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ATG1_USTMA
ID   ATG1_USTMA              Reviewed;         990 AA.
AC   Q4P0K0; A0A0D1DT05;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Serine/threonine-protein kinase ATG1 {ECO:0000250|UniProtKB:P53104};
DE            EC=2.7.11.1 {ECO:0000250|UniProtKB:P53104};
DE   AltName: Full=Autophagy-related protein 1 {ECO:0000250|UniProtKB:P53104};
GN   Name=ATG1 {ECO:0000303|PubMed:20618705}; ORFNames=UMAG_06363;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20618705; DOI=10.1111/j.1364-3703.2010.00620.x;
RA   Nadal M., Gold S.E.;
RT   "The autophagy genes ATG8 and ATG1 affect morphogenesis and pathogenicity
RT   in Ustilago maydis.";
RL   Mol. Plant Pathol. 11:463-478(2010).
CC   -!- FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to
CC       vacuole transport (Cvt) and found to be essential in autophagy, where
CC       it is required for the formation of autophagosomes. Involved in the
CC       clearance of protein aggregates which cannot be efficiently cleared by
CC       the proteasome. Required for selective autophagic degradation of the
CC       nucleus (nucleophagy) as well as for mitophagy which contributes to
CC       regulate mitochondrial quantity and quality by eliminating the
CC       mitochondria to a basal level to fulfill cellular energy requirements
CC       and preventing excess ROS production. Also involved in endoplasmic
CC       reticulum-specific autophagic process, in selective removal of ER-
CC       associated degradation (ERAD) substrates. Plays a key role in ATG9 and
CC       ATG23 cycling through the pre-autophagosomal structure and is necessary
CC       to promote ATG18 binding to ATG9 through phosphorylation of ATG9.
CC       Catalyzes phosphorylation of ATG4, decreasing the interaction between
CC       ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of
CC       ATG8 (By similarity). Required for wild-type budding of haploid
CC       sporidia and for complete symptom development during pathogenic growth
CC       such as gall formation and teliospore production in ears of mature
CC       maize (PubMed:20618705). {ECO:0000250|UniProtKB:P53104,
CC       ECO:0000269|PubMed:20618705}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000250|UniProtKB:P53104};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P53104};
CC   -!- SUBUNIT: Homodimer. Forms a ternary complex with ATG13 and ATG17.
CC       {ECO:0000250|UniProtKB:P53104}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}.
CC       Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}.
CC   -!- INDUCTION: Transcripts accumulate during carbon stress conditions.
CC       {ECO:0000269|PubMed:20618705}.
CC   -!- DISRUPTION PHENOTYPE: Prevents vacuolar accumulation of autophagosomes
CC       and affects survival during carbon starvation.
CC       {ECO:0000269|PubMed:20618705}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. APG1/unc-51/ULK1 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
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DR   EMBL; CM003162; KIS65660.1; -; Genomic_DNA.
DR   RefSeq; XP_011392657.1; XM_011394355.1.
DR   AlphaFoldDB; Q4P0K0; -.
DR   SMR; Q4P0K0; -.
DR   STRING; 5270.UM06363P0; -.
DR   EnsemblFungi; KIS65660; KIS65660; UMAG_06363.
DR   GeneID; 23565972; -.
DR   KEGG; uma:UMAG_06363; -.
DR   VEuPathDB; FungiDB:UMAG_06363; -.
DR   eggNOG; KOG0595; Eukaryota.
DR   HOGENOM; CLU_006447_0_0_1; -.
DR   InParanoid; Q4P0K0; -.
DR   OMA; INNVVQW; -.
DR   OrthoDB; 1084750at2759; -.
DR   PHI-base; PHI:2498; -.
DR   Proteomes; UP000000561; Chromosome 23.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR   GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR   InterPro; IPR045269; Atg1-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR022708; Ser/Thr_kinase_C.
DR   PANTHER; PTHR24348; PTHR24348; 1.
DR   Pfam; PF12063; DUF3543; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Autophagy; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW   Protein transport; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Transport.
FT   CHAIN           1..990
FT                   /note="Serine/threonine-protein kinase ATG1"
FT                   /id="PRO_0000085653"
FT   DOMAIN          15..334
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          375..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          529..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          970..990
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        165
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         21..29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   990 AA;  106540 MW;  FFABEF71CB4590EF CRC64;
     MSKSSTGRDE RIGDFVIENE IGKGSFAVVH KGYRLQPREP VAIKIVIRKK LTPKLLDNLE
     GEIAILKAIH HPNIVELKEC LKTEHQIYLV MAFCASGDLA QYIKKRFDIY ERAGMAEPDS
     LTKGFKPTYP HPVDGGLNET IVRSILTQLA AALEFMRARD IVHRDIKPQN LLLQPPDAAF
     LALGNPREIP QMKVADFGFA RHLSVNTLAE TLCGSPLYMA PEILRFEKYD AKADLWSVGA
     VLFEMTVGKP PFRAANHVEL LKRIERGEDK IKFPDERSAG SLAREAARRQ ELGEAPLPPP
     HPVSEDVKIL IRQLLRQRPV SRMSFDDFFA SPVISDFKAF IRPRAQPEAV ERYEDLQRSE
     RSVIIPSSGI KHVSVSSIEA STQQPGVQPP VSTATSPPAL ESRSTQEASP KAITGETIAP
     NKTPREDARP PRTLPRAFSA KYVTGEPPQP EDLEKRVPPT MTRTPSSPGI PEGSLLSGER
     DEAPQATTEH FGSSKGGEDS FLGKEYVLIE KQSVEVNALA DELAASPQSR LGLASRRPSR
     LSRLSSGPLP SAPGASPPTA PPTILSSKPI RIANNTNTAS TGAFALPPGS RPSSFPRRAS
     LSSSGSPSTR QGGQVITNMD AVASTQSNRR DGNASSFPKD EVSVLGQRLA GFGLSGSGVG
     GGPSSALAKA ISMASLRLFG VPSGVSLRDA AALVRTRAQR RGIARATDSL DEAEMTLLST
     LEDLGQKAFV LSEFADSKLA HFFPDGPHQL SQELDSSTAT SGISPSRNSV QGSARRVGSI
     SSSSSSAVDP VAAEAASAEA LMLYVRSLAF LQRAITLTKR HVESRSRPGV PAVTSAELND
     VVQWLRARFN EVYDKADFAR SRCSELPESA QQVDKLIFDK AVEVARAAAT DELENNREGS
     GWDPSHCLLA YETANSMLSS LLDPGEDAMS LSEGSILMID GYVKSINKRL WTLQEQFGGG
     VGAVGAAGAS PVGVDAEARP GVSRSRTESP
 
 
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