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GBRL2_BOVIN
ID   GBRL2_BOVIN             Reviewed;         117 AA.
AC   P60519; O08765; Q3ZC59; Q5E9G2; Q9DCP8; Q9UQF7;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 2;
DE   AltName: Full=GABA(A) receptor-associated protein-like 2;
DE   AltName: Full=Ganglioside expression factor 2;
DE            Short=GEF-2;
DE   AltName: Full=General protein transport factor p16;
DE   AltName: Full=Golgi-associated ATPase enhancer of 16 kDa;
DE            Short=GATE-16;
DE   AltName: Full=MAP1 light chain 3-related protein;
DE   Flags: Precursor;
GN   Name=GABARAPL2; Synonyms=GEF2;
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 [MRNA], PROTEIN SEQUENCE OF 24-47; 55-65; 69-74 AND
RP   107-116, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   INTERACTION WITH NSF AND GOSR1.
RC   TISSUE=Brain;
RX   PubMed=10747018; DOI=10.1093/emboj/19.7.1494;
RA   Sagiv Y., Legesse-Miller A., Porat A., Elazar Z.;
RT   "GATE-16, a membrane transport modulator, interacts with NSF and the Golgi
RT   v-SNARE GOS-28.";
RL   EMBO J. 19:1494-1504(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND SUBUNIT.
RX   PubMed=10856287; DOI=10.1074/jbc.c000307200;
RA   Paz Y., Elazar Z., Fass D.;
RT   "Structure of GATE-16, membrane transport modulator and mammalian ortholog
RT   of autophagocytosis factor Aut7p.";
RL   J. Biol. Chem. 275:25445-25450(2000).
CC   -!- FUNCTION: Ubiquitin-like modifier involved in intra-Golgi traffic
CC       (PubMed:10747018). Modulates intra-Golgi transport through coupling
CC       between NSF activity and SNAREs activation (PubMed:10747018). It first
CC       stimulates the ATPase activity of NSF which in turn stimulates the
CC       association with GOSR1 (PubMed:10747018). Involved in autophagy (By
CC       similarity). Plays a role in mitophagy which contributes to regulate
CC       mitochondrial quantity and quality by eliminating the mitochondria to a
CC       basal level to fulfill cellular energy requirements and preventing
CC       excess ROS production (By similarity). Whereas 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 (By
CC       similarity). {ECO:0000250|UniProtKB:P60520,
CC       ECO:0000269|PubMed:10747018}.
CC   -!- SUBUNIT: Monomer. Interacts with ATG3, ATG7, ATG13 and ULK1. Interacts
CC       with TP53INP1 and TP53INP2. Interacts with TBC1D25. Directly interacts
CC       with SQSTM1 and BNIP3. Interacts with TECPR2 and PCM1. Interacts with
CC       TBC1D5. Interacts with TRIM5. Interacts with MEFV and TRIM21. Interacts
CC       with WDFY3. Interacts with UBA5; promoting recruitment of UBA5 to the
CC       endoplasmic reticulum membrane (By similarity). Interacts with GOSR1
CC       (PubMed:10747018). Interacts with KBTBD6 AND KBTBD7; the interaction is
CC       direct (By similarity). {ECO:0000250|UniProtKB:P60520,
CC       ECO:0000269|PubMed:10747018}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC       {ECO:0000250|UniProtKB:P60520}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P60520}. Golgi apparatus
CC       {ECO:0000269|PubMed:10747018}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the brain,
CC       heart, prostate, ovary, spleen and skeletal muscle. Expressed at very
CC       low levels in lung, thymus and small intestine.
CC       {ECO:0000269|PubMed:10747018}.
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, GABARAPL2-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, GABARAPL2-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 GABARAPL2 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:P60520,
CC       ECO:0000250|UniProtKB:P60521}.
CC   -!- PTM: Phosphorylation at Ser-87 and Ser-88 by TBK1 prevents interaction
CC       with ATG4 (ATG4A, ATG4B, ATG4C or ATG4D). Phosphorylation by TBK1 on
CC       autophagosomes prevents their delipidation by ATG4 and premature
CC       removal from nascent autophagosomes. {ECO:0000250|UniProtKB:P60520}.
CC   -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR   EMBL; AF020262; AAD20720.1; -; mRNA.
DR   EMBL; AY117147; AAM77036.1; -; mRNA.
DR   EMBL; BT020958; AAX08975.1; -; mRNA.
DR   EMBL; BC102902; AAI02903.2; -; mRNA.
DR   RefSeq; NP_777100.1; NM_174675.2.
DR   PDB; 1EO6; X-ray; 1.80 A; A/B=1-117.
DR   PDBsum; 1EO6; -.
DR   AlphaFoldDB; P60519; -.
DR   SMR; P60519; -.
DR   STRING; 9913.ENSBTAP00000008607; -.
DR   PaxDb; P60519; -.
DR   PRIDE; P60519; -.
DR   Ensembl; ENSBTAT00000008607; ENSBTAP00000008607; ENSBTAG00000006550.
DR   GeneID; 282531; -.
DR   KEGG; bta:282531; -.
DR   CTD; 11345; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006550; -.
DR   VGNC; VGNC:29186; GABARAPL2.
DR   eggNOG; KOG1654; Eukaryota.
DR   GeneTree; ENSGT00940000155010; -.
DR   InParanoid; P60519; -.
DR   OMA; AKMKWMF; -.
DR   OrthoDB; 1508198at2759; -.
DR   EvolutionaryTrace; P60519; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000006550; Expressed in midbrain and 102 other tissues.
DR   GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0051117; F:ATPase binding; IDA:UniProtKB.
DR   GO; GO:0000149; F:SNARE binding; IDA:UniProtKB.
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:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB.
DR   GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR   GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IEA:Ensembl.
DR   GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:UniProtKB.
DR   GO; GO:0070972; P:protein localization to endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; 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   1: Evidence at protein level;
KW   3D-structure; Acetylation; Autophagy; Cytoplasmic vesicle;
KW   Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus;
KW   Lipoprotein; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..116
FT                   /note="Gamma-aminobutyric acid receptor-associated protein-
FT                   like 2"
FT                   /id="PRO_0000212372"
FT   PROPEP          117
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P60520"
FT                   /id="PRO_0000423069"
FT   SITE            116..117
FT                   /note="Cleavage; by ATG4"
FT                   /evidence="ECO:0000250|UniProtKB:P60520"
FT   MOD_RES         24
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P60520"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60520"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60520"
FT   MOD_RES         88
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60520"
FT   LIPID           116
FT                   /note="Phosphatidylethanolamine amidated glycine;
FT                   alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P60520"
FT   LIPID           116
FT                   /note="Phosphatidylserine amidated glycine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P60520"
FT   HELIX           4..8
FT                   /evidence="ECO:0007829|PDB:1EO6"
FT   HELIX           11..24
FT                   /evidence="ECO:0007829|PDB:1EO6"
FT   STRAND          28..35
FT                   /evidence="ECO:0007829|PDB:1EO6"
FT   STRAND          48..52
FT                   /evidence="ECO:0007829|PDB:1EO6"
FT   HELIX           57..68
FT                   /evidence="ECO:0007829|PDB:1EO6"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:1EO6"
FT   HELIX           91..98
FT                   /evidence="ECO:0007829|PDB:1EO6"
FT   STRAND          105..110
FT                   /evidence="ECO:0007829|PDB:1EO6"
SQ   SEQUENCE   117 AA;  13667 MW;  17ACB540FD5B975B CRC64;
     MKWMFKEDHS LEHRCVESAK IRAKYPDRVP VIVEKVSGSQ IVDIDKRKYL VPSDITVAQF
     MWIIRKRIQL PSEKAIFLFV DKTVPQSSLT MGQLYEKEKD EDGFLYVAYS GENTFGF
 
 
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