ATG10_KLUMD
ID ATG10_KLUMD Reviewed; 147 AA.
AC W0TH64; J3QW31;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Ubiquitin-like-conjugating enzyme ATG10 {ECO:0000250|UniProtKB:Q07879};
DE EC=2.3.2.- {ECO:0000250|UniProtKB:Q07879};
DE AltName: Full=Autophagy-related protein 10 {ECO:0000303|PubMed:26442587};
GN Name=ATG10 {ECO:0000303|PubMed:26442587}; ORFNames=KLMA_80409;
OS Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1003335;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275;
RX PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA Matsutani M., Murata M., Fujimoto N., Suprayogi X., Tsuchikane K.,
RA Limtong S., Fujita N., Yamada M.;
RT "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT complete genome sequence and transcriptome analyses.";
RL Biotechnol. Biofuels 8:47-47(2015).
RN [2]
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26442587; DOI=10.1074/jbc.m115.684233;
RA Yamamoto H., Shima T., Yamaguchi M., Mochizuki Y., Hoshida H., Kakuta S.,
RA Kondo-Kakuta C., Noda N.N., Inagaki F., Itoh T., Akada R., Ohsumi Y.;
RT "The thermotolerant yeast Kluyveromyces marxianus is a useful organism for
RT structural and biochemical studies of autophagy.";
RL J. Biol. Chem. 290:29506-29518(2015).
RN [3] {ECO:0000312|PDB:2LPU, ECO:0007744|PDB:2LPU, ECO:0007744|PDB:3VX7}
RP STRUCTURE BY NMR, X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), INTERACTION WITH
RP ATG5, FUNCTION, ACTIVE SITE, MUTAGENESIS OF TYR-56; THR-99; TYR-110;
RP ASN-114; CYS-116 AND THR-118, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22682742; DOI=10.1016/j.str.2012.04.018;
RA Yamaguchi M., Noda N.N., Yamamoto H., Shima T., Kumeta H., Kobashigawa Y.,
RA Akada R., Ohsumi Y., Inagaki F.;
RT "Structural insights into Atg10-mediated formation of the autophagy-
RT essential Atg12-Atg5 conjugate.";
RL Structure 20:1244-1254(2012).
CC -!- FUNCTION: E2-like enzyme required for the cytoplasm to vacuole
CC transport (Cvt), autophagy and nucleophagy (PubMed:26442587,
CC PubMed:22682742). Acts as an E2-like enzyme that catalyzes the
CC conjugation of ATG12 to ATG5 (PubMed:22682742). ATG12 conjugation to
CC ATG5 is required for proper localization of ATG8 to the
CC preautophagosomal structure (PAS) (By similarity). Likely serves as an
CC ATG5-recognition molecule (By similarity).
CC {ECO:0000250|UniProtKB:Q07879, ECO:0000269|PubMed:22682742,
CC ECO:0000269|PubMed:26442587}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for or ATG12-ATG5 conjugation {ECO:0000269|PubMed:22682742};
CC -!- SUBUNIT: Forms homooligomers (By similarity). Interacts with ATG10
CC (PubMed:22682742). Interacts with ATG7 and ATG12 (By similarity).
CC {ECO:0000250|UniProtKB:Q07879, ECO:0000269|PubMed:22682742}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q07879}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q07879}.
CC -!- DISRUPTION PHENOTYPE: Impairs the formation of preautophagosomal
CC structures (PubMed:26442587). {ECO:0000269|PubMed:26442587}.
CC -!- MISCELLANEOUS: Kluyveromyces marxianus proteins are shorter in length
CC and have a more ordered secondary structure than their S.cerevisiae
CC counterparts, which might contribute to the superior thermotolerance
CC and solubility (PubMed:26442587). K.marxianus could be therefore useful
CC as a new model organism for further elucidation of the molecular
CC details of autophagy (PubMed:26442587). {ECO:0000269|PubMed:26442587}.
CC -!- SIMILARITY: Belongs to the ATG10 family. {ECO:0000305}.
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DR EMBL; AP012220; BAO42720.1; -; Genomic_DNA.
DR PDB; 2LPU; NMR; -; A=1-147.
DR PDB; 3VX7; X-ray; 3.20 A; B=1-147.
DR PDBsum; 2LPU; -.
DR PDBsum; 3VX7; -.
DR AlphaFoldDB; W0TH64; -.
DR SMR; W0TH64; -.
DR EnsemblFungi; BAO42720; BAO42720; KLMA_80409.
DR OrthoDB; 1600752at2759; -.
DR Proteomes; UP000065495; Chromosome 8.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR007135; Atg3/Atg10.
DR Pfam; PF03987; Autophagy_act_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Membrane; Protein transport; Transferase;
KW Transport; Ubl conjugation pathway.
FT CHAIN 1..147
FT /note="Ubiquitin-like-conjugating enzyme ATG10"
FT /id="PRO_0000443900"
FT ACT_SITE 116
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q07879"
FT MUTAGEN 56
FT /note="Y->A: Forms the ATG12-ATG10 intermediate, but
FT reduces the formation of the ATG12-ATG5 conjugate."
FT /evidence="ECO:0000269|PubMed:22682742"
FT MUTAGEN 99
FT /note="T->A: Forms the ATG12-ATG10 intermediate, but
FT reduces the formation of the ATG12-ATG5 conjugate."
FT /evidence="ECO:0000269|PubMed:22682742"
FT MUTAGEN 110
FT /note="Y->A: Reduces the formation of the ATG12-ATG5
FT conjugate."
FT /evidence="ECO:0000269|PubMed:22682742"
FT MUTAGEN 114
FT /note="N->A: Forms the ATG12-ATG10 intermediate, but
FT reduces the formation of the ATG12-ATG5 conjugate."
FT /evidence="ECO:0000269|PubMed:22682742"
FT MUTAGEN 116
FT /note="C->A: Impairs the formation of the ATG12-ATG5
FT conjugate."
FT /evidence="ECO:0000269|PubMed:22682742"
FT MUTAGEN 118
FT /note="T->A: Forms the ATG12-ATG10 intermediate, but
FT reduces the formation of the ATG12-ATG5 conjugate."
FT /evidence="ECO:0000269|PubMed:22682742"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:3VX7"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:3VX7"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:3VX7"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:3VX7"
FT STRAND 54..70
FT /evidence="ECO:0007829|PDB:3VX7"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:3VX7"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:3VX7"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:3VX7"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:3VX7"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:3VX7"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:2LPU"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:3VX7"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3VX7"
SQ SEQUENCE 147 AA; 17310 MW; EF67729C426AD426 CRC64;
MLTLPEYNEQ IPNVRSLLTK WAKVERIQDV QDGLQLDVRL KTDTLLELHI YYDHVYHVPS
IKFRLWSLDT EEDISSLRLL TLSDSELRSI LNLGTFSVTL STDMEMKSVY YYINNCDTDA
NVGSDVEHYL TRWISLYIRI FDLNFVP
