ATG21_YEAST
ID ATG21_YEAST Reviewed; 496 AA.
AC Q02887; D6W3R6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Autophagy-related protein 21;
DE AltName: Full=Cytoplasm to vacuole transport protein 21;
DE AltName: Full=Homologous with SVP1 protein 1;
DE AltName: Full=Maturation of proaminopeptidase I protein 1;
GN Name=ATG21; Synonyms=CVT21, HSV1, MAI1; OrderedLocusNames=YPL100W;
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=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 [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 FUNCTION.
RX PubMed=11536337; DOI=10.1002/yea.764;
RA Georgakopoulos T., Koutroubas G., Vakonakis I., Tzermia M., Prokova V.,
RA Voutsina A., Alexandraki D.;
RT "Functional analysis of the Saccharomyces cerevisiae
RT YFR021w/YGR223c/YPL100w ORF family suggests relations to
RT mitochondrial/peroxisomal functions and amino acid signalling pathways.";
RL Yeast 18:1155-1171(2001).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11852075; DOI=10.1016/s0014-5793(02)02252-4;
RA Barth H., Meiling-Wesse K., Epple U.D., Thumm M.;
RT "Mai1p is essential for maturation of proaminopeptidase I but not for
RT autophagy.";
RL FEBS Lett. 512:173-179(2002).
RN [5]
RP NOMENCLATURE.
RX PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x;
RA Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
RA Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
RT "A unified nomenclature for yeast autophagy-related genes.";
RL Dev. Cell 5:539-545(2003).
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 INTERACTION WITH PIP2, AND SUBCELLULAR LOCATION.
RX PubMed=15103325; DOI=10.1038/sj.emboj.7600203;
RA Dove S.K., Piper R.C., McEwen R.K., Yu J.W., King M.C., Hughes D.C.,
RA Thuring J., Holmes A.B., Cooke F.T., Michell R.H., Parker P.J.,
RA Lemmon M.A.;
RT "Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate
RT effectors.";
RL EMBO J. 23:1922-1933(2004).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15194695; DOI=10.1074/jbc.m401066200;
RA Meiling-Wesse K., Barth H., Voss C., Eskelinen E.-L., Epple U.D., Thumm M.;
RT "Atg21 is required for effective recruitment of Atg8 to the
RT preautophagosomal structure during the Cvt pathway.";
RL J. Biol. Chem. 279:37741-37750(2004).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 343-ARG-ARG-344.
RX PubMed=15155809; DOI=10.1091/mbc.e04-02-0147;
RA Stromhaug P.E., Reggiori F., Guan J., Wang C.-W., Klionsky D.J.;
RT "Atg21 is a phosphoinositide binding protein required for efficient
RT lipidation and localization of Atg8 during uptake of aminopeptidase I by
RT selective autophagy.";
RL Mol. Biol. Cell 15:3553-3566(2004).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=16876790; DOI=10.1016/j.febslet.2006.07.041;
RA Krick R., Tolstrup J., Appelles A., Henke S., Thumm M.;
RT "The relevance of the phosphatidylinositolphosphat-binding motif FRRGT of
RT Atg18 and Atg21 for the Cvt pathway and autophagy.";
RL FEBS Lett. 580:4632-4638(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [13]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18769150; DOI=10.4161/auto.6801;
RA Krick R., Henke S., Tolstrup J., Thumm M.;
RT "Dissecting the localization and function of Atg18, Atg21 and Ygr223c.";
RL Autophagy 4:896-910(2008).
RN [14]
RP IDENTIFICATION BY 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-213, AND IDENTIFICATION BY
RP 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 [17]
RP FUNCTION, AND DOMAIN.
RX PubMed=20154084; DOI=10.1074/jbc.m109.080374;
RA Nair U., Cao Y., Xie Z., Klionsky D.J.;
RT "Roles of the lipid-binding motifs of Atg18 and Atg21 in the cytoplasm to
RT vacuole targeting pathway and autophagy.";
RL J. Biol. Chem. 285:11476-11488(2010).
RN [18]
RP FUNCTION.
RX PubMed=22108003; DOI=10.4161/auto.7.12.18424;
RA Nair U., Thumm M., Klionsky D.J., Krick R.;
RT "GFP-Atg8 protease protection as a tool to monitor autophagosome
RT biogenesis.";
RL Autophagy 7:1546-1550(2011).
CC -!- FUNCTION: Required for cytoplasm to vacuole transport (Cvt) vesicles
CC formation and mitophagy. Involved in binding of
CC phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to
CC the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated
CC cleavage. Essential for maturation of proaminopeptidase I.
CC {ECO:0000269|PubMed:11536337, ECO:0000269|PubMed:11852075,
CC ECO:0000269|PubMed:15155809, ECO:0000269|PubMed:15194695,
CC ECO:0000269|PubMed:16876790, ECO:0000269|PubMed:18769150,
CC ECO:0000269|PubMed:19793921, ECO:0000269|PubMed:20154084,
CC ECO:0000269|PubMed:22108003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Vacuole. Note=And perivacuolar
CC punctate structures.
CC -!- DOMAIN: Contains a beta-propeller domain involved in specific binding
CC to phosphatidylinositol 3,5-bisphosphate (PIP2).
CC -!- DOMAIN: The L/FRRG motif is essential for the cytoplasm to vacuole
CC transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to
CC the PAS in nutrient-rich medium and in both its recruitment to and
CC dissociation from the PAS under starvation conditions.
CC {ECO:0000269|PubMed:15155809}.
CC -!- MISCELLANEOUS: Present with 6020 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR EMBL; U43281; AAB68199.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11332.1; -; Genomic_DNA.
DR PIR; S61966; S61966.
DR RefSeq; NP_015225.1; NM_001183914.1.
DR AlphaFoldDB; Q02887; -.
DR SMR; Q02887; -.
DR BioGRID; 36080; 140.
DR IntAct; Q02887; 4.
DR MINT; Q02887; -.
DR STRING; 4932.YPL100W; -.
DR iPTMnet; Q02887; -.
DR MaxQB; Q02887; -.
DR PaxDb; Q02887; -.
DR PRIDE; Q02887; -.
DR EnsemblFungi; YPL100W_mRNA; YPL100W; YPL100W.
DR GeneID; 856004; -.
DR KEGG; sce:YPL100W; -.
DR SGD; S000006021; ATG21.
DR VEuPathDB; FungiDB:YPL100W; -.
DR eggNOG; KOG2110; Eukaryota.
DR HOGENOM; CLU_025895_5_2_1; -.
DR InParanoid; Q02887; -.
DR OMA; MNRKRMC; -.
DR BioCyc; YEAST:G3O-34003-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR PRO; PR:Q02887; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02887; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; 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:0006497; P:protein lipidation; IMP:SGD.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IMP:SGD.
DR GO; GO:0016050; P:vesicle organization; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; Vacuole; WD repeat.
FT CHAIN 1..496
FT /note="Autophagy-related protein 21"
FT /id="PRO_0000050882"
FT REPEAT 294..334
FT /note="WD 1"
FT REPEAT 346..385
FT /note="WD 2"
FT REPEAT 448..488
FT /note="WD 3"
FT REGION 41..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 342..346
FT /note="L/FRRG motif"
FT /evidence="ECO:0000269|PubMed:15155809"
FT COMPBIAS 43..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MUTAGEN 343..344
FT /note="RR->KK: Loss of aminopeptidase I precursor
FT maturation and no more association with vacuole and
FT punctate structures."
FT /evidence="ECO:0000269|PubMed:15155809"
SQ SEQUENCE 496 AA; 55188 MW; 4454C28180E3974D CRC64;
MKVLQFNQDA TCCVVAASSH QISIFNCDPF GKCFEIDTKN SKKKTSNNNG SASNSESRNN
EESILITNGS RDRTDAEEEE DNEDNALVTG NILKEGEFVI EMLFSTSLIA IADRGQGLNK
GKKLKIVNTK RKCTICEIVF PHEIVDVVMN RKRMCVLLES DQIFIYDISC MKPLETIDLW
EDHYKRSQAN SFSNASNTGT LEGDSANLNR VATNLLANAT QKSVNGSNPS VRTRRNSLRS
KIRPRMVLSN DDRSILCFTA YSSPKKNKPN SEALYDVVIY DTLNVTPVNY LNSVHKGNVA
CLAVSHDGKL LATASDKGTI IRVFHTGVDS DYMSSRSLFK EFRRGTRLCN LYQLAFDKSM
TMIGCVGDTD TIHLFKLDDA SNSLPGDNSS NGHWNEEEYI LASNSNPSMG TPKEIPLSKP
RIANYFSKKI KSSIPNQNLS RNFAYITVNE SNRSCLGFPD EFPNQVYIAS DDGTFSIYSI
PSKPGECVLT KNNKFT
