ATG29_YEAST
ID ATG29_YEAST Reviewed; 213 AA.
AC Q12092; D6W3K2;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Autophagy-related protein 29;
GN Name=ATG29; OrderedLocusNames=YPL166W; ORFNames=P2540;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16289106; DOI=10.1016/j.bbrc.2005.10.163;
RA Kawamata T., Kamada Y., Suzuki K., Kuboshima N., Akimatsu H., Ota S.,
RA Ohsumi M., Ohsumi Y.;
RT "Characterization of a novel autophagy-specific gene, ATG29.";
RL Biochem. Biophys. Res. Commun. 338:1884-1889(2005).
RN [7]
RP FUNCTION.
RX PubMed=17700056; DOI=10.4161/auto.4784;
RA Ma J., Jin R., Dobry C.J., Lawson S.K., Kumar A.;
RT "Overexpression of autophagy-related genes inhibits yeast filamentous
RT growth.";
RL Autophagy 3:604-609(2007).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATG1 AND ATG17.
RX PubMed=18287526; DOI=10.1091/mbc.e07-10-1048;
RA Kawamata T., Kamada Y., Kabeya Y., Sekito T., Ohsumi Y.;
RT "Organization of the pre-autophagosomal structure responsible for
RT autophagosome formation.";
RL Mol. Biol. Cell 19:2039-2050(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, 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 [10]
RP INTERACTION WITH ATG17 AND ATG31.
RX PubMed=19337029; DOI=10.4161/auto.5.5.8382;
RA Cao Y., Nair U., Yasumura-Yorimitsu K., Klionsky D.J.;
RT "A multiple ATG gene knockout strain for yeast two-hybrid analysis.";
RL Autophagy 5:699-705(2009).
RN [11]
RP IDENTIFICATION IN THE ATG17-ATG29-ATG31 COMPLEX, AND INTERACTION WITH THE
RP ATG1-ATG13 COMPLEX.
RX PubMed=19755117; DOI=10.1016/j.bbrc.2009.09.034;
RA Kabeya Y., Noda N.N., Fujioka Y., Suzuki K., Inagaki F., Ohsumi Y.;
RT "Characterization of the Atg17-Atg29-Atg31 complex specifically required
RT for starvation-induced autophagy in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 389:612-615(2009).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND SER-188, 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).
CC -!- FUNCTION: Plays a role in autophagy. Functions at the preautophagosomal
CC structure (PAS) in order to form normal autophagosomes under starvation
CC conditions. Also plays a role in mitophagy and regulation of
CC filamentous growth. {ECO:0000269|PubMed:16289106,
CC ECO:0000269|PubMed:17700056, ECO:0000269|PubMed:18287526,
CC ECO:0000269|PubMed:19793921}.
CC -!- SUBUNIT: Forms a stable complex with ATG17 and ATG31. Interacts
CC directly with ATG31. The ATG17-ATG29-ATG31 complex interacts with the
CC ATG1-ATG13 complex. Note=The interaction with the ATG1-ATG13 complex is
CC induced by starvation. {ECO:0000269|PubMed:18287526,
CC ECO:0000269|PubMed:19337029, ECO:0000269|PubMed:19755117}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16289106,
CC ECO:0000269|PubMed:18287526}. Note=Localizes also to other perivacuolar
CC punctate structures.
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATG29 family. {ECO:0000305}.
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DR EMBL; X96770; CAA65555.1; -; Genomic_DNA.
DR EMBL; Z73522; CAA97871.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11268.1; -; Genomic_DNA.
DR PIR; S65177; S65177.
DR RefSeq; NP_015159.1; NM_001183980.1.
DR AlphaFoldDB; Q12092; -.
DR SMR; Q12092; -.
DR BioGRID; 36017; 84.
DR ComplexPortal; CPX-1676; ATG1 kinase complex.
DR ComplexPortal; CPX-397; Atg17-Atg31-Atg29 complex.
DR DIP; DIP-6360N; -.
DR IntAct; Q12092; 7.
DR MINT; Q12092; -.
DR STRING; 4932.YPL166W; -.
DR iPTMnet; Q12092; -.
DR PaxDb; Q12092; -.
DR PRIDE; Q12092; -.
DR EnsemblFungi; YPL166W_mRNA; YPL166W; YPL166W.
DR GeneID; 855937; -.
DR KEGG; sce:YPL166W; -.
DR SGD; S000006087; ATG29.
DR VEuPathDB; FungiDB:YPL166W; -.
DR eggNOG; ENOG502S1W0; Eukaryota.
DR HOGENOM; CLU_121102_0_0_1; -.
DR InParanoid; Q12092; -.
DR OMA; QITTHEG; -.
DR BioCyc; YEAST:G3O-34062-MON; -.
DR PRO; PR:Q12092; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12092; protein.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR GO; GO:0032991; C:protein-containing complex; IPI:ComplexPortal.
DR GO; GO:0000149; F:SNARE binding; IDA:SGD.
DR GO; GO:0000045; P:autophagosome assembly; IDA:SGD.
DR GO; GO:0006914; P:autophagy; IDA:ComplexPortal.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0044805; P:late nucleophagy; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IDA:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042594; P:response to starvation; IC:ComplexPortal.
DR Gene3D; 1.10.10.2570; -; 1.
DR InterPro; IPR039113; ATG29.
DR InterPro; IPR040666; Atg29_N.
DR InterPro; IPR039362; ATG29_sf.
DR PANTHER; PTHR40012; PTHR40012; 1.
DR Pfam; PF18388; ATG29_N; 1.
PE 1: Evidence at protein level;
KW Autophagy; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..213
FT /note="Autophagy-related protein 29"
FT /id="PRO_0000232994"
FT REGION 157..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 213 AA; 24708 MW; E620EF94CF662BD4 CRC64;
MIMNSTNTVV YIKVKGRRPQ GFLDPPKFEW NGTKERQLWT MVSNLNYSQD QIDWQNLSKI
FETPEFFLKK RTYKLFAEHL ELLQLQLEKK RDLEKYSNDQ VNEGMSDLIH KYTPTLQNDN
LLNVSASPLT TERQDSEEVE TEVTNEALQH LQTSKILNIH KKTSDSENKP NDKLDKDGIN
KEMECGSSDD DLSSSLSVSK SALEEALMDR LQF
