Protein Details: Gamma-aminobutyric acid receptor-associated protein

Protein ID

ICDB_Pro_0291

Protein Name

Gamma-aminobutyric acid receptor-associated protein

Gene Name

GABARAP; FLC3B; HT004

Organism

Homo sapiens (Human)

Length

117 amino acids

AlphaFoldDB

AF-O95166-F1-model_v4.pdb

Function

Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in autophagy: while LC3s are involved in elongation of the phagophore membrane;the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Through its interaction with the reticulophagy receptor TEX264;participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress;which then fuse with lysosomes for endoplasmic reticulum turnover. Also required for the local activation of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex;regulating ubiquitination and degradation of TIAM1;a guanyl-nucleotide exchange factor (GEF) that activates RAC1 and downstream signal transduction. Thereby;regulates different biological processes including the organization of the cytoskeleton;cell migration and proliferation. Involved in apoptosis.

Sequence

MKFVYKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMGQLYQEHHEEDFFLYIAYSDESVYGL

PDB Structures

1GNU 1KLV 1KM7 1KOT 3D32 3DOW 3WIM 4XC2 5DPS 6HB9 6HOG 6HOH 6HOJ 6HOK 6HYL 6HYM 6HYN 6HYO 6YOP 7AA8 7BRQ 7BRT 7BRU 7BV4 7EA7 7LSW 7LT6 7VEC 7VED 7YO9 7ZKR 7ZL7 8AFI 8T2M 8T2N

Ligand Binding

1. DICL_CP

2. DICL_Pep

Binding Site

Disease

Stiff-Person Syndrome and Adrenal Gland Ganglioneuroblastoma

Location

Heart;brain;placenta;liver;skeletal muscle;kidney and pancreas

DOI ID

10.1038/16264; 10.1016/s0169-328x(00)00218-7; 10.1073/pnas.160270997; 10.1074/jbc.c000752200; 10.1074/jbc.m200385200; 10.1016/s0006-291x(02)02907-8; 10.1242/jcs.01131; 10.1007/s10529-005-3628-2; 10.1074/jbc.m702824200; 10.1091/mbc.e08-07-0671; 10.4161/auto.6.7.13075; 10.1038/nature09204; 10.1186/1752-0509-5-17; 10.1083/jcb.201008107; 10.4161/auto.21857; 10.1038/cdd.2012.30; 10.1074/jbc.m112.378109; 10.1128/mcb.06717-11; 10.1371/journal.pone.0034034; 10.1038/nature12606; 10.4161/auto.29640; 10.1016/j.devcel.2014.06.013; 10.1083/jcb.201503023; 10.1074/jbc.m116.715474; 10.1083/jcb.201708039; 10.1080/15548627.2019.1569925; 10.1016/j.molcel.2019.03.033; 10.5483/bmbrep.2019.52.12.211; 10.1016/j.devcel.2020.03.018; 10.15252/embr.202052289; 10.1016/j.molcel.2021.03.020; 10.1038/s41418-022-01098-6; 10.1074/jbc.m109753200; 10.1074/jbc.c200050200; 10.1023/a:1013884402033; 10.1016/j.jmb.2008.06.086; 10.1111/j.1742-4658.2008.06857.x; 10.1002/embr.201338003; 10.1016/j.molcel.2014.12.040; 10.1038/s41467-020-17163-y; 10.1021/acscentsci.3c00009

RefSeq

NP_009209.1