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Reviewed, UniProtKB/Swiss-Prot Q62696 (DLG1_RAT)

Last modified November 25, 2008. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Disks large homolog 1
Alternative name(s):
    Synapse-associated protein 97
      Short name=SAP-97
Gene names
Name: Dlg1
Synonyms: Dlgh1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length911 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Essential multidomain scaffolding protein required for normal development By similarity. Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation.

Subunit structure

Homotetramer Probable. Interacts through its PDZ domains with GRIN2A, KCNA1, KCNA2, KCNA3, KCNA4, KCNA5, GRIA1, GPR124 and GPR125. Interacts with cytoskeleton-associated proteins EPB41 and EZR. Found in a complex with KCNA5 and CAV3. Found in a complex with APC and CTNNB1. Interacts with CDH1 through binding to PIK3R1. Forms multiprotein complexes with CASK, LIN7A, LIN7B, LIN7C, APBA1, and KCNJ12. Interacts through its guanylate kinase-like domain with KIF13B. Interacts with TOPK. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C). May interact with HTR2A and TJAP1 By similarity. Interacts through its guanylate kinase-like domain with DLGAP1, DLGAP2, DLGAP3, DLGAP4 and MAP1A. Interacts with LRFN1.

Subcellular location

Membrane; Peripheral membrane proteinBy similarity. Basolateral cell membraneBy similarity. Endoplasmic reticulum membraneBy similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic densityBy similarity. Cell junctionsynapse. Note= Colocalizes with EPB41 at regions of intercellular contacts. Basolateral in epithelial cells. May also associate with endoplasmic reticulum membranes. Mainly found in neurons soma, moderately found at postsynaptic densities By similarity.

Tissue specificity

Widely expressed. Strongly expressed in epithelial cells, in the small intestine it is only detected in the vili. In the brain it was detected in olfactory bulbs, cerebral cortex, hippocampus, and spinal cord (at protein level). Expressed in brain, heart, muscle, lung and liver.

Induction

By BDNF.

Domain

The PDZ domains may also mediate association to membranes by binding to EPB41 and GPR124 together with the L27 domain that binds CASK and DLG2 By similarity.

The L27 domain may regulate DLG1 self-association. The N-terminal alternatively spliced region is capable of binding several SH3 domains and also moderates the level of protein oligomerization By similarity.

Post-translational modification

Phosphorylation of Ser-39 modulates transport to the plasma membrane and phosphorylation of Ser-232 regulates association with GRIN2A.

Sequence similarities

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 1 L27 domain.

Contains 3 PDZ (DHR) domains.

Contains 1 SH3 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ADRB1P085881EBI-389325,EBI-991009From a different organism.
ATP2B2Q01814-11EBI-389325,EBI-1174262From a different organism.
ATP2B4P23634-61EBI-389325,EBI-1174437From a different organism.
Lrfn2Q460M51EBI-389325,EBI-877185
Map1aP349262EBI-389325,EBI-631571
PTENP604841EBI-389325,EBI-696162From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 911911Disks large homolog 1
PRO_0000094550

Regions

Domain4 – 6461L27
Domain224 – 31087PDZ 1
Domain318 – 40487PDZ 2
Domain465 – 54581PDZ 3
Domain580 – 65071SH3
Domain721 – 896176Guanylate kinase-like
Region162 – 21251Interaction with SH3 domains By similarity

Amino acid modifications

Modified residue391Phosphoserine; by CaMK2
Modified residue1221Phosphoserine By similarity
Modified residue2321Phosphoserine; by CaMK2
Modified residue3011Phosphoserine By similarity
Modified residue3981Phosphotyrosine By similarity
Modified residue5741Phosphoserine By similarity
Modified residue6181Phosphoserine By similarity
Modified residue6831Phosphothreonine By similarity
Modified residue6841Phosphoserine By similarity
Modified residue6871Phosphoserine By similarity
Modified residue7671Phosphotyrosine By similarity

Experimental info

Mutagenesis391S → A: No enrichment in postsynaptic density upon CaMK2 activation
Mutagenesis391S → D: Localizes at the postsynaptic density
Mutagenesis2321S → A: No effect on association with GRIN2B
Mutagenesis2321S → D: Partial loss of association with GRIN2B

Secondary structure

.......................................................... 911
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q62696-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 18CEBD31DD0CAF8B

FASTA911100,571
        10         20         30         40         50         60 
MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVISI FQSNLFQALI DIQEFYEVTL 

        70         80         90        100        110        120 
LDNPKCVDHS KQCEPVQPGN PWESGSLSSA AVTSESLPGG LSPPVEKYRY QDEEVLPSER 

       130        140        150        160        170        180 
ISPQVPNEVL GPELVHVSEK SLSEIENVHG FVSHSHISPI KPTEAVPPSS PIVPVTPALP 

       190        200        210        220        230        240 
VPAESPVVLP STPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG 

       250        260        270        280        290        300 
GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EADVRDVTHS KAVEALKEAG 

       310        320        330        340        350        360 
SIVRLYVKRR KAFRKNHEIK LIKGPKGLGF SIAGGVGNQH IPGDNSIYVT KIIEGGAAHK 

       370        380        390        400        410        420 
DGKLQIGDKL LAVNSVCLEE VTHEEAVTAL KNTSDFVYLK AAKPTSMYIN DGYAPPDITN 

       430        440        450        460        470        480 
SSSQSVDNHV SPSSYLGQTP ASPARYSPIS KAVLGDDEIT REPRKVVLHR GSTGLGFNIV 

       490        500        510        520        530        540 
GGEDGEGIFI SFILAGGPAD LSGELRKGDR IISVNSVDLR AASHEQAAAA LKNAGQAVTI 

       550        560        570        580        590        600 
VAQYRPEEYS RFEAKIHDLR ETMMNSSVSS GSGSLRTSQK RSLYVRALFD YDKTKDSGLP 

       610        620        630        640        650        660 
SQGLNFKFGD ILHVINASDD EWWQARQVTP DGESDEVGVI PSKRRVEKKE RARLKTVKFN 

       670        680        690        700        710        720 
SKTRGDKGEI PDDMGSKGLK HVTSNASDSE SSYHEYGCSK GGQEEYVLSY EPVNQQEVNY 

       730        740        750        760        770        780 
TRPVIILGPM KDRVNDDLIS EFPDKFGSCV PHTTRPKRDY EVDGRDYHFV TSREQMEKDI 

       790        800        810        820        830        840 
QEHKFIEAGQ YNNHLYGTSV QSVRAVAEKG KHCILDVSGN AIKRLQIAQL YPISIFIKPK 

       850        860        870        880        890        900 
SMENIMEMNK RLTDEQARKT FERAVRLEQE FTEHFTAIVQ GDTLEDIYNQ VKQIIEEQSG 

       910 
PYIWVPAKEK L 

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References

[1]"Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein."
Mueller B.M., Kistner U., Veh R.W., Cases-Langhoff C., Becker B., Gundelfinger E.D., Garner C.C.
J. Neurosci. 15:2354-2366(1995) [PubMed: 7891172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Tissue: Brain.
[2]"SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density."
Takeuchi M., Hata Y., Hirao K., Toyoda A., Irie M., Takai Y.
J. Biol. Chem. 272:11943-11951(1997) [PubMed: 9115257] [Abstract]
Cited for: INTERACTION WITH DLGAP1; DLGAP2; DLGAP3 AND DLGAP4.
[3]"SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit."
Leonard A.S., Davare M.A., Horne M.C., Garner C.C., Hell J.W.
J. Biol. Chem. 273:19518-19524(1998) [PubMed: 9677374] [Abstract]
Cited for: INTERACTION WITH GRIA1.
[4]"Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A."
Brenman J.E., Topinka J.R., Cooper E.C., McGee A.W., Rosen J., Milroy T., Ralston H.J., Bredt D.S.
J. Neurosci. 18:8805-8813(1998) [PubMed: 9786987] [Abstract]
Cited for: INTERACTION WITH MAP1A.
[5]"PSD-95 and SAP97 exhibit distinct mechanisms for regulating K(+) channel surface expression and clustering."
Tiffany A.M., Manganas L.N., Kim E., Hsueh Y.P., Sheng M., Trimmer J.S.
J. Cell Biol. 148:147-158(2000) [PubMed: 10629225] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia."
Lee S., Fan S., Makarova O., Straight S., Margolis B.
Mol. Cell. Biol. 22:1778-1791(2002) [PubMed: 11865057] [Abstract]
Cited for: INTERACTION WITH CASK, SUBCELLULAR LOCATION.
[7]"Brain-derived neurotrophic factor signal enhances and maintains the expression of AMPA receptor-associated PDZ proteins in developing cortical neurons."
Jourdi H., Iwakura Y., Narisawa-Saito M., Ibaraki K., Xiong H., Watanabe M., Hayashi Y., Takei N., Nawa H.
Dev. Biol. 263:216-230(2003) [PubMed: 14597197] [Abstract]
Cited for: INDUCTION BY BDNF.
[8]"CaMKII-dependent phosphorylation regulates SAP97/NR2A interaction."
Gardoni F., Mauceri D., Fiorentini C., Bellone C., Missale C., Cattabeni F., Di Luca M.
J. Biol. Chem. 278:44745-44752(2003) [PubMed: 12933808] [Abstract]
Cited for: MUTAGENESIS OF SER-232, PHOSPHORYLATION AT SER-232, INTERACTION WITH GRIN2A.
[9]"A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels."
Leonoudakis D., Conti L.R., Radeke C.M., McGuire L.M., Vandenberg C.A.
J. Biol. Chem. 279:19051-19063(2004) [PubMed: 14960569] [Abstract]
Cited for: INTERACTION WITH CASK; LIN7A; LIN7B; LIN7C; APBA1 AND KCNJ12, FUNCTION.
[10]"Calcium/calmodulin-dependent protein kinase II phosphorylation drives synapse-associated protein 97 into spines."
Mauceri D., Cattabeni F., Di Luca M., Gardoni F.
J. Biol. Chem. 279:23813-23821(2004) [PubMed: 15044483] [Abstract]
Cited for: MUTAGENESIS OF SER-39, PHOSPHORYLATION AT SER-39, SUBCELLULAR LOCATION, FUNCTION.
[11]"Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions."
Nakagawa T., Futai K., Lashuel H.A., Lo I., Okamoto K., Walz T., Hayashi Y., Sheng M.
Neuron 44:453-467(2004) [PubMed: 15504326] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

U14950 mRNA. Translation: AAA79976.1.
PIRI56552.
RefSeqNP_036920.1.
UniGeneRn.89331

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1RSONMR-A/C4-63[»]
1ZOKNMR-A221-313[»]
2AWUX-ray2.44A/B318-410[»]
2AWWX-ray2.21A/B318-410[»]
2AWXX-ray1.80A/B318-410[»]
2G2LX-ray2.35A/B318-410[»]
2I0IX-ray2.80A/B/C459-543[»]
2I0LX-ray2.31A/B318-401[»]
SMRQ62696. Positions 454-554.
ModBaseSearch...

Protein-protein interaction databases

IntActQ62696.

PTM databases