ATG13_BOVIN
ID ATG13_BOVIN Reviewed; 480 AA.
AC Q08DY8;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Autophagy-related protein 13;
GN Name=ATG13;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Autophagy factor required for autophagosome formation and
CC mitophagy. Target of the TOR kinase signaling pathway that regulates
CC autophagy through the control of the phosphorylation status of ATG13
CC and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through
CC its regulation of ULK1 activity, plays a role in the regulation of the
CC kinase activity of mTORC1 and cell proliferation.
CC {ECO:0000250|UniProtKB:O75143}.
CC -!- SUBUNIT: Part of a complex consisting of ATG13, ULK1 and RB1CC1.
CC Interacts with ATG101. Interacts with ULK1 (via C-terminus). Interacts
CC with ULK2 (via C-terminus). Interacts (via the LIR motif) with GABARAP,
CC GABARAPL, GABARAPL2. Interacts (via the LIR motif) with MAP1LC3A,
CC MAP1LC3B and MAP1LC3C. Interacts with TAB2 and TAB3. Interacts with
CC C9orf72. {ECO:0000250|UniProtKB:O75143}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q91YI1}. Preautophagosomal structure
CC {ECO:0000250|UniProtKB:Q91YI1}. Note=Under starvation conditions, is
CC localized to puncate structures primarily representing the isolation
CC membrane; the isolation membrane sequesters a portion of the cytoplasm
CC resulting in autophagosome formation. {ECO:0000250|UniProtKB:Q91YI1}.
CC -!- DOMAIN: The LIR motif (LC3-interacting region) is required for the
CC interaction with the ATG8 family proteins GABARAP, GABARAPL, GABARAPL2,
CC and MAP1LC3A. {ECO:0000250|UniProtKB:O75143}.
CC -!- PTM: Phosphorylated by ULK1, ULK2 and mTOR. Phosphorylation status
CC depends on nutrient-rich conditions; dephosphorylated during starvation
CC or following treatment with rapamycin. ULK1-mediated phosphorylation of
CC ATG13 at Ser-318 is required for efficient clearance of depolarized
CC mitochondria. {ECO:0000250|UniProtKB:O75143}.
CC -!- SIMILARITY: Belongs to the ATG13 family. Metazoan subfamily.
CC {ECO:0000305}.
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DR EMBL; BC123504; AAI23505.1; -; mRNA.
DR RefSeq; NP_001070280.1; NM_001076812.1.
DR RefSeq; XP_005216493.1; XM_005216436.2.
DR AlphaFoldDB; Q08DY8; -.
DR SMR; Q08DY8; -.
DR STRING; 9913.ENSBTAP00000023036; -.
DR PaxDb; Q08DY8; -.
DR PRIDE; Q08DY8; -.
DR Ensembl; ENSBTAT00000023036; ENSBTAP00000023036; ENSBTAG00000017325.
DR GeneID; 507340; -.
DR KEGG; bta:507340; -.
DR CTD; 9776; -.
DR VEuPathDB; HostDB:ENSBTAG00000017325; -.
DR VGNC; VGNC:26251; ATG13.
DR eggNOG; KOG3874; Eukaryota.
DR GeneTree; ENSGT00390000007055; -.
DR HOGENOM; CLU_036365_0_0_1; -.
DR InParanoid; Q08DY8; -.
DR OMA; ICYRIYM; -.
DR OrthoDB; 926357at2759; -.
DR TreeFam; TF321599; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000017325; Expressed in pigment epithelium of eye and 106 other tissues.
DR ExpressionAtlas; Q08DY8; baseline and differential.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0000407; C:phagophore assembly site; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0000423; P:mitophagy; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR GO; GO:1903059; P:regulation of protein lipidation; IEA:Ensembl.
DR GO; GO:0098780; P:response to mitochondrial depolarisation; IEA:Ensembl.
DR Gene3D; 3.30.900.10; -; 1.
DR InterPro; IPR040182; ATG13.
DR InterPro; IPR018731; Atg13_N.
DR InterPro; IPR036570; HORMA_dom_sf.
DR PANTHER; PTHR13430; PTHR13430; 1.
DR Pfam; PF10033; ATG13; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Autophagy; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..480
FT /note="Autophagy-related protein 13"
FT /id="PRO_0000345150"
FT REGION 127..134
FT /note="Important for interaction with ATG101"
FT /evidence="ECO:0000250|UniProtKB:O75143"
FT REGION 254..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 407..410
FT /note="LIR"
FT /evidence="ECO:0000250"
FT COMPBIAS 300..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O75143"
FT MOD_RES 318
FT /note="Phosphoserine; by ULK1"
FT /evidence="ECO:0000250|UniProtKB:O75143"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75143"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75143"
SQ SEQUENCE 480 AA; 52426 MW; 5E57C7ABB7306461 CRC64;
METDLNSQDR KDLDKFIKFF ALKTVQVIVQ ARLGEKICTR SSSSPTGSDW FNLAIKDIPE
VTHEAKKALA GQLPAVGRSM CVEISLKTSE GDSMELEIWC LEMNEKCDKE IKVSYAVYNR
LSLLLKSLLA ITRVTPAYRL SRKQGHEYVI LYRIYFGDVQ LNGLGEGFQT VRVGTVGTPV
GTITLSCAYR INLAFMSTRH FERTPPIMGI IIDHFVDRPY PSSSPMHPCN YRTAGEDTGV
ACPSVEDSQE VCATSFSTSP PSQLMVPGKE GGVPLGPSQP AHAAQADQER LATYTPSDGA
HCAATPSSSE DAETVSNSSE GRASPHDVLE TIFVRKVGAF VNKPINQVTL TSLDIPFAMF
APKNLELEDA DPMVNPPDSP ETTSPLQGSL HSDGSSGGSS GHTQDDFVMI DFKPAFSKDD
ILPMDLGTFY REFQNPPQLS SLSLDIGAQS MAEDLDSLPE KLAAHEKNVR EFDAFVETLQ
