GBRAP_BOVIN
ID GBRAP_BOVIN Reviewed; 117 AA.
AC Q9GJW7; Q3SZ82;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Gamma-aminobutyric acid receptor-associated protein;
DE AltName: Full=GABA(A) receptor-associated protein;
DE Flags: Precursor;
GN Name=GABARAP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 78-117.
RC TISSUE=Mammary gland;
RA Pallesen L.T., Berglund L., Petersen T.E., Rasmussen J.T.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin-like modifier that plays a role in intracellular
CC transport of GABA(A) receptors and its interaction with the
CC cytoskeleton. Involved in autophagy: while LC3s are involved in
CC elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is
CC essential for a later stage in autophagosome maturation. Through its
CC interaction with the reticulophagy receptor TEX264, participates in the
CC remodeling of subdomains of the endoplasmic reticulum into
CC autophagosomes upon nutrient stress, which then fuse with lysosomes for
CC endoplasmic reticulum turnover. Also required for the local activation
CC of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex, regulating
CC ubiquitination and degradation of TIAM1, a guanyl-nucleotide exchange
CC factor (GEF) that activates RAC1 and downstream signal transduction.
CC Thereby, regulates different biological processes including the
CC organization of the cytoskeleton, cell migration and proliferation.
CC Involved in apoptosis. {ECO:0000250|UniProtKB:O95166}.
CC -!- SUBUNIT: Interacts with GPHN and NSF (By similarity). Interacts with
CC ATG3, ATG7 and ATG13. Interacts with alpha-tubulin (By similarity).
CC Interacts with beta-tubulin (By similarity). Interacts with GABRG2.
CC Interacts with RB1CC1. Interacts with ULK1. Interacts with CALR.
CC Interacts with DDX47. Interacts with TP53INP1 and TP53INP2. Interacts
CC with TBC1D5 (By similarity). Interacts with TBC1D25 (By similarity).
CC Directly interacts with SQSTM1. Interacts with MAPK15. Interacts with
CC TECPR2. Interacts with PCM1. Interacts with TRIM5 and TRIM21. Interacts
CC with MEFV (By similarity). Interacts with KIF21B (By similarity).
CC Interacts with WDFY3; this interaction is required for WDFY3
CC recruitment to MAP1LC3B-positive p62/SQSTM1 bodies. Interacts with
CC FLCN; interaction regulates autophagy (By similarity). Interacts with
CC UBA5 (By similarity). Interacts with KBTBD6 and KBTBD7; the interaction
CC is direct and required for the ubiquitination of TIAM1 (By similarity).
CC {ECO:0000250|UniProtKB:O95166, ECO:0000250|UniProtKB:P60517}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000250|UniProtKB:P60517}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P60517}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P60517}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000250|UniProtKB:O95166}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:P60517}. Note=Largely associated with
CC intracellular membrane structures including the Golgi apparatus and
CC postsynaptic cisternae. Colocalizes with microtubules (By similarity).
CC Localizes also to discrete punctae along the ciliary axoneme (By
CC similarity). {ECO:0000250|UniProtKB:P60517,
CC ECO:0000250|UniProtKB:Q9DCD6}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC103060; AAI03061.1; -; mRNA.
DR EMBL; AJ297742; CAC12804.1; -; mRNA.
DR RefSeq; NP_001029220.1; NM_001034048.1.
DR AlphaFoldDB; Q9GJW7; -.
DR BMRB; Q9GJW7; -.
DR SMR; Q9GJW7; -.
DR STRING; 9913.ENSBTAP00000019814; -.
DR PaxDb; Q9GJW7; -.
DR Ensembl; ENSBTAT00000019814; ENSBTAP00000019814; ENSBTAG00000014883.
DR GeneID; 327715; -.
DR KEGG; bta:327715; -.
DR CTD; 11337; -.
DR VEuPathDB; HostDB:ENSBTAG00000014883; -.
DR VGNC; VGNC:29185; GABARAP.
DR eggNOG; KOG1654; Eukaryota.
DR GeneTree; ENSGT00940000157496; -.
DR HOGENOM; CLU_119276_0_0_1; -.
DR InParanoid; Q9GJW7; -.
DR OMA; AVYQEHK; -.
DR OrthoDB; 1508198at2759; -.
DR TreeFam; TF314556; -.
DR Reactome; R-BTA-1632852; Macroautophagy.
DR Reactome; R-BTA-8854214; TBC/RABGAPs.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000014883; Expressed in pigment epithelium of eye and 105 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
DR GO; GO:0050811; F:GABA receptor binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
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; IEA:Ensembl.
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; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Apoptosis; Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Golgi apparatus; Lipoprotein; Membrane; Microtubule; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..116
FT /note="Gamma-aminobutyric acid receptor-associated protein"
FT /id="PRO_0000212362"
FT PROPEP 117
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:O95166"
FT /id="PRO_0000423064"
FT REGION 1..22
FT /note="Interaction with beta-tubulin"
FT /evidence="ECO:0000250|UniProtKB:O95166"
FT REGION 36..117
FT /note="Interaction with GPHN"
FT /evidence="ECO:0000250|UniProtKB:Q9DCD6"
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"
SQ SEQUENCE 117 AA; 13918 MW; BC0B84B8A51C1E32 CRC64;
MKFVYKEEHP FEKRRSEGEK IRKKYPDRVP VIVEKAPKAR IGDLDKKKYL VPSDLTVGQF
YFLIRKRIHL RAEDALFFFV NNVIPPTSAT MGQLYQEHHE EDFFLYIAYS DESVYGL
