ATG31_YEAST
ID ATG31_YEAST Reviewed; 196 AA.
AC Q12421; D6VS08; Q03939;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Autophagy-related protein 31;
DE AltName: Full=CIK1 suppressor protein 1;
DE AltName: Full=Protein CIS1;
GN Name=ATG31; Synonyms=CIS1; OrderedLocusNames=YDR022C;
GN ORFNames=PZD196, YD9335.08c;
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].
RX PubMed=8896275;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1085::aid-yea9>3.3.co;2-s;
RA Eide L.G., Sander C., Prydz H.;
RT "Sequencing and analysis of a 35.4 kb region on the right arm of chromosome
RT IV from Saccharomyces cerevisiae reveal 23 open reading frames.";
RL Yeast 12:1085-1090(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [5]
RP FUNCTION.
RX PubMed=9348527; DOI=10.1091/mbc.8.10.1829;
RA Manning B.D., Padmanabha R., Snyder M.;
RT "The Rho-GEF Rom2p localizes to sites of polarized cell growth and
RT participates in cytoskeletal functions in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 8:1829-1844(1997).
RN [6]
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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATG17.
RX PubMed=17362880; DOI=10.1016/j.bbrc.2007.02.150;
RA Kabeya Y., Kawamata T., Suzuki K., Ohsumi Y.;
RT "Cis1/Atg31 is required for autophagosome formation in Saccharomyces
RT cerevisiae.";
RL Biochem. Biophys. Res. Commun. 356:405-410(2007).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATG1.
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 [10]
RP INTERACTION WITH ATG17 AND ATG29.
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, INTERACTION WITH THE
RP ATG1-ATG13 COMPLEX, AND PHOSPHORYLATION.
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).
CC -!- FUNCTION: Plays a role in starvation-induced autophagy. Involved in
CC mitophagy. Functions with ATG17 and ATG29 at the preautophagosomal
CC structure (PAS) in order to form normal autophagosomes under starvation
CC conditions. May be involved in microtubule function, such as chromosome
CC segregation and karyogamy. {ECO:0000269|PubMed:17362880,
CC ECO:0000269|PubMed:18287526, ECO:0000269|PubMed:19793921,
CC ECO:0000269|PubMed:9348527}.
CC -!- SUBUNIT: Forms a stable complex with ATG17 and ATG29. Interacts
CC directly with ATG29. 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:17362880,
CC ECO:0000269|PubMed:18287526, ECO:0000269|PubMed:19337029,
CC ECO:0000269|PubMed:19755117}.
CC -!- INTERACTION:
CC Q12421; Q06410: ATG17; NbExp=3; IntAct=EBI-34768, EBI-30856;
CC Q12421; P28737: MSP1; NbExp=3; IntAct=EBI-34768, EBI-11435;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC Preautophagosomal structure.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:19755117}.
CC -!- MISCELLANEOUS: Present with 486 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X95966; CAA65214.1; -; Genomic_DNA.
DR EMBL; Z74318; CAA98843.1; -; Genomic_DNA.
DR EMBL; Z49770; CAA89847.1; -; Genomic_DNA.
DR EMBL; AY557645; AAS55971.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11868.1; -; Genomic_DNA.
DR PIR; S63429; S63429.
DR RefSeq; NP_010305.1; NM_001180330.1.
DR AlphaFoldDB; Q12421; -.
DR SMR; Q12421; -.
DR BioGRID; 32072; 64.
DR ComplexPortal; CPX-1676; ATG1 kinase complex.
DR ComplexPortal; CPX-397; Atg17-Atg31-Atg29 complex.
DR DIP; DIP-2667N; -.
DR IntAct; Q12421; 9.
DR MINT; Q12421; -.
DR STRING; 4932.YDR022C; -.
DR iPTMnet; Q12421; -.
DR MaxQB; Q12421; -.
DR PaxDb; Q12421; -.
DR PRIDE; Q12421; -.
DR EnsemblFungi; YDR022C_mRNA; YDR022C; YDR022C.
DR GeneID; 851585; -.
DR KEGG; sce:YDR022C; -.
DR SGD; S000002429; ATG31.
DR VEuPathDB; FungiDB:YDR022C; -.
DR eggNOG; ENOG502SA9V; Eukaryota.
DR HOGENOM; CLU_138108_0_0_1; -.
DR InParanoid; Q12421; -.
DR OMA; IRYIFED; -.
DR BioCyc; YEAST:G3O-29639-MON; -.
DR PRO; PR:Q12421; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12421; 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:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR GO; GO:0032991; C:protein-containing complex; IPI:ComplexPortal.
DR GO; GO:0000045; P:autophagosome assembly; IC:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IDA:ComplexPortal.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0000741; P:karyogamy; IEA:UniProtKB-KW.
DR GO; GO:0044805; P:late nucleophagy; IMP:SGD.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP: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 InterPro; IPR018621; Atg31.
DR Pfam; PF09795; ATG31; 1.
PE 1: Evidence at protein level;
KW Autophagy; Chromosome partition; Cytoplasm; Cytoskeleton; Karyogamy;
KW Microtubule; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..196
FT /note="Autophagy-related protein 31"
FT /id="PRO_0000076210"
FT REGION 20..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 196 AA; 22191 MW; CC2396854F29D250 CRC64;
MNVTVTVYDK NVKYRLEENI KNNKGPSNDD QPAYNNESKS TDGSDYAMFP TNIKYIFEDN
NDELVDSSDA ALTAGIDKVG DELENVIIVQ LDESGSLEDI TLISDQYELL SHRTNSLSLE
ENQMRTLSSH GDDKSNDEEE ELSVDSDRFR VDSDIELDVI SQFCDLSPFL RDLSLNDLIK
LYVTQNEQLQ MLSNSV
