位置:首页 > 蛋白库 > ATG1_CRYNJ
ATG1_CRYNJ
ID   ATG1_CRYNJ              Reviewed;         988 AA.
AC   P0CP70; Q55MD9; Q5K8D3;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 49.
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:0000250|UniProtKB:P53104};
GN   OrderedLocusNames=CNL06100 {ECO:0000303|PubMed:15653466};
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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. {ECO:0000250|UniProtKB:P53104}.
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. APG1/unc-51/ULK1 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW46622.1; Type=Erroneous gene model prediction; Evidence={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; AE017352; AAW46622.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_568139.1; XM_568139.1.
DR   AlphaFoldDB; P0CP70; -.
DR   SMR; P0CP70; -.
DR   STRING; 5207.AAW46622; -.
DR   PaxDb; P0CP70; -.
DR   EnsemblFungi; AAW46622; AAW46622; CNL06100.
DR   VEuPathDB; FungiDB:CNL06100; -.
DR   eggNOG; KOG0595; Eukaryota.
DR   InParanoid; P0CP70; -.
DR   OrthoDB; 1084750at2759; -.
DR   Proteomes; UP000002149; Chromosome 12.
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   3: Inferred from homology;
KW   ATP-binding; Autophagy; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW   Protein transport; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Transport.
FT   CHAIN           1..988
FT                   /note="Serine/threonine-protein kinase ATG1"
FT                   /id="PRO_0000085644"
FT   DOMAIN          27..346
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..461
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..492
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        183
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         33..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   988 AA;  107248 MW;  CDF0107160D35036 CRC64;
     MPDSNAQGSR EKESGHHRSH KERIGNYVVG AEIGRGSFAT VYKGYRSKTR VPIAIKAVSR
     QKLTSKLLEN LESEINILKV INHRNIVALT DCFKNDTHIY LVMEYCSGSD LSVYIKQRGN
     IPTLDFVPKA GSSMALLPTD DEGKIYWPHP PTGGLDERVT RSFLGQLAQA IKFLRAQDLM
     HRDIKPQNLL LQPATETEVA EGHPYGIPVL KVADFGFARI LPAAAMAETL CGSPLYMAPE
     ILRYEKYDAK ADLWSVGAVL FEMSVGRPPF RANNHVELLR RIEKSNDNIV FPDEKERDSK
     SSDETSIPVP SDIKALIRAL LKRKPNDRMG FDDFFNCGVW DGHMAESTEE ESLSLDVSTD
     SSAGLGESDR IRQMVASTEQ SKDRLIPTRA PQPLAADAAL NPQPAVPISR DTSEGRSRLS
     TPPSRPTPTR RSTPKYYVGD ATPSEPTAII PPSPSSAPTP TSAPDPGLTT QQSPTSRANP
     RPIITAASSA QRRMSGKGDG REASSVEEAA PITPPFAGPS PTMARPSRGI NEGSPLAAAP
     PITMGPDGRL ERSSALEGST SGVGTDYVVV EKQTVEINAL ADELDQASKR PMIRRSSRGS
     VVSRPVSSFK PISPNIAKND PTLGPISYSP PFALSSTPPF AMQVPRHASG GNSFPRNPSI
     PSSLNAFPPT TISASPSYGQ DAAARFGVSP GSLQTGALAR ALTNTAIRLI GTSANTAATA
     IARATAKRRP NIVRVSDMDA AEDDLLCTVE DLARKAFVLF ELADERLLAQ TQLAQTARTS
     STPTGLTGTT PPFSMQAAAA AQAGSRRKSS SSSMNSEVWI LRQQEAAAND AVVLYMKSLA
     FIVKAMDKVK RYWKNRTDVY DGYVASQELN EMGQWLRARF NETFEKAEWA KTQAGDTLLF
     PDWLVHDKAR DTSRQAAVAE LQGDLTTAEQ GYETSLWLLQ ALLDESVYEN GSIPDEDKVA
     YDRLMVPIKT RLDALRKKLA ESSGMTAR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024