ATG7_PICPA
ID ATG7_PICPA Reviewed; 654 AA.
AC O93922;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7;
DE AltName: Full=ATG12-activating enzyme E1 ATG7;
DE AltName: Full=Autophagy-related protein 7;
DE AltName: Full=Glucose-induced selective autophagy protein 7;
DE AltName: Full=Pexophagy zeocin-resistant mutant protein 12;
GN Name=ATG7; Synonyms=GSA7, PAZ12;
OS Komagataella pastoris (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=4922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF CYS-518 AND
RP CYS-562.
RX PubMed=10233149; DOI=10.1091/mbc.10.5.1353;
RA Yuan W., Stromhaug P.E., Dunn W.A. Jr.;
RT "Glucose-induced autophagy of peroxisomes in Pichia pastoris requires a
RT unique E1-like protein.";
RL Mol. Biol. Cell 10:1353-1366(1999).
RN [2]
RP FUNCTION.
RX PubMed=11856375; DOI=10.1046/j.1356-9597.2001.00499.x;
RA Mukaiyama H., Oku M., Baba M., Samizo T., Hammond A.T., Glick B.S.,
RA Kato N., Sakai Y.;
RT "Paz2 and 13 other PAZ gene products regulate vacuolar engulfment of
RT peroxisomes during micropexophagy.";
RL Genes Cells 7:75-90(2002).
RN [3]
RP NOMENCLATURE.
RX PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x;
RA Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
RA Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
RT "A unified nomenclature for yeast autophagy-related genes.";
RL Dev. Cell 5:539-545(2003).
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). Involved in glucose-induced micropexophagy. {ECO:0000250,
CC ECO:0000269|PubMed:10233149, ECO:0000269|PubMed:11856375}.
CC -!- SUBUNIT: Homodimer. Interacts with ATG8 through a thioester bond
CC between Cys-518 and the C-terminal 'Gly-116' of ATG8 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC structure {ECO:0000250}.
CC -!- DOMAIN: The C-terminal 40 residues are required for homodimerization.
CC {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; AF098976; AAD14610.1; -; Genomic_DNA.
DR AlphaFoldDB; O93922; -.
DR SMR; O93922; -.
DR GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0000426; P:micropexophagy; IMP:UniProtKB.
DR GO; GO:0000425; P:pexophagy; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Protein transport; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..654
FT /note="Ubiquitin-like modifier-activating enzyme ATG7"
FT /id="PRO_0000212819"
FT REGION 615..654
FT /note="Homodimerization"
FT MOTIF 332..337
FT /note="GXGXXG motif"
FT ACT_SITE 518
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000305"
FT MUTAGEN 518
FT /note="C->S: No more micropexophagy."
FT /evidence="ECO:0000269|PubMed:10233149"
FT MUTAGEN 562
FT /note="C->S: Normal micropexophagy."
FT /evidence="ECO:0000269|PubMed:10233149"
SQ SEQUENCE 654 AA; 74293 MW; 893937F5FBB30D8F CRC64;
MTSMDIPYSQ ISSFVNSSFF QKVSQLKLNK YRLDDTDKAI VGSVDFKFIG KNQPTSLSVD
ESSFNDNITY THAQFPVKGI LKNLNTVEDF RKVDKNEFLQ SQGLVVHKSI QDRSCLKDLS
KLTQFFILSF SDLKGFKFIY WFGFPSLVSR WKVNKLSGLT ESQIEPYESK LNEWLNARLP
IEQKQAFIID NLEFKPFEQL SSFSPDDQLN IGFIDTSSIL NKCSTQLRNI LYMLAYYGFE
NIKVYNFRFN NTTSFTLDIT LAEPLTSEPK TTGWERTAQG KLGPKLADIG ALVDPARLAD
QSVDLNLKLM KWRVMPELDL DIIKNSKVLL LGAGTLGSYV SRVLLGYGVR HITFVDNGKV
SFSNPVRQPL FNFTDCLEGG APKAETAAKA LKLIFPLITS QGYNLEVPMA GHPVTDEKRQ
YEDYQRLVTL IKEHDVVFLL MDSRETRWLP TVLCNVFDKI CITAALGFDS YLVMRHGNLF
NTEHIEAEEN SHRLGCYFCN DIIAPKDSTT DRTLDQMCTV TRPGVALLAS SLAAELFVSI
LQHPLKSHAP ASLHDNATVL GCLPQQLRGF LHNFETSKLE ANNYEYCSAC SIQVLNEYKS
RTWDFVKDAL NENNYLEDLT GLTKVKQESE IAEKKFQEFE NGLEFSDEDS EWIN
