ID   ATG7_SCHPO              Reviewed;         649 AA.
AC   O43069;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1999, sequence version 2.
DT   25-MAY-2022, entry version 136.
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; ORFNames=SPBC6B1.05c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   FUNCTION.
RX   PubMed=19778961; DOI=10.1099/mic.0.034389-0;
RA   Mukaiyama H., Kajiwara S., Hosomi A., Giga-Hama Y., Tanaka N., Nakamura T.,
RA   Takegawa K.;
RT   "Autophagy-deficient Schizosaccharomyces pombe mutants undergo partial
RT   sporulation during nitrogen starvation.";
RL   Microbiology 155:3816-3826(2009).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=23950735; DOI=10.1371/journal.pgen.1003715;
RA   Sun L.L., Li M., Suo F., Liu X.M., Shen E.Z., Yang B., Dong M.Q., He W.Z.,
RA   Du L.L.;
RT   "Global analysis of fission yeast mating genes reveals new autophagy
RT   factors.";
RL   PLoS Genet. 9:E1003715-E1003715(2013).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=33138913; DOI=10.7554/elife.61245;
RA   Fukuda T., Ebi Y., Saigusa T., Furukawa K., Yamashita S.I., Inoue K.,
RA   Kobayashi D., Yoshida Y., Kanki T.;
RT   "Atg43 tethers isolation membranes to mitochondria to promote starvation-
RT   induced mitophagy in fission yeast.";
RL   Elife 9:61245-61245(2020).
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). Plays a role in meiosis and sporulation. {ECO:0000250,
CC       ECO:0000269|PubMed:19778961}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}. Preautophagosomal structure membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The GxGxxG motif is important for the function, possibly
CC       through binding with ATP. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Impairs atg8-processing (PubMed:23950735).
CC       Sensitive to nitrogen starvation (PubMed:33138913).
CC       {ECO:0000269|PubMed:23950735, ECO:0000269|PubMed:33138913}.
CC   -!- SIMILARITY: Belongs to the ATG7 family. {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; CU329671; CAA17048.1; -; Genomic_DNA.
DR   PIR; T40646; T40646.
DR   RefSeq; NP_596084.1; NM_001021998.2.
DR   AlphaFoldDB; O43069; -.
DR   SMR; O43069; -.
DR   BioGRID; 277309; 15.
DR   STRING; 4896.SPBC6B1.05c.1; -.
DR   MaxQB; O43069; -.
DR   PaxDb; O43069; -.
DR   EnsemblFungi; SPBC6B1.05c.1; SPBC6B1.05c.1:pep; SPBC6B1.05c.
DR   GeneID; 2540790; -.
DR   KEGG; spo:SPBC6B1.05c; -.
DR   PomBase; SPBC6B1.05c; atg7.
DR   VEuPathDB; FungiDB:SPBC6B1.05c; -.
DR   eggNOG; KOG2337; Eukaryota.
DR   HOGENOM; CLU_012998_2_1_1; -.
DR   InParanoid; O43069; -.
DR   OMA; VQTWRYS; -.
DR   PhylomeDB; O43069; -.
DR   Reactome; R-SPO-1632852; Macroautophagy.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:O43069; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019778; F:Atg12 activating enzyme activity; ISO:PomBase.
DR   GO; GO:0019779; F:Atg8 activating enzyme activity; ISO:PomBase.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0006914; P:autophagy; IMP:PomBase.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR   GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR   GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
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; Membrane; Nucleus; Protein transport;
KW   Reference proteome; Transport; Ubl conjugation pathway.
FT   CHAIN           1..649
FT                   /note="Ubiquitin-like modifier-activating enzyme atg7"
FT                   /id="PRO_0000212820"
FT   MOTIF           342..347
FT                   /note="GXGXXG motif"
FT   ACT_SITE        521
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   649 AA;  73362 MW;  7E6D5B6271E0A547 CRC64;
     MFVGKALQFQ SFHSSIDATF WHQLSNYKVE KQKLDASPLT IHGKFNTYSR GNISIVFGEA
     PSNSNIKDCL AEGTLLNANT PQEFTNADVK KIREEIGEVL LNSIKNGVVS ERPNELLRFL
     IFSYADIKAY KYHYWCLFPS FKETPHWIVK DLSPAESLIP SGPILSQIRE FLSTADYYQR
     PFFLLIKSTL DEWTIAPLKE LSHCVDKSLQ FYLVAEDSVQ LAEYPSWPVR NILAFAFIKF
     KLKVINLFLY RDGINSDTLS KSILIKVEAD KDMILEAPLS IVGWERNGKG VLGPRVVNLS
     TVLDPFVLSE SASTLNLSLM RWRLVPQLDL DRIQNSKCLL LGAGTLGCGV ARNLLSWGVR
     HVTFVDYSTV SYSNPVRQSL FTFEDCKRKL PKAECAAQRL KEIYPNMFST GYNISIPMLG
     HPIYEAGIEK TMHDYETLEN LISTHDAIFL LTDTRESRWL PTVISTAMDK LLINSALGFD
     SWLVMRHGSV LQKENRLGCY FCNDIFAPSN SLVDRTLDQT CTVTRSGCAN IATAIAVELF
     VSLLQHPNGH AAPVLNEDQT VLGELPHQIR GFLHNFSLMK ISGMAYPQCS ACSECIINEW
     NREKWMFVLR AINEPDYVEE LCGLREVQAL GEIAGTMEEW ISDKESVIL