GBRL2_RAT
ID GBRL2_RAT Reviewed; 117 AA.
AC P60522; O08765; Q9DCP8; Q9UQF7;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 2;
DE AltName: Full=GABA(A) receptor-associated protein-like 2;
DE AltName: Full=Ganglioside expression factor 2;
DE Short=GEF-2;
DE AltName: Full=Golgi-associated ATPase enhancer of 16 kDa;
DE Short=GATE-16;
DE Flags: Precursor;
GN Name=Gabarapl2; Synonyms=Gef2;
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].
RC STRAIN=Wistar; TISSUE=Brain;
RA Ogura K.;
RT "Expression cloning of a cDNA encoding a ganglioside expression factor-2
RT (GEF-2).";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, and 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).
CC -!- FUNCTION: Ubiquitin-like modifier involved in intra-Golgi traffic.
CC Modulates intra-Golgi transport through coupling between NSF activity
CC and SNAREs activation. It first stimulates the ATPase activity of NSF
CC which in turn stimulates the association with GOSR1 (By similarity).
CC Involved in autophagy. Plays a role in mitophagy which contributes to
CC regulate mitochondrial quantity and quality by eliminating the
CC mitochondria to a basal level to fulfill cellular energy requirements
CC and preventing excess ROS production. Whereas 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 (By
CC similarity). {ECO:0000250|UniProtKB:P60519,
CC ECO:0000250|UniProtKB:P60520}.
CC -!- SUBUNIT: Monomer. Interacts with ATG3, ATG7, ATG13 and ULK1. Interacts
CC with TP53INP1 and TP53INP2. Interacts with TBC1D25. Directly interacts
CC with SQSTM1 and BNIP3. Interacts with TECPR2 and PCM1. Interacts with
CC TBC1D5. Interacts with TRIM5. Interacts with MEFV and TRIM21. Interacts
CC with WDFY3. Interacts with UBA5; promoting recruitment of UBA5 to the
CC endoplasmic reticulum membrane (By similarity). Interacts with GOSR1
CC (By similarity). Interacts with KBTBD6 AND KBTBD7; the interaction is
CC direct (By similarity). {ECO:0000250|UniProtKB:P60519,
CC ECO:0000250|UniProtKB:P60520}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC {ECO:0000250|UniProtKB:P60520}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P60520}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P60519}.
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, GABARAPL2-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, GABARAPL2-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 required for GABARAPL2 recycling
CC when autophagosomes fuse with lysosomes. 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:P60520,
CC ECO:0000250|UniProtKB:P60521}.
CC -!- PTM: Phosphorylation at Ser-87 and Ser-88 by TBK1 prevents interaction
CC with ATG4 (ATG4A, ATG4B, ATG4C or ATG4D). Phosphorylation by TBK1 on
CC autophagosomes prevents their delipidation by ATG4 and premature
CC removal from nascent autophagosomes. {ECO:0000250|UniProtKB:P60520}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR EMBL; AB003515; BAA19975.1; -; mRNA.
DR EMBL; BC058145; AAH58145.1; -; mRNA.
DR EMBL; BC088139; AAH88139.1; -; mRNA.
DR RefSeq; NP_073197.1; NM_022706.2.
DR RefSeq; XP_002729993.3; XM_002729947.5.
DR AlphaFoldDB; P60522; -.
DR SMR; P60522; -.
DR CORUM; P60522; -.
DR STRING; 10116.ENSRNOP00000040067; -.
DR PhosphoSitePlus; P60522; -.
DR jPOST; P60522; -.
DR PaxDb; P60522; -.
DR PRIDE; P60522; -.
DR Ensembl; ENSRNOT00000047078; ENSRNOP00000092094; ENSRNOG00000051416.
DR Ensembl; ENSRNOT00000048998; ENSRNOP00000040067; ENSRNOG00000019425.
DR GeneID; 100359937; -.
DR GeneID; 64670; -.
DR KEGG; rno:100359937; -.
DR KEGG; rno:64670; -.
DR UCSC; RGD:620510; rat.
DR CTD; 11345; -.
DR RGD; 620510; Gabarapl2.
DR eggNOG; KOG1654; Eukaryota.
DR GeneTree; ENSGT00940000155010; -.
DR HOGENOM; CLU_119276_0_1_1; -.
DR InParanoid; P60522; -.
DR OMA; AKMKWMF; -.
DR OrthoDB; 1508198at2759; -.
DR PhylomeDB; P60522; -.
DR TreeFam; TF312964; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR Reactome; R-RNO-8854214; TBC/RABGAPs.
DR PRO; PR:P60522; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000019425; Expressed in cerebellum and 19 other tissues.
DR Genevisible; P60522; RN.
DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; 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:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; ISO:RGD.
DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 Acetylation; Autophagy; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Golgi apparatus; Lipoprotein; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..116
FT /note="Gamma-aminobutyric acid receptor-associated protein-
FT like 2"
FT /id="PRO_0000212375"
FT PROPEP 117
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P60520"
FT /id="PRO_0000423072"
FT SITE 116..117
FT /note="Cleavage; by ATG4"
FT /evidence="ECO:0000250|UniProtKB:P60520"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60520"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60520"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60520"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60520"
FT LIPID 116
FT /note="Phosphatidylethanolamine amidated glycine;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:P60520"
FT LIPID 116
FT /note="Phosphatidylserine amidated glycine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P60520"
SQ SEQUENCE 117 AA; 13667 MW; 17ACB540FD5B975B CRC64;
MKWMFKEDHS LEHRCVESAK IRAKYPDRVP VIVEKVSGSQ IVDIDKRKYL VPSDITVAQF
MWIIRKRIQL PSEKAIFLFV DKTVPQSSLT MGQLYEKEKD EDGFLYVAYS GENTFGF
