GBRL1_RAT
ID GBRL1_RAT Reviewed; 117 AA.
AC Q0VGK0;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 1;
DE AltName: Full=GABA(A) receptor-associated protein-like 1;
DE AltName: Full=Glandular epithelial cell protein 1;
DE Short=GEC-1;
DE Flags: Precursor;
GN Name=Gabarapl1; Synonyms=Gec1;
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 [LARGE SCALE MRNA].
RC TISSUE=Liver;
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).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16650615; DOI=10.1016/j.neuroscience.2006.03.013;
RA Wang Y., Dun S.L., Huang P., Chen C., Chen Y., Unterwald E.M., Dun N.J.,
RA Van Bockstaele E.J., Liu-Chen L.-Y.;
RT "Distribution and ultrastructural localization of GEC1 in the rat CNS.";
RL Neuroscience 140:1265-1276(2006).
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:0000269|PubMed:16650615}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:16650615}. Golgi apparatus
CC {ECO:0000269|PubMed:16650615}.
CC -!- TISSUE SPECIFICITY: High expression in liver and brain, lower in lung
CC and heart and very low in kidney and skeletal muscle (at protein
CC level). Present in all brain regions and spinal cord (at protein
CC level). {ECO:0000269|PubMed:16650615}.
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; BC105627; AAI05628.1; -; mRNA.
DR RefSeq; NP_001037759.1; NM_001044294.1.
DR AlphaFoldDB; Q0VGK0; -.
DR BMRB; Q0VGK0; -.
DR SMR; Q0VGK0; -.
DR BioGRID; 603984; 2.
DR IntAct; Q0VGK0; 1.
DR STRING; 10116.ENSRNOP00000011942; -.
DR PhosphoSitePlus; Q0VGK0; -.
DR PaxDb; Q0VGK0; -.
DR PRIDE; Q0VGK0; -.
DR GeneID; 689161; -.
DR KEGG; rno:689161; -.
DR UCSC; RGD:1596143; rat.
DR CTD; 23710; -.
DR RGD; 1596143; Gabarapl1.
DR VEuPathDB; HostDB:ENSRNOG00000053362; -.
DR eggNOG; KOG1654; Eukaryota.
DR HOGENOM; CLU_119276_0_3_1; -.
DR InParanoid; Q0VGK0; -.
DR OMA; AHDQDIS; -.
DR OrthoDB; 1508198at2759; -.
DR PhylomeDB; Q0VGK0; -.
DR TreeFam; TF314556; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR PRO; PR:Q0VGK0; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000053362; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q0VGK0; RN.
DR GO; GO:0005776; C:autophagosome; ISO:RGD.
DR GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032839; C:dendrite cytoplasm; IDA:RGD.
DR GO; GO:0032590; C:dendrite membrane; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0050811; F:GABA receptor binding; IBA:GO_Central.
DR GO; GO:0030957; F:Tat protein 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: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 1: Evidence at protein level;
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_0000342410"
FT PROPEP 117
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9H0R8"
FT /id="PRO_0000420211"
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"
SQ SEQUENCE 117 AA; 14044 MW; 7F56E345255F564B CRC64;
MKFQYKEDHP FEYRKKEGEK IRKKYPDRVP VIVEKAPKAR VPDLDKRKYL VPSDLTVGQF
YFLIRKRIHL RPEDALFFFV NNTIPPTSAT MGQLYEDNHE EDYFLYVAYS DESVYGK
