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 27-MAR-2024, entry version 142. DE RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 2 {ECO:0000305}; 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 {ECO:0000312|RGD:620510}; 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. Interacts with GOSR1. Interacts with CC KBTBD6 and KBTBD7; the interaction is direct. Interacts with CC reticulophagy regulators RETREG1, RETREG2 and RETREG3. Interacts with CC IRGM (By similarity). Interacts with DNM2 (By similarity). CC {ECO:0000250|UniProtKB:P60519, 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}. 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; 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; 10116-ENSRNOP00000040067; -. DR Ensembl; ENSRNOT00000047078.5; ENSRNOP00000092094.1; ENSRNOG00000051416.2. DR Ensembl; ENSRNOT00000048998.4; ENSRNOP00000040067.3; ENSRNOG00000019425.6. DR Ensembl; ENSRNOT00055032105; ENSRNOP00055025963; ENSRNOG00055018836. DR Ensembl; ENSRNOT00060021666; ENSRNOP00060017133; ENSRNOG00060012752. DR Ensembl; ENSRNOT00065019096; ENSRNOP00065014606; ENSRNOG00065011750. DR GeneID; 64670; -. DR KEGG; rno:100359937; -. DR KEGG; rno:64670; -. DR UCSC; RGD:620510; rat. DR AGR; RGD:2323108; -. DR AGR; RGD:620510; -. DR CTD; 11345; -. DR CTD; 23766; -. 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; 652940at2759; -. 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 cell types or tissues. 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:0008429; F:phosphatidylethanolamine 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: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 CDD; cd17163; Ubl_ATG8_GABARAPL2; 1. DR InterPro; IPR004241; Atg8-like. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR10969:SF4; GAMMA-AMINOBUTYRIC ACID RECEPTOR-ASSOCIATED PROTEIN-LIKE 2; 1. DR PANTHER; PTHR10969; MICROTUBULE-ASSOCIATED PROTEINS 1A/1B LIGHT CHAIN 3-RELATED; 1. DR Pfam; PF02991; ATG8; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR Genevisible; P60522; RN. 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 //