ATG13_ASPOR
ID ATG13_ASPOR Reviewed; 974 AA.
AC Q2ULT1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Autophagy-related protein 13;
GN Name=atg13; ORFNames=AO090003000280;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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}.
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DR EMBL; AP007155; BAE57484.1; -; Genomic_DNA.
DR RefSeq; XP_001819486.1; XM_001819434.1.
DR AlphaFoldDB; Q2ULT1; -.
DR SMR; Q2ULT1; -.
DR STRING; 510516.Q2ULT1; -.
DR PRIDE; Q2ULT1; -.
DR EnsemblFungi; BAE57484; BAE57484; AO090003000280.
DR GeneID; 5991469; -.
DR KEGG; aor:AO090003000280; -.
DR VEuPathDB; FungiDB:AO090003000280; -.
DR HOGENOM; CLU_007151_1_0_1; -.
DR OMA; MHQHPRS; -.
DR Proteomes; UP000006564; Chromosome 2.
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:0006914; P:autophagy; IMP:AspGD.
DR GO; GO:0009306; P:protein secretion; IMP:AspGD.
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..974
FT /note="Autophagy-related protein 13"
FT /id="PRO_0000317945"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 103814 MW; 3B809646EF8C9E05 CRC64;
MHQHPRSPAP TAPTSSARPN SSRSRELDYR PNSPAADVRV HNSRGLGIET EPDSSGQTVQ
PAKEAIAKLN QIISNYHTKA ALIILHSRIE LPPSFNKGSD TPRVNRWFNV EIEDTDVLRE
QLRTWRTCDA TENRPPPLII ETYLDTKGLT NNQTLVALDE NGKRWDVLEA LAASQQAHPV
RPPSASSDDV ILERWRVELG DTSNALPADL GSILPTVYKK SIVLFRSLFT YSKFLPAWKF
AKRNGRLRAN PALRIKYRII IGSPNQVSSK PDHLTMPLYE SSSKVVETYS FGVTDSPAGP
FSAQVTYRTS CDFRVDDSEA LLSSRFMGAD DEIFRPSLPT RVVDSKVPPP EIGSLPQERR
TIEDPDPGRA YGSLSTFHQV GPTTSASPIS ALRAKGKLGT SSPSSPGSSS RKALAVAKAS
PVGRAAALAS EGSPGVVRRP SISFQPFKAP PLSASPSLVD PPLSSPRSVS GPRPHPPMAA
SARKSFPAVQ DNSIASPSSA SPRPSSISRY SSAFSHRRGR PSSGGINKLE DDTSSGKASA
TSSAQPGSGL LAEPTGTSAD SIHADDENIS EFLKMLDLRK DLLNTSGSAA LDATARRTTV
TSAALTRFQR MRDSNAALSD SMSSSLLLQR SSNSSSKQLS GVPPMVAGTS ISTASSPGKP
ISPHTPHTPA IPSRLSSNSI VDYTHSEGNG TELSQGHGSP LDENTSDGTT MEHGPSAVNA
IDIPTSPRLF PPVYRRSSSA AHRPRTVAVD DDEIFPFNRS VSLGAEERSN LSLGALHRQH
EYESSDTATH RAQREPRPMS SNEDAVVPPS SITRGQGSHK GVTPGPTVAS SSSSHHHVYQ
PRFSHSRGRG SSGGHHSLSS GSSSLARGAA ITPGLAERES ERDGNGSGSN SVTSAMEDRR
GVGRRPSAGR GGPPQSAQLE EDEPLLFAMS DFGASRRSFE EGKHVNHAHD PTGNIAGSRR
GGSSRRGGGF HAWS
