ATG10_YEAST
ID ATG10_YEAST Reviewed; 167 AA.
AC Q07879; D6VXW4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ubiquitin-like-conjugating enzyme ATG10;
DE EC=2.3.2.-;
DE AltName: Full=Autophagy-related protein 10;
GN Name=ATG10; Synonyms=APG10; OrderedLocusNames=YLL042C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Marsischky G., Rolfs A., Richardson A., Kane M., Baqui M., Taycher E.,
RA Hu Y., Vannberg F., Weger J., Kramer J., Moreira D., Kelley F., Zuo D.,
RA Raphael J., Hogle C., Jepson D., Williamson J., Camargo A., Gonzaga L.,
RA Vasconcelos A.T., Simpson A.J.G., Kolodner R., Harlow E., LaBaer J.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=8224160; DOI=10.1016/0014-5793(93)80398-e;
RA Tsukada M., Ohsumi Y.;
RT "Isolation and characterization of autophagy-defective mutants of
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 333:169-174(1993).
RN [5]
RP FUNCTION.
RX PubMed=9759731; DOI=10.1038/26506;
RA Mizushima N., Noda T., Yoshimori T., Tanaka Y., Ishii T., George M.D.,
RA Klionsky D.J., Ohsumi M., Ohsumi Y.;
RT "A protein conjugation system essential for autophagy.";
RL Nature 395:395-398(1998).
RN [6]
RP FUNCTION, INTERACTION WITH ATG7 AND ATG12, AND MUTAGENESIS OF CYS-26;
RP CYS-133 AND CYS-137.
RX PubMed=10508157; DOI=10.1093/emboj/18.19.5234;
RA Shintani T., Mizushima N., Ogawa Y., Matsuura A., Noda T., Ohsumi Y.;
RT "Apg10p, a novel protein-conjugating enzyme essential for autophagy in
RT yeast.";
RL EMBO J. 18:5234-5241(1999).
RN [7]
RP FUNCTION.
RX PubMed=11689437; DOI=10.1093/emboj/20.21.5971;
RA Suzuki K., Kirisako T., Kamada Y., Mizushima N., Noda T., Ohsumi Y.;
RT "The pre-autophagosomal structure organized by concerted functions of APG
RT genes is essential for autophagosome formation.";
RL EMBO J. 20:5971-5981(2001).
RN [8]
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).
RN [9]
RP INTERACTION WITH ATG12.
RX PubMed=16874032; DOI=10.4161/auto.1.2.1858;
RA Hanada T., Ohsumi Y.;
RT "Structure-function relationship of Atg12, a ubiquitin-like modifier
RT essential for autophagy.";
RL Autophagy 1:110-118(2005).
RN [10]
RP CRYSTALLIZATION.
RX PubMed=17565192; DOI=10.1107/s1744309107017472;
RA Yamaguti M., Suzuki N.N., Fujioka Y., Ohsumi Y., Inagaki F.;
RT "Crystallization and preliminary X-ray analysis of Atg10.";
RL Acta Crystallogr. F 63:443-445(2007).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=17295840; DOI=10.1111/j.1365-2443.2007.01050.x;
RA Suzuki K., Kubota Y., Sekito T., Ohsumi Y.;
RT "Hierarchy of Atg proteins in pre-autophagosomal structure organization.";
RL Genes Cells 12:209-218(2007).
RN [12]
RP FUNCTION.
RX PubMed=18725539; DOI=10.1083/jcb.200801035;
RA Cao Y., Cheong H., Song H., Klionsky D.J.;
RT "In vivo reconstitution of autophagy in Saccharomyces cerevisiae.";
RL J. Cell Biol. 182:703-713(2008).
RN [13]
RP FUNCTION.
RX PubMed=18701704; DOI=10.1091/mbc.e08-04-0363;
RA Krick R., Muehe Y., Prick T., Bremer S., Schlotterhose P., Eskelinen E.L.,
RA Millen J., Goldfarb D.S., Thumm M.;
RT "Piecemeal microautophagy of the nucleus requires the core macroautophagy
RT genes.";
RL Mol. Biol. Cell 19:4492-4505(2008).
RN [14]
RP SUBUNIT.
RX PubMed=21193819;
RA Bae J.Y., Park H.H.;
RT "Purification and characterization of a ubiquitin-like system for
RT autophagosome formation.";
RL J. Microbiol. Biotechnol. 20:1647-1652(2010).
RN [15]
RP INTERACTION WITH ATG7.
RX PubMed=23142976; DOI=10.1038/nsmb.2415;
RA Kaiser S.E., Mao K., Taherbhoy A.M., Yu S., Olszewski J.L., Duda D.M.,
RA Kurinov I., Deng A., Fenn T.D., Klionsky D.J., Schulman B.A.;
RT "Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7-Atg3 and
RT Atg7-Atg10 structures.";
RL Nat. Struct. Mol. Biol. 19:1242-1249(2012).
RN [16]
RP INTERACTION WITH ATG7.
RX PubMed=22056771; DOI=10.1038/nsmb.2165;
RA Hong S.B., Kim B.W., Lee K.E., Kim S.W., Jeon H., Kim J., Song H.K.;
RT "Insights into noncanonical E1 enzyme activation from the structure of
RT autophagic E1 Atg7 with Atg8.";
RL Nat. Struct. Mol. Biol. 18:1323-1330(2011).
RN [17]
RP FUNCTION.
RX PubMed=22768199; DOI=10.1371/journal.pone.0040013;
RA Mijaljica D., Prescott M., Devenish R.J.;
RT "A late form of nucleophagy in Saccharomyces cerevisiae.";
RL PLoS ONE 7:E40013-E40013(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND INTERACTION WITH ATG7.
RX PubMed=22993095; DOI=10.1107/s0907444912034166;
RA Hong S.B., Kim B.W., Kim J.H., Song H.K.;
RT "Structure of the autophagic E2 enzyme Atg10.";
RL Acta Crystallogr. D 68:1409-1417(2012).
CC -!- FUNCTION: E2-like enzyme required for the cytoplasm to vacuole
CC transport (Cvt), autophagy and nucleophagy. Acts as an E2-like enzyme
CC that catalyzes the conjugation of ATG12 to ATG5. ATG12 conjugation to
CC ATG5 is required for proper localization of ATG8 to the
CC preautophagosomal structure (PAS). Likely serves as an ATG5-recognition
CC molecule. {ECO:0000269|PubMed:10508157, ECO:0000269|PubMed:11689437,
CC ECO:0000269|PubMed:18701704, ECO:0000269|PubMed:18725539,
CC ECO:0000269|PubMed:22768199, ECO:0000269|PubMed:8224160,
CC ECO:0000269|PubMed:9759731}.
CC -!- SUBUNIT: Forms homooligomers. Interacts with ATG7 and ATG12.
CC {ECO:0000269|PubMed:10508157, ECO:0000269|PubMed:16874032,
CC ECO:0000269|PubMed:21193819, ECO:0000269|PubMed:22056771,
CC ECO:0000269|PubMed:22993095, ECO:0000269|PubMed:23142976}.
CC -!- INTERACTION:
CC Q07879; P38862: ATG7; NbExp=7; IntAct=EBI-36629, EBI-2677;
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:17295840}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17295840}.
CC -!- SIMILARITY: Belongs to the ATG10 family. {ECO:0000305}.
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DR EMBL; Z73147; CAA97493.1; -; Genomic_DNA.
DR EMBL; AY558190; AAS56516.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09280.1; -; Genomic_DNA.
DR PIR; S64794; S64794.
DR RefSeq; NP_013058.1; NM_001181862.1.
DR PDB; 4EBR; X-ray; 2.70 A; A/B=1-167.
DR PDB; 4GSK; X-ray; 2.90 A; Y/Z=1-167.
DR PDBsum; 4EBR; -.
DR PDBsum; 4GSK; -.
DR AlphaFoldDB; Q07879; -.
DR SMR; Q07879; -.
DR BioGRID; 31271; 135.
DR DIP; DIP-4842N; -.
DR IntAct; Q07879; 3.
DR STRING; 4932.YLL042C; -.
DR PaxDb; Q07879; -.
DR EnsemblFungi; YLL042C_mRNA; YLL042C; YLL042C.
DR GeneID; 850684; -.
DR KEGG; sce:YLL042C; -.
DR SGD; S000003965; ATG10.
DR VEuPathDB; FungiDB:YLL042C; -.
DR eggNOG; ENOG502S7IG; Eukaryota.
DR HOGENOM; CLU_114192_0_0_1; -.
DR InParanoid; Q07879; -.
DR OMA; CDTDANV; -.
DR BioCyc; YEAST:G3O-32143-MON; -.
DR PRO; PR:Q07879; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07879; protein.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019777; F:Atg12 transferase activity; IMP:SGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0044805; P:late nucleophagy; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IMP:SGD.
DR InterPro; IPR016524; Atg10.
DR InterPro; IPR007135; Atg3/Atg10.
DR Pfam; PF03987; Autophagy_act_C; 1.
DR PIRSF; PIRSF007802; Autophagy-rel_ATG10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Membrane; Protein transport; Reference proteome;
KW Transferase; Transport; Ubl conjugation pathway.
FT CHAIN 1..167
FT /note="Ubiquitin-like-conjugating enzyme ATG10"
FT /id="PRO_0000096190"
FT ACT_SITE 133
FT /note="Glycyl thioester intermediate"
FT MUTAGEN 26
FT /note="C->S: No effect on conjugating activity. Normal
FT autophagic activity."
FT /evidence="ECO:0000269|PubMed:10508157"
FT MUTAGEN 133
FT /note="C->A: Complete loss of covalent binding to ATG12."
FT /evidence="ECO:0000269|PubMed:10508157"
FT MUTAGEN 133
FT /note="C->S: Strong decrease of binding to ATG12. No more
FT formation of ATG12-ATG5 conjugate. Defect in autophagy."
FT /evidence="ECO:0000269|PubMed:10508157"
FT MUTAGEN 137
FT /note="C->S: No effect on conjugating activity. Normal
FT autophagic activity."
FT /evidence="ECO:0000269|PubMed:10508157"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:4EBR"
FT TURN 17..22
FT /evidence="ECO:0007829|PDB:4EBR"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:4EBR"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:4GSK"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:4EBR"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:4GSK"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:4EBR"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:4EBR"
FT STRAND 75..88
FT /evidence="ECO:0007829|PDB:4EBR"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:4EBR"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:4EBR"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:4EBR"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:4EBR"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:4EBR"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:4EBR"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:4EBR"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:4EBR"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:4EBR"
SQ SEQUENCE 167 AA; 19760 MW; 9B90684B8D3D26C5 CRC64;
MIPYQEWHSQ LQSLYDSQIF HNWALCQDVH LNDEKDGLLL RLIPTRQLQK NTERIENKLL
NHIELYLTYS KVYNEPLLLL RIWEEKSIDG IPMTKLMLPT DIESLLDVQG KFQLGLDTII
NLEGSVWYSF HPCDTSCIVG DQAEFMSTYL RRWVSIFIFS WLGYEDS
