSF50044; 2.
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; PS51022; L27; 1.
DR   PROSITE; PS50106; PDZ; 3.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell junction; Cell membrane; Complete proteome;
KW   Endoplasmic reticulum; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Reference proteome; Repeat; SH3 domain;
KW   Synapse.
FT   CHAIN         1    911       Disks large homolog 1.
FT                                /FTId=PRO_0000094550.
FT   DOMAIN        4     64       L27. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00365}.
FT   DOMAIN      224    310       PDZ 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00143}.
FT   DOMAIN      318    404       PDZ 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00143}.
FT   DOMAIN      465    545       PDZ 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00143}.
FT   DOMAIN      580    650       SH3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00192}.
FT   DOMAIN      721    896       Guanylate kinase-like.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00100}.
FT   REGION      162    212       Interaction with SH3 domains.
FT                                {ECO:0000250}.
FT   MOD_RES      39     39       Phosphoserine; by CaMK2.
FT                                {ECO:0000269|PubMed:15044483}.
FT   MOD_RES     122    122       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     158    158       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     232    232       Phosphoserine; by CaMK2.
FT                                {ECO:0000269|PubMed:12933808}.
FT   MOD_RES     398    398       Phosphotyrosine. {ECO:0000250}.
FT   MOD_RES     567    567       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     574    574       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     618    618       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     684    684       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     687    687       Phosphoserine. {ECO:0000250}.
FT   MUTAGEN      39     39       S->A: No enrichment in postsynaptic
FT                                density upon CaMK2 activation.
FT                                {ECO:0000269|PubMed:15044483}.
FT   MUTAGEN      39     39       S->D: Localizes at the postsynaptic
FT                                density. {ECO:0000269|PubMed:15044483}.
FT   MUTAGEN     232    232       S->A: No effect on association with
FT                                GRIN2B. {ECO:0000269|PubMed:12933808}.
FT   MUTAGEN     232    232       S->D: Partial loss of association with
FT                                GRIN2B. {ECO:0000269|PubMed:12933808}.
FT   HELIX         5     20
FT   STRAND       23     26
FT   HELIX        28     42
FT   HELIX        44     52
FT   STRAND       55     61
FT   STRAND      225    227
FT   STRAND      235    239
FT   STRAND      242    246
FT   STRAND      254    258
FT   STRAND      260    262
FT   HELIX       263    267
FT   STRAND      277    279
FT   HELIX       289    297
FT   STRAND      301    306
FT   STRAND      316    322
FT   STRAND      327    334
FT   STRAND      347    352
FT   HELIX       357    361
FT   STRAND      369    373
FT   HELIX       383    391
FT   STRAND      395    402
FT   STRAND      405    407
FT   STRAND      464    469
FT   STRAND      476    481
FT   STRAND      483    486
FT   STRAND      488    493
FT   HELIX       498    502
FT   HELIX       524    532
FT   STRAND      536    542
FT   STRAND      583    587
FT   TURN        593    595
FT   STRAND      611    616
FT   STRAND      619    628
FT   STRAND      638    641
FT   HELIX       643    651
FT   STRAND      709    717
FT   STRAND      724    728
FT   HELIX       731    741
FT   TURN        743    745
FT   TURN        763    765
FT   HELIX       773    781
FT   STRAND      785    791
FT   STRAND      794    799
FT   HELIX       800    807
FT   TURN        808    810
FT   STRAND      812    815
FT   HELIX       820    827
FT   STRAND      833    837
FT   HELIX       842    848
FT   HELIX       854    871
FT   HELIX       872    874
FT   STRAND      876    879
FT   HELIX       884    898
FT   STRAND      900    906
SQ   SEQUENCE   911 AA;  100571 MW;  18CEBD31DD0CAF8B CRC64;
     MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVISI FQSNLFQALI DIQEFYEVTL
     LDNPKCVDHS KQCEPVQPGN PWESGSLSSA AVTSESLPGG LSPPVEKYRY QDEEVLPSER
     ISPQVPNEVL GPELVHVSEK SLSEIENVHG FVSHSHISPI KPTEAVPPSS PIVPVTPALP
     VPAESPVVLP STPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG
     GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EADVRDVTHS KAVEALKEAG
     SIVRLYVKRR KAFRKNHEIK LIKGPKGLGF SIAGGVGNQH IPGDNSIYVT KIIEGGAAHK
     DGKLQIGDKL LAVNSVCLEE VTHEEAVTAL KNTSDFVYLK AAKPTSMYIN DGYAPPDITN
     SSSQSVDNHV SPSSYLGQTP ASPARYSPIS KAVLGDDEIT REPRKVVLHR GSTGLGFNIV
     GGEDGEGIFI SFILAGGPAD LSGELRKGDR IISVNSVDLR AASHEQAAAA LKNAGQAVTI
     VAQYRPEEYS RFEAKIHDLR ETMMNSSVSS GSGSLRTSQK RSLYVRALFD YDKTKDSGLP
     SQGLNFKFGD ILHVINASDD EWWQARQVTP DGESDEVGVI PSKRRVEKKE RARLKTVKFN
     SKTRGDKGEI PDDMGSKGLK HVTSNASDSE SSYHEYGCSK GGQEEYVLSY EPVNQQEVNY
     TRPVIILGPM KDRVNDDLIS EFPDKFGSCV PHTTRPKRDY EVDGRDYHFV TSREQMEKDI
     QEHKFIEAGQ YNNHLYGTSV QSVRAVAEKG KHCILDVSGN AIKRLQIAQL YPISIFIKPK
     SMENIMEMNK RLTDEQARKT FERAVRLEQE FTEHFTAIVQ GDTLEDIYNQ VKQIIEEQSG
     PYIWVPAKEK L
//
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