ATG13_COCIM
ID ATG13_COCIM Reviewed; 980 AA.
AC Q1E891; A0A0D6K9Q1; J3KIX9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Autophagy-related protein 13;
GN Name=ATG13; ORFNames=CIMG_01222;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704911; EAS35868.1; -; Genomic_DNA.
DR RefSeq; XP_001247451.1; XM_001247450.2.
DR AlphaFoldDB; Q1E891; -.
DR SMR; Q1E891; -.
DR STRING; 246410.Q1E891; -.
DR PRIDE; Q1E891; -.
DR EnsemblFungi; EAS35868; EAS35868; CIMG_01222.
DR GeneID; 4565626; -.
DR KEGG; cim:CIMG_01222; -.
DR VEuPathDB; FungiDB:CIMG_01222; -.
DR InParanoid; Q1E891; -.
DR OMA; MHQHPRS; -.
DR OrthoDB; 1519629at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
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..980
FT /note="Autophagy-related protein 13"
FT /id="PRO_0000317946"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 105385 MW; B9BCB4F623F731E3 CRC64;
MHQHRRTSSA VASPVSSPHP SSSRPITRDR GTARFGPNVS RGLGIDRQMD ASDQEQTIES
PEKSPSQKLD QIIQNYHTKA ALVILHSRVD LSPATYHGVI RTNKWFNVEV NETEDLKDSL
GVWKYSNCTD SRPPPLIIEV YLDLTQLTNN QSLVIIDDSG KRWDVVEALA TYGCLDNSRT
SKSGVILERW RIDLGPGPDD LPLDMGSILP TVYKKSIVVF RSLYAYSKLL PAWKYSKRHS
KIRPNPALSL KYRILQGPGG QIRSTNDPLT VPLHPGNGPV VDTYSFGVTD SPAGPLSALV
TYRTNCDFRV DDSEALLSSR FMGVDERFFK PSLPSEDNFA AAGQEHGSLP VQKRDVGRPD
LGQAYGSMST FHQVGATTGA SPISALRAAR ELAAGSPSSP TRPSHSPRPS QAGRVAALSG
EGNHLIQRRP SISIQPFKAP PLSASPALVD SPVGSQPKNS APRVGPMDIT SSARQMPPPH
GTPTTSRRSA HVSESAIASS TSGSPRPAPI SKYSSSFSHR RGRLSSGGAS KTDDDNNSSG
RVSVSSSTVH PGSGTSADPA TTSSGSLQAD EDNISDFLKM LEMGKDLLSR KDSKSLDKNT
KRTSAALSRF QKMRDSNAVL SDSMSSSLLL QPSSISSSKQ LPNAATSVAG ASISVSSSPG
KAISPHTQHI PAVPSRLSSN SVVDYSHSHE DRHERRHRLS HESRRSPSEE RANDEPRLKR
DESTANAIDI PTSPRPFIPS FRRSSSAAQR RSSPPVEDDL GDFLPFGMRS LSLGAEDRST
LSLSELVRQQ ESSVPASDTN ALQQQNQKDT RTGQSIVDES PSRIDNVPGT SSPRQYQPRF
AHGRGRGSFG HPQPHVSAAS SLGRASPIPN VTDADREGYI GSGNNGGTAV PPDTRRGSSH
RFSFNRHLGT PANMDEDEPL LFAMSDFGAS RRSLEEGRKG ATTAGADHGG APSTELQPAA
ETRSEGGPPS VSRGRYRAWP
