ATG7_DICDI
ID ATG7_DICDI Reviewed; 707 AA.
AC Q86CR9; Q55BK5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 122.
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; Synonyms=apg7; ORFNames=DDB_G0271096;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=AX3 / DH1;
RX PubMed=12626495; DOI=10.1074/jbc.m212467200;
RA Otto G.P., Wu M.Y., Kazgan N., Anderson O.R., Kessin R.H.;
RT "Macroautophagy is required for multicellular development of the social
RT amoeba Dictyostelium discoideum.";
RL J. Biol. Chem. 278:17636-17645(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19667176; DOI=10.1073/pnas.0813319106;
RA Jia K., Thomas C., Akbar M., Sun Q., Adams-Huet B., Gilpin C., Levine B.;
RT "Autophagy genes protect against Salmonella typhimurium infection and
RT mediate insulin signaling-regulated pathogen resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14564-14569(2009).
CC -!- FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like
CC systems required for autophagy (PubMed:12626495). Activates atg12 for
CC its conjugation with atg5 and atg8 for its conjugation with
CC phosphatidylethanolamine. Both systems are needed for the atg8
CC association to autophagosomes membranes (By similarity). Required for
CC normal survival when exposed to pathogenic bacteria S.typhimurium by
CC promoting autophagic degradation of intracellular S.typhimurium
CC (PubMed:19667176). {ECO:0000250|UniProtKB:P38862,
CC ECO:0000269|PubMed:12626495, ECO:0000269|PubMed:19667176}.
CC -!- SUBUNIT: Homodimer. Interacts with atg8 through a thioester bond
CC between Cys-563 and the C-terminal 'Gly-120' of atg8 and with ATG12
CC through a thioester bond between Cys-563 and the C-terminal 'Gly-124'
CC of atg12 (By similarity). {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.
CC -!- DISRUPTION PHENOTYPE: Impaired survival when exposed to pathogenic
CC bacteria S.typhimurium associated with the accumulation of
CC S.typhimuriumin in large vacuoles which fail to undergo autophagy.
CC {ECO:0000269|PubMed:19667176}.
CC -!- SIMILARITY: Belongs to the ATG7 family. {ECO:0000305}.
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DR EMBL; AY191014; AAO39077.1; -; Genomic_DNA.
DR EMBL; AAFI02000006; EAL71880.1; -; Genomic_DNA.
DR RefSeq; XP_645809.1; XM_640717.1.
DR AlphaFoldDB; Q86CR9; -.
DR SMR; Q86CR9; -.
DR STRING; 44689.DDB0214819; -.
DR PaxDb; Q86CR9; -.
DR EnsemblProtists; EAL71880; EAL71880; DDB_G0271096.
DR GeneID; 8617799; -.
DR KEGG; ddi:DDB_G0271096; -.
DR dictyBase; DDB_G0271096; atg7.
DR eggNOG; KOG2337; Eukaryota.
DR HOGENOM; CLU_012998_2_1_1; -.
DR InParanoid; Q86CR9; -.
DR OMA; VQTWRYS; -.
DR PhylomeDB; Q86CR9; -.
DR Reactome; R-DDI-1632852; Macroautophagy.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q86CR9; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0019778; F:Atg12 activating enzyme activity; IBA:GO_Central.
DR GO; GO:0019779; F:Atg8 activating enzyme activity; IBA:GO_Central.
DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; ISS:dictyBase.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
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; IMP:dictyBase.
DR GO; GO:0042742; P:defense response to bacterium; IDA:dictyBase.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:dictyBase.
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 GO; GO:0010468; P:regulation of gene expression; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0044671; P:sorocarp spore cell differentiation; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
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; Reference proteome; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..707
FT /note="Ubiquitin-like modifier-activating enzyme atg7"
FT /id="PRO_0000327586"
FT REGION 686..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 368..373
FT /note="GXGXXG motif"
FT /evidence="ECO:0000250"
FT ACT_SITE 563
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 707 AA; 79859 MW; 3979C45675D4DEED CRC64;
MTNTLQFKEF SSFVNISFWH ELSNKKLDEL KLSEESIPLN GHYTFSPSQQ LDPFLCLEFN
AFLRNNVTNS TENQYVLPPR SYLSHGTLYN YNTVDDFKQS PKIKLFNDAS KRIWNDINNG
NIDKDTSLLN RFILLTYADI KNHQFYYMFG IPALLPSQPI QQFTEKPESI NIESLKSFSN
QILPQYFCLK QQQQESSTTT TTSFELIGSI EEKGNQYLNE CLENDLIPLV GFCDPCSLPL
NPGWPLRNFL IYLSIKYPML KKIKVLCYRG NGSTSNSILL SLELPSMGEQ LIKKQQEEDA
GEWSGKSVGW EKDSNGKIAP RFVSLASTMD PLKLAEQSVD LNLKLMRWRV MPSLELEKIK
TTSCLLLGSG TLGCNVARSL MSWGVRNITF VDSSKVSYSN PVRQSLFTFA DCSPKAKEKS
IAAADALKKI FPAINANAHV FSIPMPGHSV PQSEYQSIRN TIELLENLIK QHDVIYLLTD
SRESRWLPTM LSRAHGKLCI NAALGFDSYL VIRHGIKDQC QNELNPSISS KLGYQGSDLG
CYFCNDVIAP TDTLKDRTLD QMCTVTRPGL SMMASSIAVE LLISTIHHPY GGRAKGETET
DVYVQGSTPL GIIPHQLRGF ISHYQTLPLF SNPYKHCTAC SDYIIDEYNS KGFDFIINVM
NDSSCLTKIC GIDDLKNTEV NIDWDIDISD DDDDNNNNNN KEKNDDF
