ATG13_CANAL
ID ATG13_CANAL Reviewed; 761 AA.
AC Q5A1Z5; A0A1D8PSD2; Q5A245;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Autophagy-related protein 13;
GN Name=ATG13; Synonyms=APG13; OrderedLocusNames=CAALFM_CR02910WA;
GN ORFNames=CaO19.10367, CaO19.2848;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017630; AOW31030.1; -; Genomic_DNA.
DR RefSeq; XP_715779.2; XM_710686.2.
DR AlphaFoldDB; Q5A1Z5; -.
DR SMR; Q5A1Z5; -.
DR STRING; 237561.Q5A1Z5; -.
DR PRIDE; Q5A1Z5; -.
DR GeneID; 3642586; -.
DR KEGG; cal:CAALFM_CR02910WA; -.
DR CGD; CAL0000176796; orf19.10367.
DR VEuPathDB; FungiDB:CR_02910W_A; -.
DR eggNOG; KOG4573; Eukaryota.
DR HOGENOM; CLU_366802_0_0_1; -.
DR InParanoid; Q5A1Z5; -.
DR OrthoDB; 1519629at2759; -.
DR PRO; PR:Q5A1Z5; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0000423; P:mitophagy; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
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..761
FT /note="Autophagy-related protein 13"
FT /id="PRO_0000157966"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 84411 MW; F1B1910839900D9B CRC64;
MLSDFKQQQQ QKHHSHNPPN SHDDTQTKLQ VAKLTQVIQK FFTKAAQIIL ESRAYPETST
PSLYPTKEES SKINKWFNLY MTNIPDSCKD DLKLWKGVDL TTIPPMIIET YIDLRSLPAD
QTLVLMDDEK HPWTVAKSRG KKQEVVLERW LIEFEPNTTD ATVMVEELPL SYKQAIVLFR
SIYGFTRLMP AFKVKKNLQN KLPLGNKILD GNQPISSKGR IGLSKPIINT RTNESHMTQK
YFQPVHTSLG TLKISVAYRM DSEFCLHENE ELLSSHFHKR DEEETKKKVS SSVSPLSSGT
SLKETSTSPR KSQPPIRIQP FKVGSMSTSP PVQSPSISQP GTAPIQNQPS VPSSSLERRV
SITSNKSTSN ASLAAFLRNA RSSTPSANNI PIINANPISG TSVPRSFSSS TGHEDSIFVN
PDSASNTPRF ASSFGSRASR RYSSTSIRQQ TPQSDLMGQT NSVDAALSGI DADDDISDFV
RMIDSKSDLR LGGGGGGGNS SVHNMSINES SYHGDALNKF QSLRSQYQQL SDSVSASLIL
QSRHSSRKSS LNSPAGSFDS HHHQHQQQQQ QQQNQQQSQS PHTNTTSSIH SHAHSYSHSR
MKDARPRSED HQQTKFSAAR RSSNISPTTA VPSSIGTPSS ISSRIPHVTT IISSSDVSST
GGNRTKSAAT TAIVSGMATS PSIYDYRSPR YQNVFDDDDE DDNDEEEGDR EGNQLHEGRN
STESSQNQSK RIMKHIKKDE EDSEDDEDLL FTMSDMNSRN F
