ATG32_YEAST
ID ATG32_YEAST Reviewed; 529 AA.
AC P40458; D6VVE1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Autophagy-related protein 32;
DE AltName: Full=Extracellular mutant protein 37;
GN Name=ATG32; Synonyms=ECM17; OrderedLocusNames=YIL146C;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP IDENTIFICATION.
RX PubMed=9335584; DOI=10.1093/genetics/147.2.435;
RA Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J.,
RA Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C.,
RA Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M.,
RA Davies J., Klis F.M., Robbins P.W., Bussey H.;
RT "Large scale identification of genes involved in cell surface biosynthesis
RT and architecture in Saccharomyces cerevisiae.";
RL Genetics 147:435-450(1997).
RN [5]
RP FUNCTION.
RX PubMed=19770589; DOI=10.4161/auto.5.8.9830;
RA Okamoto K., Kondo-Okamoto N., Ohsumi Y.;
RT "A landmark protein essential for mitophagy: Atg32 recruits the autophagic
RT machinery to mitochondria.";
RL Autophagy 5:1203-1205(2009).
RN [6]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH ATG8 AND ATG11.
RX PubMed=19619494; DOI=10.1016/j.devcel.2009.06.013;
RA Okamoto K., Kondo-Okamoto N., Ohsumi Y.;
RT "Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria
RT via selective autophagy.";
RL Dev. Cell 17:87-97(2009).
RN [7]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH ATG11.
RX PubMed=19619495; DOI=10.1016/j.devcel.2009.06.014;
RA Kanki T., Wang K., Cao Y., Baba M., Klionsky D.J.;
RT "Atg32 is a mitochondrial protein that confers selectivity during
RT mitophagy.";
RL Dev. Cell 17:98-109(2009).
RN [8]
RP FUNCTION.
RX PubMed=19793921; DOI=10.1091/mbc.e09-03-0225;
RA Kanki T., Wang K., Baba M., Bartholomew C.R., Lynch-Day M.A., Du Z.,
RA Geng J., Mao K., Yang Z., Yen W.L., Klionsky D.J.;
RT "A genomic screen for yeast mutants defective in selective mitochondria
RT autophagy.";
RL Mol. Biol. Cell 20:4730-4738(2009).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21576396; DOI=10.1083/jcb.201102092;
RA Mao K., Wang K., Zhao M., Xu T., Klionsky D.J.;
RT "Two MAPK-signaling pathways are required for mitophagy in Saccharomyces
RT cerevisiae.";
RL J. Cell Biol. 193:755-767(2011).
RN [10]
RP INTERACTION WITH ATG8 AND ATG11, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP SER-114 AND SER-119, AND MUTAGENESIS OF SER-114 AND SER-119.
RX PubMed=21757540; DOI=10.1091/mbc.e11-02-0145;
RA Aoki Y., Kanki T., Hirota Y., Kurihara Y., Saigusa T., Uchiumi T., Kang D.;
RT "Phosphorylation of Serine 114 on Atg32 mediates mitophagy.";
RL Mol. Biol. Cell 22:3206-3217(2011).
RN [11]
RP FUNCTION.
RX PubMed=22914317; DOI=10.4161/auto.21275;
RA Sampaio-Marques B., Felgueiras C., Silva A., Rodrigues M., Tenreiro S.,
RA Franssens V., Reichert A.S., Outeiro T.F., Winderickx J., Ludovico P.;
RT "SNCA (alpha-synuclein)-induced toxicity in yeast cells is dependent on
RT sirtuin 2 (Sir2)-mediated mitophagy.";
RL Autophagy 8:1494-1509(2012).
RN [12]
RP FUNCTION.
RX PubMed=22643220; DOI=10.1038/emboj.2012.151;
RA Motley A.M., Nuttall J.M., Hettema E.H.;
RT "Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces
RT cerevisiae.";
RL EMBO J. 31:2852-2868(2012).
RN [13]
RP FUNCTION.
RX PubMed=22157017; DOI=10.1074/jbc.m111.280156;
RA Kurihara Y., Kanki T., Aoki Y., Hirota Y., Saigusa T., Uchiumi T., Kang D.;
RT "Mitophagy plays an essential role in reducing mitochondrial production of
RT reactive oxygen species and mutation of mitochondrial DNA by maintaining
RT mitochondrial quantity and quality in yeast.";
RL J. Biol. Chem. 287:3265-3272(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 85-90, FUNCTION, AND INTERACTION
RP WITH ATG8 AND ATG11.
RX PubMed=22308029; DOI=10.1074/jbc.m111.299917;
RA Kondo-Okamoto N., Noda N.N., Suzuki S.W., Nakatogawa H., Takahashi I.,
RA Matsunami M., Hashimoto A., Inagaki F., Ohsumi Y., Okamoto K.;
RT "Autophagy-related protein 32 acts as autophagic degron and directly
RT initiates mitophagy.";
RL J. Biol. Chem. 287:10631-10638(2012).
CC -!- FUNCTION: Mitophagy-specific receptor that recruits the autophagic
CC machinery to mitochondria and regulates selective degradation of
CC mitochondria. Mitophagy contributes to regulate mitochondrial quantity
CC and quality by eliminating the mitochondria to a basal level to fulfill
CC cellular energy requirements and preventing excess ROS production.
CC Recruits ATG11 to the surface of mitochondria. Promotes also autophagy-
CC dependent peroxisome degradation. {ECO:0000269|PubMed:19619494,
CC ECO:0000269|PubMed:19619495, ECO:0000269|PubMed:19770589,
CC ECO:0000269|PubMed:19793921, ECO:0000269|PubMed:21576396,
CC ECO:0000269|PubMed:22157017, ECO:0000269|PubMed:22308029,
CC ECO:0000269|PubMed:22643220, ECO:0000269|PubMed:22914317}.
CC -!- SUBUNIT: interacts with ATG8 and ATG11. {ECO:0000269|PubMed:19619494,
CC ECO:0000269|PubMed:19619495, ECO:0000269|PubMed:21757540,
CC ECO:0000269|PubMed:22308029}.
CC -!- INTERACTION:
CC P40458; Q12527: ATG11; NbExp=2; IntAct=EBI-25256, EBI-31977;
CC P40458; P15790: CKA1; NbExp=2; IntAct=EBI-25256, EBI-9533;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC membrane protein. Vacuole membrane; Single-pass membrane protein.
CC Preautophagosomal structure membrane; Single-pass membrane protein.
CC Note=Is recruited to the preautophagosomal structure during mitophagy
CC and imported into the vacuole along with mitochondria during
CC starvation.
CC -!- PTM: Phosphorylation of Ser-114 and Ser-119 are critically important
CC for mitophagy and for the ATG11-ATG32 interaction. Phosphorylation
CC depends on both HOG1 and PBS2. {ECO:0000269|PubMed:21757540}.
CC -!- SIMILARITY: Belongs to the ATG32 family. {ECO:0000305}.
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DR EMBL; Z38059; CAA86132.1; -; Genomic_DNA.
DR EMBL; AY692933; AAT92952.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08407.1; -; Genomic_DNA.
DR PIR; S48388; S48388.
DR RefSeq; NP_012120.1; NM_001179494.1.
DR PDB; 3VXW; X-ray; 3.00 A; B=85-90.
DR PDB; 5WLP; NMR; -; A=200-341.
DR PDBsum; 3VXW; -.
DR PDBsum; 5WLP; -.
DR AlphaFoldDB; P40458; -.
DR SMR; P40458; -.
DR BioGRID; 34846; 244.
DR IntAct; P40458; 6.
DR MINT; P40458; -.
DR STRING; 4932.YIL146C; -.
DR iPTMnet; P40458; -.
DR MaxQB; P40458; -.
DR PaxDb; P40458; -.
DR PRIDE; P40458; -.
DR DNASU; 854660; -.
DR EnsemblFungi; YIL146C_mRNA; YIL146C; YIL146C.
DR GeneID; 854660; -.
DR KEGG; sce:YIL146C; -.
DR SGD; S000001408; ATG32.
DR VEuPathDB; FungiDB:YIL146C; -.
DR eggNOG; ENOG502QY5V; Eukaryota.
DR HOGENOM; CLU_039418_0_0_1; -.
DR InParanoid; P40458; -.
DR OMA; IPICQPG; -.
DR BioCyc; YEAST:G3O-31395-MON; -.
DR PRO; PR:P40458; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40458; protein.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0031930; P:mitochondria-nucleus signaling pathway; IGI:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..529
FT /note="Autophagy-related protein 32"
FT /id="PRO_0000086920"
FT TRANSMEM 390..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21757540"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21757540"
FT MUTAGEN 114
FT /note="S->A,N,G,Y: Abolishes mitophagy and impairs
FT interaction with ATG11."
FT /evidence="ECO:0000269|PubMed:21757540"
FT MUTAGEN 119
FT /note="S->A: Decreases mitophagy and impairs interaction
FT with ATG11."
FT /evidence="ECO:0000269|PubMed:21757540"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:5WLP"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:5WLP"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:5WLP"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:5WLP"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:5WLP"
FT TURN 247..251
FT /evidence="ECO:0007829|PDB:5WLP"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:5WLP"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:5WLP"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:5WLP"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:5WLP"
FT HELIX 293..299
FT /evidence="ECO:0007829|PDB:5WLP"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:5WLP"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:5WLP"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:5WLP"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:5WLP"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:5WLP"
FT HELIX 329..338
FT /evidence="ECO:0007829|PDB:5WLP"
SQ SEQUENCE 529 AA; 58969 MW; DB6A3DAFD50FB619 CRC64;
MVLEYQQREG KGSSSKSMPP DSSSTTIHTC SEAQTGEDKG LLDPHLSVLE LLSKTGHSPS
PMGQNLVTSI DISGNHNVND SISGSWQAIQ PLDLGASFIP ERCSSQTTNG SILSSSDTSE
EEQELLQAPA ADIINIIKQG QEGANVVSPS HPFKQLQKII SLPLPGKEKT PFNEQDDDGD
EDEAFEEDSV TITKSLTSST NSFVMPKLSL TQKNPVFRLL ILGRTGSSFY QSIPKEYQSL
FELPKYHDSA TFPQYTGIVI IFQELREMVS LLNRIVQYSQ GKPVIPICQP GQVIQVKNVL
KSFLRNKLVK LLFPPVVVTN KRDLKKMFQR LQDLSLEYGE DVNEEDNDDE AIHTKSRSYC
RNKKAENSKK KSPKSNKKPK RKKQKFFTSW FTWGISITIG ISFGCCVTYF VTAAYEHQTV
KSLSLRPSIL ASLLSLDSSS DTINTPATAS PSSTEQFLWF DKGTLQINFH SDGFIMKSLT
IIKETWGKMN TFVLHALSKP LKFLENLNKS SEFSIDESNR ILALGYILL
