ID   GBRL3_HUMAN             Reviewed;         117 AA.
AC   Q9BY60;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 3;
DE   AltName: Full=GABA(A) receptor-associated protein-like 3;
DE   Flags: Precursor;
GN   Name=GABARAPL3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
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).
CC   -!- FUNCTION: Ubiquitin-like modifier involved in autophagosome formation.
CC       Whereas LC3s are involved in elongation of the phagophore membrane, the
CC       GABARAP/GATE-16 subfamily is essential for a later stage in
CC       autophagosome maturation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with GABRG2 and beta-tubulin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC       Cytoplasmic vesicle, autophagosome membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at very high levels in the
CC       brain, heart, peripheral blood leukocytes, liver, kidney, placenta and
CC       skeletal muscle. Expressed at very low levels in thymus and small
CC       intestine. {ECO:0000269|PubMed:11414770}.
CC   -!- PTM: The precursor molecule is cleaved by ATG4B to form the cytosolic
CC       form, GABARAPL3-I. This is activated by APG7L/ATG7, transferred to ATG3
CC       and conjugated to phospholipid to form the membrane-bound form,
CC       GABARAPL3-II. ATG4B also mediates the delipidation required for
CC       GABARAPL1 recycling when autophagosomes fuse with lysosomes (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR   EMBL; AF180519; AAK16237.1; -; mRNA.
DR   AlphaFoldDB; Q9BY60; -.
DR   SMR; Q9BY60; -.
DR   BioMuta; HGNC:4069; -.
DR   DMDM; 44887972; -.
DR   MassIVE; Q9BY60; -.
DR   PaxDb; Q9BY60; -.
DR   PeptideAtlas; Q9BY60; -.
DR   PRIDE; Q9BY60; -.
DR   GeneCards; GABARAPL3; -.
DR   HGNC; HGNC:4069; GABARAPL3.
DR   neXtProt; NX_Q9BY60; -.
DR   InParanoid; Q9BY60; -.
DR   PhylomeDB; Q9BY60; -.
DR   TreeFam; TF314556; -.
DR   PathwayCommons; Q9BY60; -.
DR   Reactome; R-HSA-1632852; Macroautophagy.
DR   Pharos; Q9BY60; Tdark.
DR   PRO; PR:Q9BY60; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q9BY60; protein.
DR   GO; GO:0005776; C:autophagosome; IBA:GO_Central.
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; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Lipoprotein;
KW   Membrane; Microtubule; Reference proteome.
FT   CHAIN           1..116
FT                   /note="Gamma-aminobutyric acid receptor-associated protein-
FT                   like 3"
FT                   /id="PRO_0000212376"
FT   PROPEP          117
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000423073"
FT   REGION          1..22
FT                   /note="Interaction with beta-tubulin"
FT                   /evidence="ECO:0000250"
FT   REGION          36..68
FT                   /note="Interaction with GABRG2"
FT                   /evidence="ECO:0000250"
FT   SITE            116..117
FT                   /note="Cleavage; by ATG4B"
FT                   /evidence="ECO:0000250"
FT   LIPID           116
FT                   /note="Phosphatidylethanolamine amidated glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P60520"
SQ   SEQUENCE   117 AA;  13976 MW;  A4AA4C7C958AF32D CRC64;
     MKFQYKEVHP FEYRKKEGEK IRKKYPDRVP LIVEKAPKAR VPDLDRRKYL VPSDLTDGQF
     YLLIRKRIHL RPEDALFFFV NNTIPPTSAT MGQLYEDSHE EDDFLYVAYS NESVYGK