ATG10_ARATH
ID ATG10_ARATH Reviewed; 225 AA.
AC Q8VZ52; F4JEH1;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Ubiquitin-like-conjugating enzyme ATG10;
DE EC=2.3.2.-;
DE AltName: Full=Autophagy-related protein 10;
DE Short=AtATG10;
GN Name=ATG10; OrderedLocusNames=At3g07525; ORFNames=F21O3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18245858; DOI=10.1534/genetics.107.086199;
RA Phillips A.R., Suttangkakul A., Vierstra R.D.;
RT "The ATG12-conjugating enzyme ATG10 is essential for autophagic vesicle
RT formation in Arabidopsis thaliana.";
RL Genetics 178:1339-1353(2008).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20085894; DOI=10.1093/mp/ssp071;
RA Pourcel L., Irani N.G., Lu Y., Riedl K., Schwartz S., Grotewold E.;
RT "The formation of anthocyanic vacuolar inclusions in Arabidopsis thaliana
RT and implications for the sequestration of anthocyanin pigments.";
RL Mol. Plant 3:78-90(2010).
RN [6]
RP FUNCTION IN PLANT DEFENSE, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21332848; DOI=10.1111/j.1365-313x.2011.04546.x;
RA Lenz H.D., Haller E., Melzer E., Kober K., Wurster K., Stahl M.,
RA Bassham D.C., Vierstra R.D., Parker J.E., Bautor J., Molina A.,
RA Escudero V., Shindo T., van der Hoorn R.A., Gust A.A., Nuernberger T.;
RT "Autophagy differentially controls plant basal immunity to biotrophic and
RT necrotrophic pathogens.";
RL Plant J. 66:818-830(2011).
RN [7]
RP INDUCTION BY BOTRYTIS CINEREA.
RC STRAIN=cv. Columbia;
RX PubMed=21395886; DOI=10.1111/j.1365-313x.2011.04553.x;
RA Lai Z., Wang F., Zheng Z., Fan B., Chen Z.;
RT "A critical role of autophagy in plant resistance to necrotrophic fungal
RT pathogens.";
RL Plant J. 66:953-968(2011).
RN [8]
RP FUNCTION IN PLANT DEFENSE, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21645148; DOI=10.1111/j.1365-313x.2011.04669.x;
RA Wang Y., Nishimura M.T., Zhao T., Tang D.;
RT "ATG2, an autophagy-related protein, negatively affects powdery mildew
RT resistance and mildew-induced cell death in Arabidopsis.";
RL Plant J. 68:74-87(2011).
CC -!- FUNCTION: E2-like enzyme involved in autophagy. Acts as an E2-like
CC enzyme that catalyzes the conjugation of ATG12 to ATG5. The ATG12-ATG5
CC conjugates is required for the formation of autophagic vesicles and for
CC the timely progression of senescence and programmed cell death (PCD).
CC Likely serves as an ATG5-recognition molecule. Confers some resistance
CC to nitrogen and carbon starvation. Is also involved in the formation of
CC anthocyanic vacuolar inclusions (AVI). Promotes an autophagic process
CC that constitutes a pro-survival mechanism by controlling the
CC containment of host tissue-destructive microbial infections during
CC necrotrophic pathogen infection, but negatively controls SA-dependent
CC defenses and basal immunity to bacterial infection during biotrophic
CC infection. {ECO:0000269|PubMed:18245858, ECO:0000269|PubMed:20085894,
CC ECO:0000269|PubMed:21332848, ECO:0000269|PubMed:21645148}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VZ52-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VZ52-2; Sequence=VSP_053427;
CC -!- INDUCTION: Slightly induced upon B.cinerea infection.
CC {ECO:0000269|PubMed:21395886}.
CC -!- DISRUPTION PHENOTYPE: Mutant atg10-1 cannot form the ATG12-ATG5
CC conjugate and fails to accumulate autophagic bodies inside the vacuole.
CC Plants are hypersensitive to nitrogen and carbon starvation and
CC initiate senescence and programmed cell death (PCD) more quickly.
CC Reduced anthocyanin levels under anthocyanin-inductive conditions.
CC Development of spreading necrosis upon infection with the necrotrophic
CC fungal pathogen, A.brassicicola, which is accompanied by the production
CC of reactive oxygen intermediates and by enhanced hyphal growth. By
CC contrast, in response to the virulent biotrophic phytopathogen,
CC P.syringae pv. tomato, plants exhibit a marked resistance without
CC spreading necrosis. Enhanced powdery mildew (e.g. G.cichoracearum)
CC resistance. {ECO:0000269|PubMed:18245858, ECO:0000269|PubMed:20085894,
CC ECO:0000269|PubMed:21332848, ECO:0000269|PubMed:21645148}.
CC -!- SIMILARITY: Belongs to the ATG10 family. {ECO:0000305}.
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DR EMBL; AC009853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE74555.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74556.1; -; Genomic_DNA.
DR EMBL; AY065244; AAL38720.1; -; mRNA.
DR EMBL; AY142587; AAN13156.1; -; mRNA.
DR RefSeq; NP_850532.1; NM_180201.3. [Q8VZ52-1]
DR RefSeq; NP_850533.1; NM_180202.1. [Q8VZ52-2]
DR AlphaFoldDB; Q8VZ52; -.
DR SMR; Q8VZ52; -.
DR BioGRID; 5276; 4.
DR IntAct; Q8VZ52; 4.
DR STRING; 3702.AT3G07525.2; -.
DR TCDB; 9.A.15.3.1; the autophagy-related phagophore-formation transporter (apt) family.
DR PaxDb; Q8VZ52; -.
DR PRIDE; Q8VZ52; -.
DR DNASU; 819941; -.
DR EnsemblPlants; AT3G07525.1; AT3G07525.1; AT3G07525. [Q8VZ52-1]
DR EnsemblPlants; AT3G07525.2; AT3G07525.2; AT3G07525. [Q8VZ52-2]
DR GeneID; 819941; -.
DR Gramene; AT3G07525.1; AT3G07525.1; AT3G07525. [Q8VZ52-1]
DR Gramene; AT3G07525.2; AT3G07525.2; AT3G07525. [Q8VZ52-2]
DR KEGG; ath:AT3G07525; -.
DR Araport; AT3G07525; -.
DR TAIR; locus:1005716578; AT3G07525.
DR eggNOG; KOG4741; Eukaryota.
DR HOGENOM; CLU_072332_3_0_1; -.
DR OMA; CDFHIVY; -.
DR PhylomeDB; Q8VZ52; -.
DR PRO; PR:Q8VZ52; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VZ52; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IMP:TAIR.
DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IMP:TAIR.
DR GO; GO:0043482; P:cellular pigment accumulation; IMP:UniProtKB.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IMP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0090549; P:response to carbon starvation; IMP:UniProtKB.
DR InterPro; IPR007135; Atg3/Atg10.
DR PANTHER; PTHR12866; PTHR12866; 1.
DR Pfam; PF03987; Autophagy_act_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Membrane; Plant defense;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway.
FT CHAIN 1..225
FT /note="Ubiquitin-like-conjugating enzyme ATG10"
FT /id="PRO_0000424379"
FT TRANSMEM 200..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 178
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255"
FT VAR_SEQ 53
FT /note="K -> KQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053427"
SQ SEQUENCE 225 AA; 25621 MW; AAC18740D3B1C7C6 CRC64;
MDSAREVSDG RLTVEGFSVA SRAFADKWKI HNQSFPPWSW VPLINRTLLV SKKEEGYLSL
EKIIILSSLE EEIPEDESLN VATDCLEKEE TVDHTILVPT MENEAHYYDF HIVYSASYKV
PVLYFRGYCS GGEPLALDVI KKDVPSCSVS LLLESKWTFI TQEEHPYLNR PWFKLHPCGT
EDWIKLLSQS SSSSGCQMPI VLYLVSWFSV VGQVVGLRIP LEMLN
