ATG13_ASPNC
ID ATG13_ASPNC Reviewed; 958 AA.
AC A2QWA6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Autophagy-related protein 13;
GN Name=atg13; ORFNames=An11g04460;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Activates the atg1 kinase in a nutritional condition
CC dependent manner through the TOR pathway, leading to autophagy. Also
CC involved in cytoplasm to vacuole transport (Cvt) and more specifically
CC in Cvt vesicle formation. Seems to play a role in the switching
CC machinery regulating the conversion between the Cvt pathway and
CC autophagy. Finally, atg13 is also required for glycogen storage during
CC stationary phase (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with atg1 to form the atg1-atg13 kinase complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06628}.
CC Preautophagosomal structure {ECO:0000250|UniProtKB:Q06628}.
CC -!- SIMILARITY: Belongs to the ATG13 family. Fungi subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM270234; CAK45934.1; -; Genomic_DNA.
DR RefSeq; XP_001394439.1; XM_001394402.2.
DR AlphaFoldDB; A2QWA6; -.
DR SMR; A2QWA6; -.
DR PaxDb; A2QWA6; -.
DR EnsemblFungi; CAK45934; CAK45934; An11g04460.
DR GeneID; 4984677; -.
DR KEGG; ang:ANI_1_606094; -.
DR VEuPathDB; FungiDB:An11g04460; -.
DR HOGENOM; CLU_007151_1_0_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
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..958
FT /note="Autophagy-related protein 13"
FT /id="PRO_0000317944"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..759
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..958
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 958 AA; 102909 MW; 68376513AE3015C3 CRC64;
MHQHPRSPAP AAPPSASRPG ANRSDDRPNS PAFDPRVQLT RGLGIETEAR SSGQTSSSRP
AKEAISKLNQ LVTNYHTKAA LVILASRIDL TRSDDTPKIN PKVNRWFAID LEDIDALREQ
LRFWRINDVS EQPPPPLIIE TYLDTKDLTN NQSLVALDEQ GKRFDVLESL SRSSEAHAKG
PVSSRSEDVI LERWRVELGN TPNKALPADL GSILPKIYKQ SIVTFRTLFT YSKLLPAWKL
AKRNGRLHAH PALQIRYRIL AGKPNPDDSR PDRLTTPLFD SSNKVVETYT FGTTESPVGY
LSIQVTYRTS CEFRVDDSEA LLSSRFMGAD DEVFRPSLPS RESNLKAANS GVGSAPVEKR
TVEDPDPSRA YGSLSTFHHV GPTTSASPIS ALRAARESGA ASPSPPSSSS RKPVEVVKAS
PLGRAAVLAN ESSPGVARRS SISFPPFKAP PLSASPSLVD PPLGMSPRSG TMTRPQFPES
KNMPPPSMAA SARKSLPLPG ASETTATSSN SASPRPTPIA RYSSAFTHRR GRPSSGNINR
IDDENSSGKT SATSSNPQPG SGLLAEATGT SADSIHADDE NITEFLKMLD LRKDLLRTSN
SASADVTARR TTATSAALTR FQRMRDSNAQ LSESMSSSML LQRSSTSSSK QLSGVPPMVA
GTSISTASSP GKPISPHTPH TPAIPSRLSS NSIVDYGNER GREQPSSVGD YTPEGPTIPH
RPSVVTVNAI DIPTSPGLPF PPYRRPSSAA PPPPPVATDD DEIFPFNLRS VSLGAEERSH
NSLSALQRQH DLEGAKSNTQ PTRREQRPPL ASEDPSRRSS STGHGTSPHK RTSLSGPTVA
PSPSNNHVYQ PRFSLCRGRG LSGGPHSLSS GSSSLARGAP SDLAERDHDR DVNASGSNSG
TSTVEDRRAA GRRPSSGRNI PPPSQVEEDE PLLFAMSDFG ASRRSFEEGR HGNHGRRL
