ID   ATG13_PONAB             Reviewed;         517 AA.
AC   Q5RE28;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Autophagy-related protein 13;
GN   Name=ATG13;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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 (By similarity).
CC       {ECO:0000250}.
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, and LC3A. Interacts with TAB2 and TAB3. Interacts
CC       with 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 LC3A. {ECO:0000250}.
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-355 is required for efficient clearance of depolarized
CC       mitochondria. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG13 family. Metazoan subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR857710; CAH89979.1; -; mRNA.
DR   RefSeq; NP_001124934.1; NM_001131462.2.
DR   RefSeq; XP_009244667.1; XM_009246392.1.
DR   RefSeq; XP_009244668.1; XM_009246393.1.
DR   AlphaFoldDB; Q5RE28; -.
DR   SMR; Q5RE28; -.
DR   STRING; 9601.ENSPPYP00000003811; -.
DR   Ensembl; ENSPPYT00000003958; ENSPPYP00000003811; ENSPPYG00000003320.
DR   GeneID; 100171805; -.
DR   KEGG; pon:100171805; -.
DR   CTD; 9776; -.
DR   eggNOG; KOG3874; Eukaryota.
DR   GeneTree; ENSGT00390000007055; -.
DR   HOGENOM; CLU_036365_0_0_1; -.
DR   InParanoid; Q5RE28; -.
DR   OMA; ICYRIYM; -.
DR   TreeFam; TF321599; -.
DR   Proteomes; UP000001595; Chromosome 11.
DR   GO; GO:1990316; C:Atg1/ULK1 kinase complex; IEA:InterPro.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0000407; C:phagophore assembly site; ISS:UniProtKB.
DR   GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
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..517
FT                   /note="Autophagy-related protein 13"
FT                   /id="PRO_0000345153"
FT   REGION          333..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           444..447
FT                   /note="LIR"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        417..439
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         355
FT                   /note="Phosphoserine; by ULK1"
FT                   /evidence="ECO:0000250|UniProtKB:O75143"
FT   MOD_RES         356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75143"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75143"
SQ   SEQUENCE   517 AA;  56489 MW;  0F808991C6E1C129 CRC64;
     METDLNSQDR KDLDKFIKFF ALKTVQVIVQ ARLGEKICTR SSSSPTGSDW FNLAIKDIPE
     VTHEAKKALA GQLPAVGRSM CVEISLKTSE GDSMELEIWC LEMNEKCDKE IKVSYTVYNR
     LSLLLKSLLA ITRVTPAYRL SRKQGHEYVI LYRIYFGEVQ LSGLGEGFQT VRVGTVGTPV
     GTITLSCAYR INLAFMSTRQ FERTPPIMGI IIDHFVDRPY PSSSPMHPCN YRTAGEDTGV
     IYPSVEDSQE VCTTSFSTSP PSQLSSSRLS YQPAALGVGS ADLAYPVVFA AGLNATHLHQ
     LMVPGKEGGV PLAPNQPVHG TQADQERLAT CTPSDGTHCA ATPSSSEDTE TVSNSSEGRA
     SPHDVLETIF VRKVGAFVNK PINQVTLTSL DIPFAMFAPK NLELEDTDPM VNPPDSPETE
     SPLQGSLHSD GSSGGSSGNT HDDFVMIDFK PAFSKDDILP MDLGTFYREF QNPPQLSSLS
     IDIGAQSMAE DLDSLPEKLA VHEKNVREFD AFVETLQ