ATG13_PANTR
ID ATG13_PANTR Reviewed; 474 AA.
AC A5A6N3;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Autophagy-related protein 13;
GN Name=ATG13;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT large potential divergence of the transcriptome.";
RL Gene 399:1-10(2007).
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; AB222161; BAF62406.1; -; mRNA.
DR RefSeq; NP_001092013.1; NM_001098543.1.
DR AlphaFoldDB; A5A6N3; -.
DR SMR; A5A6N3; -.
DR STRING; 9598.ENSPTRP00000006164; -.
DR PaxDb; A5A6N3; -.
DR GeneID; 451155; -.
DR KEGG; ptr:451155; -.
DR CTD; 9776; -.
DR eggNOG; KOG3874; Eukaryota.
DR InParanoid; A5A6N3; -.
DR Proteomes; UP000002277; Unplaced.
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:0000407; C:phagophore assembly site; ISS:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0000423; P:mitophagy; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
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..474
FT /note="Autophagy-related protein 13"
FT /id="PRO_0000345152"
FT REGION 127..134
FT /note="Important for interaction with ATG101"
FT /evidence="ECO:0000250|UniProtKB:O75143"
FT REGION 295..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 407..410
FT /note="LIR"
FT /evidence="ECO:0000250"
FT COMPBIAS 380..402
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 474 AA; 52069 MW; 7205DB49BB9E035A CRC64;
METDLNSQDR KDLDKFIKFF ALKTVQVIVQ ARLGEKICTR SSSSPTGSDW FNLAIKDIPE
ITHEAKKALA GQLPAVGRSM CVEISLKTSE GDSMELEIWC LEMNEKCDKE IKVSYTVYNR
LSLLLKSLLA ITRVTPAYRL SRKQGHEYVI LYRIYFGEVQ LSGLGEGFQT VRVGTVGTPV
GTITLSCAYR INLAFMSTRQ FERTPPIMGI IIDHFVDRPY PSSSPMHPCN YRTAGEDTGV
IYPSVEDSQE VCTTSFSTSP PSQLMVPGKE GGVPLAPNQP VHGTHADQER LATCTPSDGT
HCAATPSSSE DTETVSNSSE GRASPHDVLE TIFVRKVGAF VNKPINQVTL TSLDIPFAMF
APKNLELEDT DPMVNPPDSP ETESPLQGSL HSDGSSGGSS GNTHDDFVMI DFKPAFSKDD
ILPMDLGTFY REFQNPPQLS SLSIDIGAQS MAEDLDSLPE KNVREFDAFV ETLQ
