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Protein

Autophagy-related protein 32

Gene

ATG32

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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 - Biological processi

  • 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 Componenti: Chromosome IX

Organism-specific databases

CYGDiYIL146c.
EuPathDBiFungiDB:YIL146C.
SGDiS000001408. ATG32.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei390 – 41425HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

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 32PRO_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 PBS2.1 Publication

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. 53 interactions.
IntActiP40458. 6 interactions.
MINTiMINT-2781265.
STRINGi4932.YIL146C.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VXWX-ray3.00B85-90[»]
ProteinModelPortaliP40458.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATG32 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG44523.
InParanoidiP40458.
KOiK17984.
OMAiNDINTHT.
OrthoDBiEOG7SN8QQ.

Sequencei

Sequence statusi: Complete.

P40458-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLEYQQREG KGSSSKSMPP DSSSTTIHTC SEAQTGEDKG LLDPHLSVLE
60 70 80 90 100
LLSKTGHSPS PMGQNLVTSI DISGNHNVND SISGSWQAIQ PLDLGASFIP
110 120 130 140 150
ERCSSQTTNG SILSSSDTSE EEQELLQAPA ADIINIIKQG QEGANVVSPS
160 170 180 190 200
HPFKQLQKII SLPLPGKEKT PFNEQDDDGD EDEAFEEDSV TITKSLTSST
210 220 230 240 250
NSFVMPKLSL TQKNPVFRLL ILGRTGSSFY QSIPKEYQSL FELPKYHDSA
260 270 280 290 300
TFPQYTGIVI IFQELREMVS LLNRIVQYSQ GKPVIPICQP GQVIQVKNVL
310 320 330 340 350
KSFLRNKLVK LLFPPVVVTN KRDLKKMFQR LQDLSLEYGE DVNEEDNDDE
360 370 380 390 400
AIHTKSRSYC RNKKAENSKK KSPKSNKKPK RKKQKFFTSW FTWGISITIG
410 420 430 440 450
ISFGCCVTYF VTAAYEHQTV KSLSLRPSIL ASLLSLDSSS DTINTPATAS
460 470 480 490 500
PSSTEQFLWF DKGTLQINFH SDGFIMKSLT IIKETWGKMN TFVLHALSKP
510 520
LKFLENLNKS SEFSIDESNR ILALGYILL
Length:529
Mass (Da):58,969
Last modified:February 1, 1995 - v1
Checksum:iDB6A3DAFD50FB619
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VXWX-ray3.00B85-90[»]
ProteinModelPortaliP40458.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34846. 53 interactions.
IntActiP40458. 6 interactions.
MINTiMINT-2781265.
STRINGi4932.YIL146C.

Proteomic databases

MaxQBiP40458.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYIL146c.
EuPathDBiFungiDB:YIL146C.
SGDiS000001408. ATG32.

Phylogenomic databases

eggNOGiNOG44523.
InParanoidiP40458.
KOiK17984.
OMAiNDINTHT.
OrthoDBiEOG7SN8QQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-31395-MONOMER.

Miscellaneous databases

NextBioi977229.
PROiP40458.

Gene expression databases

GenevestigatoriP40458.

Family and domain databases

ProtoNetiSearch...

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: April 29, 2015
This is version 100 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.