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GBRL1_BOVIN
ID   GBRL1_BOVIN             Reviewed;         117 AA.
AC   Q8HYB6; Q3ZBC6;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 1;
DE   AltName: Full=GABA(A) receptor-associated protein-like 1;
DE   Flags: Precursor;
GN   Name=GABARAPL1;
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 8-117.
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).
CC   -!- FUNCTION: Ubiquitin-like modifier that increases cell-surface
CC       expression of kappa-type opioid receptor through facilitating
CC       anterograde intracellular trafficking of the receptor. Involved in
CC       formation of autophagosomal vacuoles. 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. {ECO:0000250|UniProtKB:Q9H0R8}.
CC   -!- SUBUNIT: Interacts with ATG13, OPRK1, RB1CC1 and ULK1. Interacts with
CC       TP53INP1 and TP53INP2. Directly interacts with SQSTM1. Interacts with
CC       ATG3, ATG7 and MAP15. Interacts with TECPR2. Interacts with TBC1D5.
CC       Interacts with MAPK15. Interacts with TRIM5. Interacts with MEFV and
CC       TRIM21. Interacts with WDFY3. Interacts with the reticulophagy receptor
CC       TEX264. Interacts with UBA5. Interacts with KBTBD6 AND KBTBD7; the
CC       interaction is direct (By similarity). {ECO:0000250|UniProtKB:Q9H0R8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC       {ECO:0000250|UniProtKB:Q9H0R8}. Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:Q9H0R8}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q9H0R8}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q0VGK0}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q0VGK0}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q0VGK0}.
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, GABARAPL1-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, GABARAPL1-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 GABARAPL1 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:Q8R3R8,
CC       ECO:0000250|UniProtKB:Q9H0R8}.
CC   -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR   EMBL; BC103442; AAI03443.1; -; mRNA.
DR   EMBL; AY117146; AAM77035.1; -; mRNA.
DR   RefSeq; NP_001028788.1; NM_001033616.1.
DR   AlphaFoldDB; Q8HYB6; -.
DR   SMR; Q8HYB6; -.
DR   STRING; 9913.ENSBTAP00000047993; -.
DR   PaxDb; Q8HYB6; -.
DR   PRIDE; Q8HYB6; -.
DR   Ensembl; ENSBTAT00000055075; ENSBTAP00000047993; ENSBTAG00000011765.
DR   GeneID; 338472; -.
DR   KEGG; bta:338472; -.
DR   CTD; 23710; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011765; -.
DR   VGNC; VGNC:56201; GABARAPL1.
DR   eggNOG; KOG1654; Eukaryota.
DR   GeneTree; ENSGT00940000156876; -.
DR   HOGENOM; CLU_119276_0_3_1; -.
DR   InParanoid; Q8HYB6; -.
DR   OMA; AHDQDIS; -.
DR   OrthoDB; 1508198at2759; -.
DR   TreeFam; TF314556; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000011765; Expressed in metanephros cortex and 105 other tissues.
DR   ExpressionAtlas; Q8HYB6; baseline and differential.
DR   GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR   GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0050811; F:GABA receptor binding; IBA:GO_Central.
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:0016236; P:macroautophagy; IBA:GO_Central.
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   Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW   Endoplasmic reticulum; Golgi apparatus; Lipoprotein; Membrane; Microtubule;
KW   Reference proteome.
FT   CHAIN           1..116
FT                   /note="Gamma-aminobutyric acid receptor-associated protein-
FT                   like 1"
FT                   /id="PRO_0000212367"
FT   PROPEP          117
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0R8"
FT                   /id="PRO_0000420206"
FT   SITE            116..117
FT                   /note="Cleavage; by ATG4B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0R8"
FT   LIPID           116
FT                   /note="Phosphatidylethanolamine amidated glycine;
FT                   alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0R8"
FT   LIPID           116
FT                   /note="Phosphatidylserine amidated glycine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0R8"
FT   CONFLICT        114
FT                   /note="V -> T (in Ref. 2; AAM77035)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="K -> SA (in Ref. 2; AAM77035)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   117 AA;  14044 MW;  7F56E345255F564B CRC64;
     MKFQYKEDHP FEYRKKEGEK IRKKYPDRVP VIVEKAPKAR VPDLDKRKYL VPSDLTVGQF
     YFLIRKRIHL RPEDALFFFV NNTIPPTSAT MGQLYEDNHE EDYFLYVAYS DESVYGK
 
 
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