ID   GBRL1_XENLA             Reviewed;         117 AA.
AC   Q6GQ27;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney, and Liver;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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.
CC       {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, some atg4
CC       proteins mediate delipidation of ATG8 proteins conjugated to PS during
CC       non-canonical autophagy. {ECO:0000250|UniProtKB:Q9H0R8}.
CC   -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR   EMBL; BC072921; AAH72921.1; -; mRNA.
DR   EMBL; BC082864; AAH82864.1; -; mRNA.
DR   RefSeq; NP_001085553.1; NM_001092084.1.
DR   RefSeq; NP_001088067.1; NM_001094598.1.
DR   AlphaFoldDB; Q6GQ27; -.
DR   BMRB; Q6GQ27; -.
DR   SMR; Q6GQ27; -.
DR   MaxQB; Q6GQ27; -.
DR   DNASU; 443979; -.
DR   GeneID; 443979; -.
DR   GeneID; 494762; -.
DR   KEGG; xla:443979; -.
DR   CTD; 443979; -.
DR   CTD; 494762; -.
DR   Xenbase; XB-GENE-6077975; gabarapl1.L.
DR   Xenbase; XB-GENE-17333322; gabarapl1.S.
DR   OrthoDB; 1508198at2759; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 443979; Expressed in brain and 17 other tissues.
DR   GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
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_0000438280"
FT   PROPEP          117
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000342411"
FT   SITE            116..117
FT                   /note="Cleavage; by ATG4B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0R8"
FT   LIPID           116
FT                   /note="Phosphatidylethanolamine amidated glycine"
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