GBRL1_MOUSE
ID GBRL1_MOUSE Reviewed; 117 AA.
AC Q8R3R8; Q3TG14; Q3TJB9; Q3TXZ5; Q9JJ97;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 145.
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=Apg8l, Atg8l, Gec1; ORFNames=MNCb-0091;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11414770; DOI=10.1006/geno.2001.6555;
RA Xin Y., Yu L., Chen Z., Zheng L., Fu Q., Jiang J., Zhang P., Gong R.,
RA Zhao S.;
RT "Cloning, expression patterns, and chromosome localization of three human
RT and two mouse homologues of GABA(A) receptor-associated protein.";
RL Genomics 74:408-413(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Amnion, Cecum, Embryo, Placenta, Testis, and Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [5]
RP CLEAVAGE BY ATG4B, AND SUBCELLULAR LOCATION.
RX PubMed=14530254; DOI=10.1074/jbc.m308762200;
RA Hemelaar J., Lelyveld V.S., Kessler B.M., Ploegh H.L.;
RT "A single protease, Apg4B, is specific for the autophagy-related ubiquitin-
RT like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L.";
RL J. Biol. Chem. 278:51841-51850(2003).
RN [6]
RP CLEAVAGE BY ATG4B, AND INTERACTION WITH ATG3 AND ATG7.
RX PubMed=16704426; DOI=10.1111/j.1742-4658.2006.05260.x;
RA Tanida I., Sou Y.S., Minematsu-Ikeguchi N., Ueno T., Kominami E.;
RT "Atg8L/Apg8L is the fourth mammalian modifier of mammalian Atg8 conjugation
RT mediated by human Atg4B, Atg7 and Atg3.";
RL FEBS J. 273:2553-2562(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP LIPIDATION, AND DELIPIDATION.
RX PubMed=33795848; DOI=10.1038/s41418-021-00776-1;
RA Tamargo-Gomez I., Martinez-Garcia G.G., Suarez M.F., Rey V., Fueyo A.,
RA Codina-Martinez H., Bretones G., Caravia X.M., Morel E., Dupont N.,
RA Cabo R., Tomas-Zapico C., Souquere S., Pierron G., Codogno P.,
RA Lopez-Otin C., Fernandez A.F., Marino G.;
RT "ATG4D is the main ATG8 delipidating enzyme in mammalian cells and protects
RT against cerebellar neurodegeneration.";
RL Cell Death Differ. 28:2651-2672(2021).
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 (By similarity).
CC Interacts with TP53INP1 and TP53INP2 (By similarity). Directly
CC interacts with SQSTM1 (By similarity). Interacts with ATG3, ATG7 and
CC MAP15 (PubMed:16704426). Interacts with TECPR2 (By similarity).
CC Interacts with TBC1D5 (By similarity). Interacts with MAPK15 (By
CC similarity). Interacts with TRIM5 (By similarity). Interacts with MEFV
CC and TRIM21 (By similarity). Interacts with WDFY3 (By similarity).
CC Interacts with the reticulophagy receptor TEX264 (By similarity).
CC Interacts with UBA5 (By similarity). Interacts with KBTBD6 AND KBTBD7;
CC the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:Q9H0R8, ECO:0000269|PubMed:16704426}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC {ECO:0000269|PubMed:14530254}. 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 -!- TISSUE SPECIFICITY: Expressed in testis and heart at high levels.
CC {ECO:0000269|PubMed:11414770}.
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 (PubMed:14530254, PubMed:16704426). The processed
CC form is then activated by APG7L/ATG7, transferred to ATG3 and
CC conjugated to phosphatidylethanolamine (PE) phospholipid to form the
CC membrane-bound form, GABARAPL1-II (By similarity). During non-canonical
CC autophagy, the processed form is conjugated to phosphatidylserine (PS)
CC phospholipid (By similarity). ATG4 proteins also mediate the
CC delipidation of PE-conjugated forms required for GABARAPL1 recycling
CC when autophagosomes fuse with lysosomes (PubMed:33795848). In addition,
CC ATG4B and ATG4D mediate delipidation of ATG8 proteins conjugated to PS
CC during non-canonical autophagy (By similarity). ATG4B constitutes the
CC major protein for proteolytic activation (By similarity). ATG4D is the
CC main enzyme for delipidation activity (PubMed:33795848).
CC {ECO:0000250|UniProtKB:Q9H0R8, ECO:0000269|PubMed:14530254,
CC ECO:0000269|PubMed:16704426, ECO:0000269|PubMed:33795848}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE39576.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF180518; AAK16236.1; -; mRNA.
DR EMBL; AB041648; BAA95100.1; -; mRNA.
DR EMBL; AK011975; BAB27950.1; -; mRNA.
DR EMBL; AK014083; BAB29146.1; -; mRNA.
DR EMBL; AK015049; BAB29690.1; -; mRNA.
DR EMBL; AK018687; BAB31345.1; -; mRNA.
DR EMBL; AK159015; BAE34769.1; -; mRNA.
DR EMBL; AK167500; BAE39576.1; ALT_INIT; mRNA.
DR EMBL; AK168921; BAE40734.1; -; mRNA.
DR EMBL; BC004602; AAH04602.1; -; mRNA.
DR EMBL; BC024706; AAH24706.1; -; mRNA.
DR CCDS; CCDS51923.1; -.
DR RefSeq; NP_065615.1; NM_020590.4.
DR PDB; 5YIP; X-ray; 1.85 A; A=1-117.
DR PDB; 7CDB; X-ray; 1.95 A; A/B=1-117.
DR PDBsum; 5YIP; -.
DR PDBsum; 7CDB; -.
DR AlphaFoldDB; Q8R3R8; -.
DR SMR; Q8R3R8; -.
DR BioGRID; 208293; 26.
DR IntAct; Q8R3R8; 1.
DR MINT; Q8R3R8; -.
DR STRING; 10090.ENSMUSP00000032264; -.
DR iPTMnet; Q8R3R8; -.
DR PhosphoSitePlus; Q8R3R8; -.
DR EPD; Q8R3R8; -.
DR MaxQB; Q8R3R8; -.
DR PaxDb; Q8R3R8; -.
DR PeptideAtlas; Q8R3R8; -.
DR PRIDE; Q8R3R8; -.
DR ProteomicsDB; 266783; -.
DR Antibodypedia; 42119; 437 antibodies from 30 providers.
DR DNASU; 57436; -.
DR Ensembl; ENSMUST00000032264; ENSMUSP00000032264; ENSMUSG00000030161.
DR Ensembl; ENSMUST00000204956; ENSMUSP00000145175; ENSMUSG00000030161.
DR GeneID; 57436; -.
DR KEGG; mmu:57436; -.
DR UCSC; uc009efz.1; mouse.
DR CTD; 23710; -.
DR MGI; MGI:1914980; Gabarapl1.
DR VEuPathDB; HostDB:ENSMUSG00000030161; -.
DR eggNOG; KOG1654; Eukaryota.
DR GeneTree; ENSGT00940000156876; -.
DR HOGENOM; CLU_119276_0_3_1; -.
DR InParanoid; Q8R3R8; -.
DR OMA; AHDQDIS; -.
DR OrthoDB; 1508198at2759; -.
DR PhylomeDB; Q8R3R8; -.
DR TreeFam; TF314556; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR BioGRID-ORCS; 57436; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Gabarapl1; mouse.
DR PRO; PR:Q8R3R8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8R3R8; protein.
DR Bgee; ENSMUSG00000030161; Expressed in hypothalamus and 87 other tissues.
DR ExpressionAtlas; Q8R3R8; baseline and differential.
DR Genevisible; Q8R3R8; MM.
DR GO; GO:0005776; C:autophagosome; ISO:MGI.
DR GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
DR GO; GO:0044297; C:cell body; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0032590; C:dendrite membrane; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISA:MGI.
DR GO; GO:0050811; F:GABA receptor binding; IBA:GO_Central.
DR GO; GO:0043495; F:protein-membrane adaptor activity; ISO:MGI.
DR GO; GO:0030957; F:Tat protein binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
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:0061723; P:glycophagy; IMP:MGI.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0061753; P:substrate localization to autophagosome; ISO:MGI.
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 3D-structure; 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_0000212370"
FT PROPEP 117
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:16704426"
FT /id="PRO_0000420209"
FT SITE 116..117
FT /note="Cleavage; by ATG4B"
FT /evidence="ECO:0000269|PubMed:16704426"
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 6
FT /note="K -> E (in Ref. 3; BAE34769)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="Y -> H (in Ref. 4; AAH24706)"
FT /evidence="ECO:0000305"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:5YIP"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:5YIP"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:5YIP"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:5YIP"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:5YIP"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:5YIP"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:5YIP"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:5YIP"
SQ SEQUENCE 117 AA; 14044 MW; 7F56E345255F564B CRC64;
MKFQYKEDHP FEYRKKEGEK IRKKYPDRVP VIVEKAPKAR VPDLDKRKYL VPSDLTVGQF
YFLIRKRIHL RPEDALFFFV NNTIPPTSAT MGQLYEDNHE EDYFLYVAYS DESVYGK
