Gamma-aminobutyric acid receptor-associated protein Recombinant Protein | GABARAP recombinant protein

Recombinant Human Gamma-aminobutyric acid receptor-associated protein

Cat. Num. AAA717135

• Gene Names: GABARAP; MM46; ATG8A; GABARAP-a
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Gamma-aminobutyric acid receptor-associated protein; Recombinant Human Gamma-aminobutyric acid receptor-associated protein; GABA(A) receptor-associated protein; MM46; GABARAP recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 2-117aa; Partial
• Sequence: KFVYKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMGQLYQEHHEEDFFLYIAYSDESVYGL
• Sequence Length: 117

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for GABARAP recombinant protein

Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in apoptosis. Involved in autophagy. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation.

Product Categories/Family for GABARAP recombinant protein

Transport

References

GABA(A) -receptor-associated protein links GABA(A) receptors and the cytoskeleton.Wang H., Bedford F.K., Brandon N.J., Moss S.J., Olsen R.W.Nature 397:69-72(1999) Interaction of the Unc-51-like kinase and microtubule-associated protein light chain 3 related proteins in the brain possible role of vesicular transport in axonal elongation.Okazaki N., Yan J., Yuasa S., Ueno T., Kominami E., Masuho Y., Koga H., Muramatsu M.-A.Brain Res. Mol. Brain Res. 85:1-12(2000) Iijima M., Mitsui Y.Ye M., Fu G., Wu J., Zhou J., Zhang Q., Shen Y., Kan L., He K., Gu B., Chen S., Mao M., Chen Z.Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3.Tanida I., Tanida-Miyake E., Ueno T., Kominami E.J. Biol. Chem. 276:1701-1706(2001) Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p.Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.J. Biol. Chem. 277:13739-13744(2002) GATE-16 and GABARAP are authentic modifiers mediated by Apg7 and Apg3.Tanida I., Komatsu M., Ueno T., Kominami E.Biochem. Biophys. Res. Commun. 300:637-644(2003) LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation.Kabeya Y., Mizushima N., Yamamoto A., Oshitani-Okamoto S., Ohsumi Y., Yoshimori T.J. Cell Sci. 117:2805-2812(2004) GABAA receptor-associated protein (GABARAP) induces apoptosis by interacting with DEAD (Asp-Glu-Ala-Asp/His) box polypeptide 47 (DDX 47) .Lee J.H., Rho S.B., Chun T.Biotechnol. Lett. 27:623-628(2005) p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy.Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H., Overvatn A., Bjorkoy G., Johansen T.J. Biol. Chem. 282:24131-24145(2007) The TP53INP2 protein is required for autophagy in mammalian cells.Nowak J., Archange C., Tardivel-Lacombe J., Pontarotti P., Pebusque M.J., Vaccaro M.I., Velasco G., Dagorn J.C., Iovanna J.L.Mol. Biol. Cell 20:870-881(2009) Network organization of the human autophagy system.Behrends C., Sowa M.E., Gygi S.P., Harper J.W.Nature 466:68-76(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation.Itoh T., Kanno E., Uemura T., Waguri S., Fukuda M.J. Cell Biol. 192:839-853(2011) MAPK15/ERK8 stimulates autophagy by interacting with LC3 and GABARAP proteins.Colecchia D., Strambi A., Sanzone S., Iavarone C., Rossi M., Dall'Armi C., Piccioni F., Verrotti di Pianella A., Chiariello M.Autophagy 8:1724-1740(2012) TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death.Seillier M., Peuget S., Gayet O., Gauthier C., N'guessan P., Monte M., Carrier A., Iovanna J.L., Dusetti N.J.Cell Death Differ. 19:1525-1535(2012) ATG8 family proteins act as scaffolds for assembly of the ULK complex sequence requirements for LC3-interacting region (LIR) motifs.Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B., Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.J. Biol. Chem. 287:39275-39290(2012) Rab GTPase-activating proteins in autophagy regulation of endocytic and autophagy pathways by direct binding to human ATG8 modifiers.Popovic D., Akutsu M., Novak I., Harper J.W., Behrends C., Dikic I.Mol. Cell. Biol. 32:1733-1744(2012) DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding dual regulators of autophagy and transcription.Sancho A., Duran J., Garcia-Espana A., Mauvezin C., Alemu E.A., Lamark T., Macias M.J., Desalle R., Royo M., Sala D., Chicote J.U., Palacin M., Johansen T., Zorzano A.PLoS ONE 7:E34034-E34034(2012) Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites.Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.Nature 502:254-257(2013) The X-ray crystal structure and putative ligand-derived peptide binding properties of gamma-aminobutyric acid receptor type A receptor-associated protein.Knight D., Harris R., McAlister M.S.B., Phelan J.P., Geddes S., Moss S.J., Driscoll P.C., Keep N.H.J. Biol. Chem. 277:5556-5561(2002) Solution structure of human GABA(A) receptor-associated protein GABARAP implications for biological function and its regulation.Stangler T., Mayr L.M., Willbold D.J. Biol. Chem. 277:13363-13366(2002) 1H, 13C and '5N resonance assignments of GABARAP, GABAA receptor associated protein.Kouno T., Miura K., Kanematsu T., Shirakawa M., Hirata M., Kawano K.J. Biomol. NMR 22:97-98(2002) Ligand binding mode of GABAA receptor-associated protein.Weiergraber O.H., Stangler T., Thielmann Y., Mohrluder J., Wiesehan K., Willbold D.J. Mol. Biol. 381:1320-1331(2008) Structural framework of the GABARAP-calreticulin interface --implications for substrate binding to endoplasmic reticulum chaperones.Thielmann Y., Weiergraber O.H., Mohrluder J., Willbold D.FEBS J. 276:1140-1152(2009)

NCBI and Uniprot Product Information

• NCBI GI #: 6005764
• NCBI GeneID: 11337
• NCBI Accession #: NP_009209.1
• NCBI GenBank Nucleotide #: NM_007278.1
• UniProt Accession #: O95166
• Molecular Weight: 40.8 kDa
• NCBI Official Full Name: gamma-aminobutyric acid receptor-associated protein
• NCBI Official Synonym Full Names: GABA(A) receptor-associated protein
• NCBI Official Symbol: GABARAP
• NCBI Official Synonym Symbols: MM46; ATG8A; GABARAP-a
• NCBI Protein Information: gamma-aminobutyric acid receptor-associated protein
• UniProt Protein Name: Gamma-aminobutyric acid receptor-associated protein
• Protein Family: Gamma-aminobutyric acid receptor-associated protein
• UniProt Gene Name: GABARAP
• UniProt Synonym Gene Names: FLC3B
• UniProt Entry Name: GBRAP_HUMAN

NCBI Description

Gamma-aminobutyric acid A receptors [GABA(A) receptors] are ligand-gated chloride channels that mediate inhibitory neurotransmission. This gene encodes GABA(A) receptor-associated protein, which is highly positively charged in its N-terminus and shares sequence similarity with light chain-3 of microtubule-associated proteins 1A and 1B. This protein clusters neurotransmitter receptors by mediating interaction with the cytoskeleton. [provided by RefSeq, Jul 2008]

Uniprot Description

GABARAP: is a ubiquitin-like protein that is a constituent of the ATG8-conjugation system, one of two evolutionarily conserved phosphatidylethanolamine conjugation systems necessary for the formation of the autophagosome. The human ATG8 system includes seven ubiquitin-like light chain proteins (LCPs) that are homologs of yeast LC3: MAP1LC3A, -B, -C, GABARAP, GABARAPL1, -2, and -3. Pro-LCPs are cleaved by ATG4B to expose a C-terminal glycine residue, the cytosolic LCP-I form. The exposed C-terminus is conjugated to the head group amine of phosphatidylethanolamine (PE) through an amide bond by a sequence of ubiquitination-like reactions that involves an E1 (ATG7), an E2 (ATG3), and an E3 (a complex including ATG5, ATG12, and ATG16L). The PE-congugated form (LCP-II) is tightly associated with the autophagosomal membrane. The LCP-II forms can also be delipidated by the ATG4 proteases: most of the LCPs are delipidated and liberated from the membrane before autophagosomes fuse with lysosomes. May play a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Belongs to the MAP1 LC3 family. Interacts with GPHN and NSF. Interacts with GABRG2, beta-tubulin and ULK1.

Protein type: Adaptor/scaffold; Ubiquitin-like modifier; Autophagy; Microtubule-binding; Vesicle

Chromosomal Location of Human Ortholog: 17p13.1

Cellular Component: actin cytoskeleton; autophagic vacuole; axoneme; cytoplasmic vesicle; cytosol; Golgi membrane; lysosome; microtubule; microtubule associated complex; perinuclear region of cytoplasm; plasma membrane; smooth endoplasmic reticulum

Molecular Function: beta-tubulin binding; GABA receptor binding; microtubule binding; protein binding; ubiquitin protein ligase binding

Biological Process: induction of apoptosis via death domain receptors; macroautophagy; microtubule cytoskeleton organization and biogenesis; protein targeting; synaptic transmission