ATG13_OGAPD
ID ATG13_OGAPD Reviewed; 700 AA.
AC W1QCN1;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Autophagy-related protein 13 {ECO:0000303|PubMed:29438555};
GN Name=ATG13 {ECO:0000303|PubMed:29438555}; ORFNames=HPODL_03959;
OS Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=871575;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1;
RX PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA Skryabin K.G.;
RT "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL BMC Genomics 14:837-837(2013).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29438555; DOI=10.1093/femsyr/foy010;
RA Dmytruk K.V., Ruchala J., Grabek-Lejko D., Puchalski C., Bulbotka N.V.,
RA Sibirny A.A.;
RT "Autophagy-related gene ATG13 is involved in control of xylose alcoholic
RT fermentation in the thermotolerant methylotrophic yeast Ogataea
RT polymorpha.";
RL FEMS Yeast Res. 0:0-0(2018).
CC -!- FUNCTION: Activates the ATG1 kinase in a nutritional condition
CC dependent manner through the TOR pathway, leading to autophagy (By
CC similarity). Involved in ATG9 and ATG23 cycling through the pre-
CC autophagosomal structure (By similarity). Also involved in cytoplasm to
CC vacuole transport (Cvt) and more specifically in Cvt vesicle formation
CC (By similarity). Seems to play a role in the switching machinery
CC regulating the conversion between the Cvt pathway and autophagy (By
CC similarity). Finally, ATG13 is also required for glycogen storage
CC during stationary phase (By similarity).
CC {ECO:0000250|UniProtKB:Q06628}.
CC -!- FUNCTION: Acts as a negative regulator of xylose alcoholic
CC fermentation, a role that is not related to autophagy
CC (PubMed:29438555). {ECO:0000269|PubMed:29438555}.
CC -!- SUBUNIT: Hypophosphorylated form interacts with ATG1 to form the ATG1-
CC ATG13 kinase complex (By similarity). The ATG1-ATG13 complex interacts
CC with the ATG17-ATG29-ATG31 complex through direct interaction with
CC ATG17. Interacts with VAC8 (By similarity).
CC {ECO:0000250|UniProtKB:Q06628}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06628}.
CC Preautophagosomal structure {ECO:0000250|UniProtKB:Q06628}.
CC -!- DISRUPTION PHENOTYPE: Leads to derepression of several genes involved
CC in xylose catabolism including PDC1, DAS1 and AOX1, and subsequent
CC increased ethanol production from xylose (PubMed:29438555).
CC {ECO:0000269|PubMed:29438555}.
CC -!- SIMILARITY: Belongs to the ATG13 family. Fungi subfamily.
CC {ECO:0000305}.
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DR EMBL; AEOI02000008; ESW98330.1; -; Genomic_DNA.
DR RefSeq; XP_013934213.1; XM_014078738.1.
DR AlphaFoldDB; W1QCN1; -.
DR SMR; W1QCN1; -.
DR STRING; 1005962.W1QCN1; -.
DR EnsemblFungi; ESW98330; ESW98330; HPODL_03959.
DR GeneID; 25773390; -.
DR eggNOG; KOG4573; Eukaryota.
DR HOGENOM; CLU_448417_0_0_1; -.
DR OMA; YAKLHRP; -.
DR OrthoDB; 1519629at2759; -.
DR Proteomes; UP000008673; Chromosome V.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IEA:InterPro.
DR GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR GO; GO:0000045; P:autophagosome assembly; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Autophagy; Cytoplasm; Protein transport; Reference proteome; Transport.
FT CHAIN 1..700
FT /note="Autophagy-related protein 13"
FT /id="PRO_0000443909"
FT REGION 319..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..407
FT /note="ATG17-binding"
FT /evidence="ECO:0000250|UniProtKB:W0TA43"
FT REGION 428..487
FT /note="ATG1-binding"
FT /evidence="ECO:0000250|UniProtKB:W0TA43"
FT REGION 506..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 77768 MW; 9BE6B66989B67E0A CRC64;
MSSVRRPSKL LSEKQSDKLA QIIQNFFLKA AHVIFHFRVA FPSVVLQPDD SYGAMGDSFA
QSKYNNRWFN LDLGNYEIPR TELSLWRNKD ILSLPPLVLE TFLDLRGLSS NQTLMLDDVI
VKTSKKSEIV LERWLIEFDL STFDNEVMEF PSIYKKIIIL FRSLYLLAGL LPSYKLRDKL
VKSKSKNSAI HVSCRILDGS KPITSKGRIG LSKKLLSEDE HTSSKKLQPI LTPIGALRVS
VSYRTNCNFQ VSDNEEALSS QFMLDHLPSV RTNYDSDGNS LTSPMDYLQN RVSSASIHLS
DQSPRRRSST RSVQLFKVGS INSSSSPPPG ATQSNQSVSS FSTSKPIPVT LNKTNSSASL
VPILRQNRDS LPKSIGSMVQ NQMQETGHQV SSNSRRFSSS FGSRFRTVSS RNNSLDGQLV
VANQPFSTPN NPILHNFRSR NKSPSVSSTE LGPSSSIYMD DDLDSFMKML DSKPDLRFPS
NSPSVYEDPL ANFKTFQKSN DFLTLEQQQH GSPSSNQIMI HSQSQTSQSQ VFKRTVSSDR
SRRGSVSSNY SPSSQALRPG VSAPMVTPSV TYGKFHASSG SPSNSSLAQY LRHNSSPPAS
ATAVATVHNS LRRLTSSSQR TNTNSTNSST RPVNPELLKL KSFNEDVFES DDDEHDEHSP
RSTDTKSRNT GPSSGHAEDD EDDLLFAMSD MTLAKNNQEF
