DLG1

1PDR, 2M3M, 2OQS, 2X7Z, 3RL7, 3RL8, 3W9Y, 4AMH, 4G69173913383ENSG00000075711ENSMUSG00000022770Q12959Q811D0NM_004087NM_001363865NM_001366203NM_001366204NM_001366205NM_001366206NM_001366207NM_001366208NM_001366209NM_001366210NM_001366211NM_001366212NM_001366213NM_001366214NM_001366215NM_001366216NM_001366217NM_001366218NM_001366219NM_001366220NM_001366221NM_001366222NM_001357281NM_001357282NP_004078NP_001350794NP_001353132NP_001353133NP_001353134NP_001353135NP_001353136NP_001353137NP_001353138NP_001353139NP_001353140NP_001353141NP_001353142NP_001353143NP_001353144NP_001353145NP_001353146NP_001353147NP_001353148NP_001353149NP_001353150NP_001353151NP_001344210NP_001344211Discs large homolog 1 (DLG1), also known as synapse-associated protein 97 or SAP97, is a scaffold protein that in humans is encoded by the SAP97 gene.1iu0: The first PDZ domain of PSD-951iu2: The first PDZ domain of PSD-951kef: PDZ1 of SAP901pdr: CRYSTAL STRUCTURE OF THE THIRD PDZ DOMAIN FROM THE HUMAN HOMOLOG OF DISCS LARGE PROTEIN1rgr: Cyclic Peptides Targeting PDZ Domains of PSD-95: Structural Basis for Enhanced Affinity and Enzymatic Stability1rso: Hetero-tetrameric L27 (Lin-2, Lin-7) domain complexes as organization platforms of supra-molecular assemblies1zok: PDZ1 Domain Of Synapse Associated Protein 972awu: Synapse associated protein 97 PDZ2 domain variant C378G2aww: Synapse associated protein 97 PDZ2 domain variant C378G with C-terminal GluR-A peptide2awx: Synapse associated protein 97 PDZ2 domain variant C378S2g2l: Crystal Structure of the Second PDZ Domain of SAP97 in Complex with a GluR-A C-terminal Peptide2i0i: X-ray crystal structure of Sap97 PDZ3 bound to the C-terminal peptide of HPV18 E62i0l: X-ray crystal structure of Sap97 PDZ2 bound to the C-terminal peptide of HPV18 E6. Discs large homolog 1 (DLG1), also known as synapse-associated protein 97 or SAP97, is a scaffold protein that in humans is encoded by the SAP97 gene. SAP97 is a mammalian MAGUK-family member protein that is similar to the Drosophila protein Dlg1 (the protein is alternatively referred to as hDlg1, and the human gene is DLG1). SAP97 is expressed throughout the body in epithelial cells. In the brain it is involved in the trafficking of ionotropic receptors from the endoplasmic reticulum to the plasma membrane, and may be involved in the trafficking AMPAR during synaptic plasticity. SAP97 is expressed throughout the body in epithelial cells, including the kidney and brain. There is some evidence that SAP97 regulates cell-to-cell adhesion during cell death, and may interact with HPV. In the brain, SAP97's function is involved in the trafficking of transmembrane receptors from the ER to the plasma membrane. SAP97's function has been investigated by reducing its expression by knockout or increasing its expression heterologously. Mice in which the SAP97 gene has been knocked out die perinatally, have a cleft palate, and deficiencies in renal function. Overexpression of SAP97 in mammalian neurons leads to increased synaptic strength. Mutations in DLG1 are associated to Crohn's Disease. SAP97's protein structure consists of an alternatively-spliced n-terminal domain, three PDZ domains, an SH3 domain, hook domain, I3 domain, and finally an inactive guanylate kinase (GK) domain. Each of these domains has specific interacting partners that help define SAP97's unique function. The n-terminal of SAP97 can be alternatively spliced to contain a double-cysteine/palmitoylation site (α-isoform), or an L27 domain (β-isoform. The L27 domain is involved in SAP97 oligomerization with other SAP97 molecules, CASK, and other L27-domain-containing proteins. There is also a myosin VI binding site near n-terminal which may be involved in the internalization of AMPAR. Each of SAP97's PDZ domains have different binding partners, including the AMPAR subunit GluR1 for the first PDZ domain, and neuroligin for the last. SAP97's I3 domain is unique to SAP97 among the MAGUK family, and is known to regulate the post-synaptic localization of SAP97 and to bind the protein 4.1N. The GK domain allows SAP97 to bind to GKAP/SAPAP-family proteins.