ATG32_ASHGO
ID ATG32_ASHGO Reviewed; 452 AA.
AC Q753M9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Autophagy-related protein 32;
GN Name=ATG32; OrderedLocusNames=AFR283W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Vacuole membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC Preautophagosomal structure membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}. Note=Is recruited to the
CC preautophagosomal structure during mitophagy and imported into the
CC vacuole along with mitochondria during starvation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG32 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016819; AAS53654.1; -; Genomic_DNA.
DR RefSeq; NP_985830.1; NM_211185.2.
DR AlphaFoldDB; Q753M9; -.
DR SMR; Q753M9; -.
DR STRING; 33169.AAS53654; -.
DR PRIDE; Q753M9; -.
DR EnsemblFungi; AAS53654; AAS53654; AGOS_AFR283W.
DR GeneID; 4622093; -.
DR KEGG; ago:AGOS_AFR283W; -.
DR eggNOG; ENOG502QY5V; Eukaryota.
DR HOGENOM; CLU_039418_0_0_1; -.
DR InParanoid; Q753M9; -.
DR OMA; IPICQPG; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Autophagy; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..452
FT /note="Autophagy-related protein 32"
FT /id="PRO_0000399756"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 50405 MW; 677AFEFE4EB9A648 CRC64;
MSTKSQVTRR VRTSIATPED GVHGNNQHKG ILDPHLSVLE MLDRQDGDGA GQVEEGAVMT
VGKRRVERSL HHSISESWQA IKRSDYSFLS GTHEVGAMHS SVGILSSSDT SEEEAEMRPS
AHGTVHLGSS LASPMRQLLV EEDNSCAEED DCQTVTISMP SSSTSLVMPK LSLSQRLGEP
QLLLVGQPAR KFWLTIPKCY QKLFDVKNLG MVTRWDVGQR YLAVMVVFHD IAQAPELLDG
LCEKAPCPTV IPVCQKGQKS TLAALLKRYT ARKCIRVYCS PIIMSNHHEK HRLLKHLHNL
CNESESGYET ELTVKSKKQH RRPRKKDAGP VALRHWAIWT ASFTIGIGIG CCISLMATTR
FTFFSSAPLP LTAVIPAQIP SSVASDKPPH RLVPHFYMLC KTTIRQLGTS LRLFFFEKFE
SRTWVHIFGM DLHSDDPLAS LGRLMPLDFI ML