ID GBRL2_BOVIN Reviewed; 117 AA.
AC P60519; O08765; Q3ZC59; Q5E9G2; Q9DCP8; Q9UQF7;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 2 {ECO:0000250|UniProtKB:P60520};
DE AltName: Full=GABA(A) receptor-associated protein-like 2;
DE AltName: Full=Ganglioside expression factor 2;
DE Short=GEF-2;
DE AltName: Full=General protein transport factor p16;
DE AltName: Full=Golgi-associated ATPase enhancer of 16 kDa;
DE Short=GATE-16;
DE AltName: Full=MAP1 light chain 3-related protein;
DE Flags: Precursor;
GN Name=GABARAPL2 {ECO:0000250|UniProtKB:P60520}; Synonyms=GEF2;
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 [MRNA], PROTEIN SEQUENCE OF 24-47; 55-65; 69-74 AND
RP 107-116, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH NSF AND GOSR1.
RC TISSUE=Brain;
RX PubMed=10747018; DOI=10.1093/emboj/19.7.1494;
RA Sagiv Y., Legesse-Miller A., Porat A., Elazar Z.;
RT "GATE-16, a membrane transport modulator, interacts with NSF and the Golgi
RT v-SNARE GOS-28.";
RL EMBO J. 19:1494-1504(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=12438634; DOI=10.1128/jvi.76.24.13069-13076.2002;
RA Becher P., Thiel H.-J., Collins M., Brownlie J., Orlich M.;
RT "Cellular sequences in pestivirus genomes encoding gamma-aminobutyric acid
RT (A) receptor-associated protein and Golgi-associated ATPase enhancer of 16
RT kilodaltons.";
RL J. Virol. 76:13069-13076(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND SUBUNIT.
RX PubMed=10856287; DOI=10.1074/jbc.c000307200;
RA Paz Y., Elazar Z., Fass D.;
RT "Structure of GATE-16, membrane transport modulator and mammalian ortholog
RT of autophagocytosis factor Aut7p.";
RL J. Biol. Chem. 275:25445-25450(2000).
CC -!- FUNCTION: Ubiquitin-like modifier involved in intra-Golgi traffic
CC (PubMed:10747018). Modulates intra-Golgi transport through coupling
CC between NSF activity and SNAREs activation (PubMed:10747018). It first
CC stimulates the ATPase activity of NSF which in turn stimulates the
CC association with GOSR1 (PubMed:10747018). Involved in autophagy (By
CC similarity). Plays a role in mitophagy which contributes to regulate
CC mitochondrial quantity and quality by eliminating the mitochondria to a
CC basal level to fulfill cellular energy requirements and preventing
CC excess ROS production (By similarity). 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:P60520,
CC ECO:0000269|PubMed:10747018}.
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 (PubMed:10747018). Interacts with KBTBD6 and KBTBD7; the interaction is
CC direct (By similarity). Interacts with reticulophagy regulators
CC RETREG1, RETREG2 and RETREG3 (By similarity). Interacts with IRGM (By
CC similarity). Interacts with DNM2 (By similarity).
CC {ECO:0000250|UniProtKB:P60520, ECO:0000269|PubMed:10747018}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC {ECO:0000250|UniProtKB:P60520}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P60520}. Golgi apparatus
CC {ECO:0000269|PubMed:10747018}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the brain,
CC heart, prostate, ovary, spleen and skeletal muscle. Expressed at very
CC low levels in lung, thymus and small intestine.
CC {ECO:0000269|PubMed:10747018}.
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; AF020262; AAD20720.1; -; mRNA.
DR EMBL; AY117147; AAM77036.1; -; mRNA.
DR EMBL; BT020958; AAX08975.1; -; mRNA.
DR EMBL; BC102902; AAI02903.2; -; mRNA.
DR RefSeq; NP_777100.1; NM_174675.2.
DR PDB; 1EO6; X-ray; 1.80 A; A/B=1-117.
DR PDBsum; 1EO6; -.
DR AlphaFoldDB; P60519; -.
DR SMR; P60519; -.
DR STRING; 9913.ENSBTAP00000008607; -.
DR PaxDb; 9913-ENSBTAP00000008607; -.
DR Ensembl; ENSBTAT00000008607.4; ENSBTAP00000008607.4; ENSBTAG00000006550.4.
DR GeneID; 282531; -.
DR KEGG; bta:282531; -.
DR CTD; 11345; -.
DR VEuPathDB; HostDB:ENSBTAG00000006550; -.
DR VGNC; VGNC:29186; GABARAPL2.
DR eggNOG; KOG1654; Eukaryota.
DR GeneTree; ENSGT00940000155010; -.
DR InParanoid; P60519; -.
DR OMA; AKMKWMF; -.
DR OrthoDB; 652940at2759; -.
DR Reactome; R-BTA-1632852; Macroautophagy.
DR Reactome; R-BTA-8854214; TBC/RABGAPs.
DR EvolutionaryTrace; P60519; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000006550; Expressed in midbrain and 102 other cell types or tissues.
DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IDA:UniProtKB.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IEA:Ensembl.
DR GO; GO:0000149; F:SNARE binding; IDA:UniProtKB.
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:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:UniProtKB.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Autophagy; Cytoplasmic vesicle;
KW Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus;
KW 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_0000212372"
FT PROPEP 117
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P60520"
FT /id="PRO_0000423069"
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"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:1EO6"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:1EO6"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:1EO6"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1EO6"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:1EO6"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:1EO6"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:1EO6"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:1EO6"
SQ SEQUENCE 117 AA; 13667 MW; 17ACB540FD5B975B CRC64;
MKWMFKEDHS LEHRCVESAK IRAKYPDRVP VIVEKVSGSQ IVDIDKRKYL VPSDITVAQF
MWIIRKRIQL PSEKAIFLFV DKTVPQSSLT MGQLYEKEKD EDGFLYVAYS GENTFGF
//
