[1]
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NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=7891172 [NCBI, ExPASy, EBI, Israel, Japan]
Mueller B.M.,
Kistner U.,
Veh R.W.,
Cases-Langhoff C.,
Becker B.,
Gundelfinger E.D.,
Garner C.C.;
"Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein.";
J. Neurosci. 15:2354-2366(1995).
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[2]
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INTERACTION WITH DLGAP1; DLGAP2; DLGAP3 AND DLGAP4.
DOI=10.1074/jbc.272.18.11943; PubMed=9115257 [NCBI, ExPASy, EBI, Israel, Japan]
Takeuchi M.,
Hata Y.,
Hirao K.,
Toyoda A.,
Irie M.,
Takai Y.;
"SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density.";
J. Biol. Chem. 272:11943-11951(1997).
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[3]
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INTERACTION WITH GRIA1.
DOI=10.1074/jbc.273.31.19518; PubMed=9677374 [NCBI, ExPASy, EBI, Israel, Japan]
Leonard A.S.,
Davare M.A.,
Horne M.C.,
Garner C.C.,
Hell J.W.;
"SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit.";
J. Biol. Chem. 273:19518-19524(1998).
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[4]
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INTERACTION WITH MAP1A.
PubMed=9786987 [NCBI, ExPASy, EBI, Israel, Japan]
Brenman J.E.,
Topinka J.R.,
Cooper E.C.,
McGee A.W.,
Rosen J.,
Milroy T.,
Ralston H.J.,
Bredt D.S.;
"Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A.";
J. Neurosci. 18:8805-8813(1998).
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[5]
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SUBCELLULAR LOCATION.
DOI=10.1083/jcb.148.1.147; PubMed=10629225 [NCBI, ExPASy, EBI, Israel, Japan]
Tiffany A.M.,
Manganas L.N.,
Kim E.,
Hsueh Y.P.,
Sheng M.,
Trimmer J.S.;
"PSD-95 and SAP97 exhibit distinct mechanisms for regulating K(+) channel surface expression and clustering.";
J. Cell Biol. 148:147-158(2000).
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[6]
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INTERACTION WITH CASK, AND SUBCELLULAR LOCATION.
DOI=10.1128/MCB.22.6.1778-1791.2002; PubMed=11865057 [NCBI, ExPASy, EBI, Israel, Japan]
Lee S.,
Fan S.,
Makarova O.,
Straight S.,
Margolis B.;
"A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia.";
Mol. Cell. Biol. 22:1778-1791(2002).
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[7]
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INDUCTION BY BDNF.
DOI=10.1016/j.ydbio.2003.07.008; PubMed=14597197 [NCBI, ExPASy, EBI, Israel, Japan]
Jourdi H.,
Iwakura Y.,
Narisawa-Saito M.,
Ibaraki K.,
Xiong H.,
Watanabe M.,
Hayashi Y.,
Takei N.,
Nawa H.;
"Brain-derived neurotrophic factor signal enhances and maintains the expression of AMPA receptor-associated PDZ proteins in developing cortical neurons.";
Dev. Biol. 263:216-230(2003).
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[8]
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MUTAGENESIS OF SER-232, PHOSPHORYLATION AT SER-232, AND INTERACTION WITH GRIN2A.
DOI=10.1074/jbc.M303576200; PubMed=12933808 [NCBI, ExPASy, EBI, Israel, Japan]
Gardoni F.,
Mauceri D.,
Fiorentini C.,
Bellone C.,
Missale C.,
Cattabeni F.,
Di Luca M.;
"CaMKII-dependent phosphorylation regulates SAP97/NR2A interaction.";
J. Biol. Chem. 278:44745-44752(2003).
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[9]
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INTERACTION WITH CASK; LIN7A; LIN7B; LIN7C; APBA1 AND KCNJ12, AND FUNCTION.
DOI=10.1074/jbc.M400284200; PubMed=14960569 [NCBI, ExPASy, EBI, Israel, Japan]
Leonoudakis D.,
Conti L.R.,
Radeke C.M.,
McGuire L.M.,
Vandenberg C.A.;
"A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels.";
J. Biol. Chem. 279:19051-19063(2004).
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[10]
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MUTAGENESIS OF SER-39, PHOSPHORYLATION AT SER-39, SUBCELLULAR LOCATION, AND FUNCTION.
DOI=10.1074/jbc.M402796200; PubMed=15044483 [NCBI, ExPASy, EBI, Israel, Japan]
Mauceri D.,
Cattabeni F.,
Di Luca M.,
Gardoni F.;
"Calcium/calmodulin-dependent protein kinase II phosphorylation drives synapse-associated protein 97 into spines.";
J. Biol. Chem. 279:23813-23821(2004).
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[11]
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FUNCTION.
DOI=10.1016/j.neuron.2004.10.012; PubMed=15504326 [NCBI, ExPASy, EBI, Israel, Japan]
Nakagawa T.,
Futai K.,
Lashuel H.A.,
Lo I.,
Okamoto K.,
Walz T.,
Hayashi Y.,
Sheng M.;
"Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions.";
Neuron 44:453-467(2004).
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- 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: 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.
- INTERACTION:
Q460M5:-; NbExp=1; IntAct=EBI-389325, EBI-877185;
P08588:ADRB1 (xeno); NbExp=1; IntAct=EBI-389325, EBI-991009;
Q01814-1:ATP2B2 (xeno); NbExp=1; IntAct=EBI-389325, EBI-1174262;
P23634-6:ATP2B4 (xeno); NbExp=1; IntAct=EBI-389325, EBI-1174437;
P34926:Map1a; NbExp=2; IntAct=EBI-389325, EBI-631571;
P60484:PTEN (xeno); NbExp=1; IntAct=EBI-389325, EBI-696162;
- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By similarity). Basolateral cell membrane (By similarity). Endoplasmic reticulum membrane (By similarity). Cell junction, synapse, postsynaptic cell membrane, postsynaptic density (By similarity). Cell junction, synapse. 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).
- DOMAIN: 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).
- PTM: Phosphorylation of Ser-39 modulates transport to the plasma membrane and phosphorylation of Ser-232 regulates association with GRIN2A.
- SIMILARITY: Belongs to the MAGUK family.
- SIMILARITY: Contains 1 guanylate kinase-like domain.
- SIMILARITY: Contains 1 L27 domain.
- SIMILARITY: Contains 3 PDZ (DHR) domains.
- SIMILARITY: Contains 1 SH3 domain.
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