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ATG13_DEBHA
ID   ATG13_DEBHA             Reviewed;         837 AA.
AC   Q6BQ20; B5RTX9;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Autophagy-related protein 13;
GN   Name=ATG13; OrderedLocusNames=DEHA2E09020g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382137; CAR65791.1; -; Genomic_DNA.
DR   RefSeq; XP_002770448.1; XM_002770402.1.
DR   AlphaFoldDB; Q6BQ20; -.
DR   SMR; Q6BQ20; -.
DR   STRING; 4959.XP_002770448.1; -.
DR   EnsemblFungi; CAR65791; CAR65791; DEHA2E09020g.
DR   GeneID; 8998709; -.
DR   KEGG; dha:DEHA2E09020g; -.
DR   VEuPathDB; FungiDB:DEHA2E09020g; -.
DR   eggNOG; KOG4573; Eukaryota.
DR   HOGENOM; CLU_366802_0_0_1; -.
DR   InParanoid; Q6BQ20; -.
DR   OMA; MHQHPRS; -.
DR   OrthoDB; 1519629at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
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..837
FT                   /note="Autophagy-related protein 13"
FT                   /id="PRO_0000157968"
FT   REGION          302..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          631..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..353
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..812
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   837 AA;  92307 MW;  AE7E6361679BAE30 CRC64;
     MVSPGQNDLS SDKSQIDPFV KKQNAKLTQV IQNFFSKSVQ IVLQSRIQSE SHNKEEQLKV
     GGDVGGHNVS SKINKWFNLH MYNDNLPKEE LKLWKNINDV SQMPPMIIEV YLDLRQLTAI
     QTVILRDDNG NPWTVAKGGS KKHEVVLERW LIEFDANTVS GTIVDELPLI YKQAIILFRS
     LYGYTRLMPT FKLKKNLNKS NLNIGCKILD GKQPISSKGR IGLSKSIIPH QMLTTESHMS
     HKHFLPIQTT LGTLKISIAY RNHHEFSIHD NEELLSTHFV NIDDNDKDSE ITPVEIEFKE
     ELKIDRDSTT NEKVNEPEDD ESHHADVESS QEHLQSEEPD ESFEQDAKHI SGSRKKFSIS
     NNASMSLSPC SSGPQTVTED SPSHNKPSAN TTPIVSQRPT INPFKVGSIS TSPPATTNFG
     GSSLERKVSI TSNKSASNAS LAAMLRNPRS STSSTNTTAN IPIANNNSNN QYNSTFPRSV
     SSSHGSNLAH DNDNLLGFSN PDNTSNTPRF SSSFGSRASR RFSNTSGRQS SLPSGNMNDT
     SLLATSAGSA SSDAPMSGLY IDDDIGDFVR MIDSKSDLRF SGYNSNNDSK ISYNQGSNSQ
     IDALNKFQML KNQHQQLSDS VSASLILHHN QLSGSRPSSR KSSHSIHSPP PSLPSGSYDN
     SHLPSINSKL RENSSTSGND DNLARDSGTP SSRKNSFDYS TNSNTTFLKS PITNKLVSSP
     VTSTTPIHSC LHKTNNESGV ISGLATTPSI YNDRRQIHYE SVFDDDDDDY ANNTADNRDQ
     DDSLKLYLTN KLANAPKSNT NSRSLKSSTN PPNIGEDDDD DDDDLLFTMS DMNLAKH
 
 
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