ATG7_CRYNB
ID ATG7_CRYNB Reviewed; 673 AA.
AC P0CM39; Q55NS2; Q5KC57;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7;
DE AltName: Full=ATG12-activating enzyme E1 ATG7;
DE AltName: Full=Autophagy-related protein 7;
GN Name=ATG7; OrderedLocusNames=CNBH0170;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
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: E1-like activating enzyme involved in the 2 ubiquitin-like
CC systems required for cytoplasm to vacuole transport (Cvt) and
CC autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for
CC its conjugation with phosphatidylethanolamine. Both systems are needed
CC for the ATG8 association to Cvt vesicles and autophagosomes membranes.
CC Autophagy is essential for maintenance of amino acid levels and protein
CC synthesis under nitrogen starvation. Required for selective autophagic
CC degradation of the nucleus (nucleophagy) as well as for mitophagy which
CC contributes to regulate mitochondrial quantity and quality by
CC eliminating the mitochondria to a basal level to fulfill cellular
CC energy requirements and preventing excess ROS production. Plays a role
CC in the regulation of filamentous growth and chronological longevity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC structure {ECO:0000250}.
CC -!- DOMAIN: The GxGxxG motif is important for the function, possibly
CC through binding with ATP. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}.
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DR EMBL; AAEY01000040; EAL19445.1; -; Genomic_DNA.
DR RefSeq; XP_774092.1; XM_768999.1.
DR AlphaFoldDB; P0CM39; -.
DR SMR; P0CM39; -.
DR EnsemblFungi; EAL19445; EAL19445; CNBH0170.
DR GeneID; 4937519; -.
DR KEGG; cnb:CNBH0170; -.
DR VEuPathDB; FungiDB:CNBH0170; -.
DR HOGENOM; CLU_012998_2_1_1; -.
DR Proteomes; UP000001435; Chromosome 8.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0097632; C:extrinsic component of phagophore assembly site membrane; IEA:EnsemblFungi.
DR GO; GO:0019778; F:Atg12 activating enzyme activity; IEA:EnsemblFungi.
DR GO; GO:0019779; F:Atg8 activating enzyme activity; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0006501; P:C-terminal protein lipidation; IEA:EnsemblFungi.
DR GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR GO; GO:0016236; P:macroautophagy; IEA:EnsemblFungi.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IEA:EnsemblFungi.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.140.100; -; 1.
DR Gene3D; 3.40.140.70; -; 1.
DR InterPro; IPR006285; Atg7.
DR InterPro; IPR032197; Atg7_N.
DR InterPro; IPR042522; Atg7_N_1.
DR InterPro; IPR042523; Atg7_N_2.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF16420; ATG7_N; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR TIGRFAMs; TIGR01381; E1_like_apg7; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasm; Protein transport; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..673
FT /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT /id="PRO_0000410021"
FT REGION 268..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 346..351
FT /note="GXGXXG motif"
FT ACT_SITE 536
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 673 AA; 73352 MW; 81DA4A55A6D33334 CRC64;
MAPLQFQPLA SQPTPAFWAA LAAHKLNHLK LDDSHLPITA QIEPAKRVLI NKERVDDTAD
VGIDGSLVVG GDAFEAERGR LPPNAVSVTG TLKIFNTIEE FKDTSAKKRL FDDLVSQMLE
SFDTDRPVLN PFLLVTFADL KKYVYHYWFA FPALVSSPAW VMDGEFMPVD EIEDIRNLAQ
SHFQHNTAAF LLKGAAPHLS AAPLSSCSTF YDKTQSEMVT VVFHDTSSLP SNPGWGLRNV
LYYLSAKHGI TSLVVICLRG GSSSTQASLS LSSPPSTAPA KPPQAVGWER HPSGKLSPRV
ADLGPMMDPT RLAAQAVDLN LKLIKWRLLP ALDLDKISGT RCLLLGAGTL GCYVARILMG
WGVRNITLVD SSTVSYSNPV RQPLFTFSDC LNGGLPKAPT AAKKLQEIFP GVNAQGVVLG
IPMPGHPISS SDDAVEKDVA KLEALVKSHD AVFLLMDSRE SRWLPTVLGR KWGKVVVNAA
LGFDSFLVMR HGAGAGARRI QWDEGGVGEK GLGCYYCNDI VAPADSLSDR TLDQMCTVTR
PGVAPIAAAM AVELLISVLQ HPLGVHAPAE RPDTAETSTS TKTSPLGCVP HQLRGQMYQW
KTQIVEGEAF DRCTGCSDYV LNEYETNGFA FLRRVFNEKD YLEKVTGLDE LYRESEKVIE
GMEGLDWDSE GEE