GBRAP_RAT
ID GBRAP_RAT Reviewed; 117 AA.
AC P60517; Q9QUI7;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Gamma-aminobutyric acid receptor-associated protein;
DE AltName: Full=GABA(A) receptor-associated protein;
DE Flags: Precursor;
GN Name=Gabarap;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP BETA-TUBULIN.
RX PubMed=10899939; DOI=10.1046/j.1471-4159.2000.0750644.x;
RA Wang H., Olsen R.W.;
RT "Binding of the GABA(A) receptor-associated protein (GABARAP) to
RT microtubules and microfilaments suggests involvement of the cytoskeleton in
RT GABARAPGABA(A) receptor interaction.";
RL J. Neurochem. 75:644-655(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH GPHN.
RX PubMed=10900017; DOI=10.1073/pnas.97.15.8594;
RA Kneussel M., Haverkamp S., Fuhrmann J.C., Wang H., Waessle H., Olsen R.W.,
RA Betz H.;
RT "The gamma-aminobutyric acid type A receptor (GABAAR)-associated protein
RT GABARAP interacts with gephyrin but is not involved in receptor anchoring
RT at the synapse.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8594-8599(2000).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP NSF.
RX PubMed=11461150; DOI=10.1006/mcne.2001.1005;
RA Kittler J.T., Rostaing P., Schiavo G., Fritschy J.-M., Olsen R.,
RA Triller A., Moss S.J.;
RT "The subcellular distribution of GABARAP and its ability to interact with
RT NSF suggest a role for this protein in the intracellular transport of
RT GABA(A) receptors.";
RL Mol. Cell. Neurosci. 18:13-25(2001).
RN [5]
RP INTERACTION WITH KIF21B, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25172774; DOI=10.1016/j.ejcb.2014.07.007;
RA Labonte D., Thies E., Kneussel M.;
RT "The kinesin KIF21B participates in the cell surface delivery of gamma2
RT subunit-containing GABAA receptors.";
RL Eur. J. Cell Biol. 93:338-346(2014).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=11818336; DOI=10.1093/embo-reports/kvf026;
RA Bavro V.N., Sola M., Bracher A., Kneussel M., Betz H., Weissenhorn W.;
RT "Crystal structure of the GABA(A)-receptor-associated protein, GABARAP.";
RL EMBO Rep. 3:183-189(2002).
CC -!- FUNCTION: Ubiquitin-like modifier that plays a role in intracellular
CC transport of GABA(A) receptors and its interaction with the
CC cytoskeleton (PubMed:11461150). Involved in autophagy: while LC3s are
CC involved in elongation of the phagophore membrane, the GABARAP/GATE-16
CC subfamily is essential for a later stage in autophagosome maturation
CC (By similarity). Through its interaction with the reticulophagy
CC receptor TEX264, participates in the remodeling of subdomains of the
CC endoplasmic reticulum into autophagosomes upon nutrient stress, which
CC then fuse with lysosomes for endoplasmic reticulum turnover (By
CC similarity). Also required for the local activation of the
CC CUL3(KBTBD6/7) E3 ubiquitin ligase complex, regulating ubiquitination a
CC nd degradation of TIAM1, a guanyl-nucleotide exchange factor (GEF) that
CC activates RAC1 and downstream signal transduction. Thereby, regulates
CC different biological processes including the organization of the
CC cytoskeleton, cell migration and proliferation (By similarity).
CC Involved in apoptosis (By similarity). {ECO:0000250|UniProtKB:O95166,
CC ECO:0000269|PubMed:11461150}.
CC -!- SUBUNIT: Interacts with GPHN and NSF (PubMed:10900017,
CC PubMed:11461150). Interacts with ATG3, ATG7 and ATG13 (By similarity).
CC Interacts with alpha-tubulin (By similarity). Interacts with beta-
CC tubulin (PubMed:10899939). Interacts with GABRG2 (By similarity).
CC Interacts with RB1CC1 (By similarity). Interacts with ULK1 (By
CC similarity). Interacts with CALR (By similarity). Interacts with DDX47
CC (By similarity). Interacts with TP53INP1 and TP53INP2 (By similarity).
CC Interacts with TBC1D5 (By similarity). Interacts with TBC1D25 (By
CC similarity). Directly interacts with SQSTM1 (By similarity). Interacts
CC with MAPK15 (By similarity). Interacts with TECPR2 (By similarity).
CC Interacts with PCM1 (By similarity). Interacts with TRIM5 and TRIM21
CC (By similarity). Interacts with MEFV (By similarity). Interacts with
CC KIF21B (PubMed:25172774). Interacts with WDFY3; this interaction is
CC required for WDFY3 recruitment to MAP1LC3B-positive p62/SQSTM1 bodies
CC (By similarity). Interacts with FLCN; interaction regulates autophagy
CC (By similarity). Interacts with UBA5 (By similarity). Interacts with
CC KBTBD6 and KBTBD7; the interaction is direct and required for the
CC ubiquitination of TIAM1 (By similarity). {ECO:0000250|UniProtKB:O95166,
CC ECO:0000269|PubMed:10899939, ECO:0000269|PubMed:10900017,
CC ECO:0000269|PubMed:11461150, ECO:0000269|PubMed:25172774}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250|UniProtKB:O95166}. Endomembrane system
CC {ECO:0000269|PubMed:11461150}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10899939}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:11461150}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:25172774}. Note=Largely associated with
CC intracellular membrane structures including the Golgi apparatus and
CC postsynaptic cisternae (PubMed:11461150). Colocalizes with microtubules
CC (PubMed:10899939). Localizes also to discrete punctae along the ciliary
CC axoneme (By similarity). {ECO:0000250|UniProtKB:Q9DCD6,
CC ECO:0000269|PubMed:10899939, ECO:0000269|PubMed:11461150}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level)
CC (PubMed:25172774). Can be found in both somatodendritic and axonal
CC compartment of neurons (PubMed:11461150). {ECO:0000269|PubMed:11461150,
CC ECO:0000269|PubMed:25172774}.
CC -!- PTM: The precursor molecule is cleaved by ATG4 (ATG4A, ATG4B, ATG4C or
CC ATG4D) to expose the glycine at the C-terminus and form the cytosolic
CC form, GABARAP-I. The processed form is then activated by APG7L/ATG7,
CC transferred to ATG3 and conjugated to phosphatidylethanolamine (PE)
CC phospholipid to form the membrane-bound form, GABARAP-II. During non-
CC canonical autophagy, the processed form is conjugated to
CC phosphatidylserine (PS) phospholipid. ATG4 proteins also mediate the
CC delipidation of PE-conjugated forms. In addition, ATG4B and ATG4D
CC mediate delipidation of ATG8 proteins conjugated to PS during non-
CC canonical autophagy. ATG4B constitutes the major protein for
CC proteolytic activation (By similarity). ATG4D is the main enzyme for
CC delipidation activity (By similarity). {ECO:0000250|UniProtKB:O95166,
CC ECO:0000250|UniProtKB:Q9DCD6}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR EMBL; AF161588; AAD47643.1; -; mRNA.
DR EMBL; BC058441; AAH58441.1; -; mRNA.
DR RefSeq; NP_742033.1; NM_172036.3.
DR PDB; 1KJT; X-ray; 2.00 A; A=1-117.
DR PDBsum; 1KJT; -.
DR AlphaFoldDB; P60517; -.
DR BMRB; P60517; -.
DR SMR; P60517; -.
DR BioGRID; 248705; 5.
DR IntAct; P60517; 1.
DR STRING; 10116.ENSRNOP00000023724; -.
DR iPTMnet; P60517; -.
DR PhosphoSitePlus; P60517; -.
DR PaxDb; P60517; -.
DR GeneID; 58974; -.
DR KEGG; rno:58974; -.
DR UCSC; RGD:61911; rat.
DR CTD; 11337; -.
DR RGD; 61911; Gabarap.
DR VEuPathDB; HostDB:ENSRNOG00000017417; -.
DR eggNOG; KOG1654; Eukaryota.
DR HOGENOM; CLU_119276_0_0_1; -.
DR InParanoid; P60517; -.
DR OMA; AVYQEHK; -.
DR OrthoDB; 1508198at2759; -.
DR PhylomeDB; P60517; -.
DR TreeFam; TF314556; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR Reactome; R-RNO-8854214; TBC/RABGAPs.
DR EvolutionaryTrace; P60517; -.
DR PRO; PR:P60517; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000017417; Expressed in testis and 20 other tissues.
DR Genevisible; P60517; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; ISO:RGD.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:RGD.
DR GO; GO:0097225; C:sperm midpiece; ISO:RGD.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:RGD.
DR GO; GO:0050811; F:GABA receptor binding; IPI:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISS:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:1902524; P:positive regulation of protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IMP:RGD.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; ISS:UniProtKB.
DR InterPro; IPR004241; Atg8-like.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10969; PTHR10969; 1.
DR Pfam; PF02991; ATG8; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Autophagy; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Golgi apparatus; Lipoprotein; Membrane; Microtubule;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..116
FT /note="Gamma-aminobutyric acid receptor-associated protein"
FT /id="PRO_0000212366"
FT PROPEP 117
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:O95166"
FT /id="PRO_0000423068"
FT REGION 1..22
FT /note="Interaction with beta-tubulin"
FT /evidence="ECO:0000269|PubMed:10899939"
FT REGION 36..117
FT /note="Interaction with GPHN"
FT /evidence="ECO:0000269|PubMed:10900017"
FT REGION 36..68
FT /note="Interaction with GABRG2"
FT /evidence="ECO:0000250|UniProtKB:O95166"
FT SITE 116..117
FT /note="Cleavage; by ATG4B"
FT /evidence="ECO:0000250|UniProtKB:O95166"
FT LIPID 116
FT /note="Phosphatidylethanolamine amidated glycine;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:O95166"
FT LIPID 116
FT /note="Phosphatidylserine amidated glycine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O95166"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:1KJT"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:1KJT"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:1KJT"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1KJT"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:1KJT"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1KJT"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:1KJT"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:1KJT"
SQ SEQUENCE 117 AA; 13918 MW; BC0B84B8A51C1E32 CRC64;
MKFVYKEEHP FEKRRSEGEK IRKKYPDRVP VIVEKAPKAR IGDLDKKKYL VPSDLTVGQF
YFLIRKRIHL RAEDALFFFV NNVIPPTSAT MGQLYQEHHE EDFFLYIAYS DESVYGL
