ID   ATG33_YEAST             Reviewed;         197 AA.
AC   Q06485; D6VYZ4;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Autophagy-related protein 33;
GN   Name=ATG33; OrderedLocusNames=YLR356W;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-129, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [9]
RP   FUNCTION.
RX   PubMed=20364111; DOI=10.4161/auto.6.2.10901;
RA   Kanki T., Wang K., Klionsky D.J.;
RT   "A genomic screen for yeast mutants defective in mitophagy.";
RL   Autophagy 6:278-280(2010).
CC   -!- FUNCTION: Involved in the selective degradation of mitochondria via
CC       autophagy during starvation and at post-log phase.
CC       {ECO:0000269|PubMed:19793921, ECO:0000269|PubMed:20364111}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATG33 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; U19102; AAB67748.1; -; Genomic_DNA.
DR   EMBL; AY558222; AAS56548.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09660.1; -; Genomic_DNA.
DR   PIR; S51464; S51464.
DR   RefSeq; NP_013460.1; NM_001182245.1.
DR   AlphaFoldDB; Q06485; -.
DR   BioGRID; 31618; 169.
DR   DIP; DIP-4664N; -.
DR   IntAct; Q06485; 1.
DR   MINT; Q06485; -.
DR   STRING; 4932.YLR356W; -.
DR   iPTMnet; Q06485; -.
DR   MaxQB; Q06485; -.
DR   PaxDb; 4932-YLR356W; -.
DR   PeptideAtlas; Q06485; -.
DR   EnsemblFungi; YLR356W_mRNA; YLR356W; YLR356W.
DR   GeneID; 851070; -.
DR   KEGG; sce:YLR356W; -.
DR   AGR; SGD:S000004348; -.
DR   SGD; S000004348; ATG33.
DR   VEuPathDB; FungiDB:YLR356W; -.
DR   eggNOG; ENOG502S27M; Eukaryota.
DR   GeneTree; ENSGT00940000176491; -.
DR   HOGENOM; CLU_105986_1_0_1; -.
DR   InParanoid; Q06485; -.
DR   OMA; HANCNAS; -.
DR   OrthoDB; 2039252at2759; -.
DR   BioCyc; YEAST:G3O-32428-MONOMER; -.
DR   BioGRID-ORCS; 851070; 1 hit in 10 CRISPR screens.
DR   PRO; PR:Q06485; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q06485; Protein.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR   GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR   PANTHER; PTHR37278; AUTOPHAGY-RELATED PROTEIN 33-RELATED; 1.
DR   PANTHER; PTHR37278:SF1; AUTOPHAGY-RELATED PROTEIN 33-RELATED; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Membrane; Mitochondrion; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..197
FT                   /note="Autophagy-related protein 33"
FT                   /id="PRO_0000247213"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          135..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   197 AA;  20400 MW;  4BA9F5CD485FB259 CRC64;
     MSVCLAITKG IAVSSIGLYS GLLASASLIT STTPLEVLTG SLTPTLTTLK NAATALGAFA
     STFFCVSFFG APPSLRHPYL LYGMLVAPLS SFVLGCASNY QSRKYSKVSK ESSLFPEDSK
     LAASELSDSI IDLGEDNHAS ENTPRDGKPA ATTVSKPAEA LHTGPPIHTK NLIAATAIAI
     VGFVQAVIGV YGEGQFI
//