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P40458

- ATG32_YEAST

UniProt

P40458 - ATG32_YEAST

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Protein
Autophagy-related protein 32
Gene
ATG32, ECM17, YIL146C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Mitophagy-specific receptor that recruits the autophagic machinery to mitochondria and regulates selective degradation of mitochondria. Mitophagy contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Recruits ATG11 to the surface of mitochondria. Promotes also autophagy-dependent peroxisome degradation.9 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. mitochondrion degradation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Autophagy

Enzyme and pathway databases

BioCyciYEAST:G3O-31395-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Autophagy-related protein 32
Alternative name(s):
Extracellular mutant protein 37
Gene namesi
Name:ATG32
Synonyms:ECM17
Ordered Locus Names:YIL146C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IX

Organism-specific databases

CYGDiYIL146c.
SGDiS000001408. ATG32.

Subcellular locationi

Mitochondrion outer membrane; Single-pass membrane protein. Vacuole membrane; Single-pass membrane protein. Preautophagosomal structure membrane; Single-pass membrane protein
Note: Is recruited to the preautophagosomal structure during mitophagy and imported into the vacuole along with mitochondria during starvation.4 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei390 – 41425Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of mitochondrial outer membrane Source: SGD
  2. pre-autophagosomal structure membrane Source: UniProtKB-SubCell
  3. vacuolar membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141S → A, N, G or Y: Abolishes mitophagy and impairs interaction with ATG11. 1 Publication
Mutagenesisi119 – 1191S → A: Decreases mitophagy and impairs interaction with ATG11. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Autophagy-related protein 32
PRO_0000086920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141Phosphoserine1 Publication
Modified residuei119 – 1191Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation of Ser-114 and Ser-119 are critically important for mitophagy and for the ATG11-ATG32 interaction. Phosphorylation depends on both HOG1 and PBS2.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40458.

Expressioni

Gene expression databases

GenevestigatoriP40458.

Interactioni

Subunit structurei

interacts with ATG8 and ATG11.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATG11Q125272EBI-25256,EBI-31977
CKA1P157902EBI-25256,EBI-9533

Protein-protein interaction databases

BioGridi34846. 52 interactions.
IntActiP40458. 6 interactions.
MINTiMINT-2781265.
STRINGi4932.YIL146C.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VXWX-ray3.00B85-90[»]
ProteinModelPortaliP40458.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATG32 family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG44523.
KOiK17984.
OrthoDBiEOG7SN8QQ.

Sequencei

Sequence statusi: Complete.

P40458-1 [UniParc]FASTAAdd to Basket

« Hide

MVLEYQQREG KGSSSKSMPP DSSSTTIHTC SEAQTGEDKG LLDPHLSVLE    50
LLSKTGHSPS PMGQNLVTSI DISGNHNVND SISGSWQAIQ PLDLGASFIP 100
ERCSSQTTNG SILSSSDTSE EEQELLQAPA ADIINIIKQG QEGANVVSPS 150
HPFKQLQKII SLPLPGKEKT PFNEQDDDGD EDEAFEEDSV TITKSLTSST 200
NSFVMPKLSL TQKNPVFRLL ILGRTGSSFY QSIPKEYQSL FELPKYHDSA 250
TFPQYTGIVI IFQELREMVS LLNRIVQYSQ GKPVIPICQP GQVIQVKNVL 300
KSFLRNKLVK LLFPPVVVTN KRDLKKMFQR LQDLSLEYGE DVNEEDNDDE 350
AIHTKSRSYC RNKKAENSKK KSPKSNKKPK RKKQKFFTSW FTWGISITIG 400
ISFGCCVTYF VTAAYEHQTV KSLSLRPSIL ASLLSLDSSS DTINTPATAS 450
PSSTEQFLWF DKGTLQINFH SDGFIMKSLT IIKETWGKMN TFVLHALSKP 500
LKFLENLNKS SEFSIDESNR ILALGYILL 529
Length:529
Mass (Da):58,969
Last modified:February 1, 1995 - v1
Checksum:iDB6A3DAFD50FB619
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z38059 Genomic DNA. Translation: CAA86132.1.
AY692933 Genomic DNA. Translation: AAT92952.1.
BK006942 Genomic DNA. Translation: DAA08407.1.
PIRiS48388.
RefSeqiNP_012120.1. NM_001179494.1.

Genome annotation databases

EnsemblFungiiYIL146C; YIL146C; YIL146C.
GeneIDi854660.
KEGGisce:YIL146C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z38059 Genomic DNA. Translation: CAA86132.1 .
AY692933 Genomic DNA. Translation: AAT92952.1 .
BK006942 Genomic DNA. Translation: DAA08407.1 .
PIRi S48388.
RefSeqi NP_012120.1. NM_001179494.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3VXW X-ray 3.00 B 85-90 [» ]
ProteinModelPortali P40458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34846. 52 interactions.
IntActi P40458. 6 interactions.
MINTi MINT-2781265.
STRINGi 4932.YIL146C.

Proteomic databases

MaxQBi P40458.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YIL146C ; YIL146C ; YIL146C .
GeneIDi 854660.
KEGGi sce:YIL146C.

Organism-specific databases

CYGDi YIL146c.
SGDi S000001408. ATG32.

Phylogenomic databases

eggNOGi NOG44523.
KOi K17984.
OrthoDBi EOG7SN8QQ.

Enzyme and pathway databases

BioCyci YEAST:G3O-31395-MONOMER.

Miscellaneous databases

NextBioi 977229.

Gene expression databases

Genevestigatori P40458.

Family and domain databases

ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae."
    Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J., Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C., Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M., Davies J., Klis F.M., Robbins P.W., Bussey H.
    Genetics 147:435-450(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  5. "A landmark protein essential for mitophagy: Atg32 recruits the autophagic machinery to mitochondria."
    Okamoto K., Kondo-Okamoto N., Ohsumi Y.
    Autophagy 5:1203-1205(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy."
    Okamoto K., Kondo-Okamoto N., Ohsumi Y.
    Dev. Cell 17:87-97(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH ATG8 AND ATG11.
  7. "Atg32 is a mitochondrial protein that confers selectivity during mitophagy."
    Kanki T., Wang K., Cao Y., Baba M., Klionsky D.J.
    Dev. Cell 17:98-109(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH ATG11.
  8. "A genomic screen for yeast mutants defective in selective mitochondria autophagy."
    Kanki T., Wang K., Baba M., Bartholomew C.R., Lynch-Day M.A., Du Z., Geng J., Mao K., Yang Z., Yen W.L., Klionsky D.J.
    Mol. Biol. Cell 20:4730-4738(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Two MAPK-signaling pathways are required for mitophagy in Saccharomyces cerevisiae."
    Mao K., Wang K., Zhao M., Xu T., Klionsky D.J.
    J. Cell Biol. 193:755-767(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Phosphorylation of Serine 114 on Atg32 mediates mitophagy."
    Aoki Y., Kanki T., Hirota Y., Kurihara Y., Saigusa T., Uchiumi T., Kang D.
    Mol. Biol. Cell 22:3206-3217(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATG8 AND ATG11, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-114 AND SER-119, MUTAGENESIS OF SER-114 AND SER-119.
  11. "SNCA (alpha-synuclein)-induced toxicity in yeast cells is dependent on sirtuin 2 (Sir2)-mediated mitophagy."
    Sampaio-Marques B., Felgueiras C., Silva A., Rodrigues M., Tenreiro S., Franssens V., Reichert A.S., Outeiro T.F., Winderickx J., Ludovico P.
    Autophagy 8:1494-1509(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae."
    Motley A.M., Nuttall J.M., Hettema E.H.
    EMBO J. 31:2852-2868(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Mitophagy plays an essential role in reducing mitochondrial production of reactive oxygen species and mutation of mitochondrial DNA by maintaining mitochondrial quantity and quality in yeast."
    Kurihara Y., Kanki T., Aoki Y., Hirota Y., Saigusa T., Uchiumi T., Kang D.
    J. Biol. Chem. 287:3265-3272(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Autophagy-related protein 32 acts as autophagic degron and directly initiates mitophagy."
    Kondo-Okamoto N., Noda N.N., Suzuki S.W., Nakatogawa H., Takahashi I., Matsunami M., Hashimoto A., Inagaki F., Ohsumi Y., Okamoto K.
    J. Biol. Chem. 287:10631-10638(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 85-90, FUNCTION, INTERACTION WITH ATG8 AND ATG11.

Entry informationi

Entry nameiATG32_YEAST
AccessioniPrimary (citable) accession number: P40458
Secondary accession number(s): D6VVE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

External Data

Dasty 3

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