DOA1_YEAST
ID DOA1_YEAST Reviewed; 715 AA.
AC P36037; D6VWZ0;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Protein DOA1 {ECO:0000303|PubMed:2111732};
DE AltName: Full=Degradation of alpha protein 1 {ECO:0000303|PubMed:2111732};
DE AltName: Full=Ubiquitin fusion degradation protein 3 {ECO:0000303|PubMed:7615550};
GN Name=DOA1 {ECO:0000303|PubMed:2111732, ECO:0000312|SGD:S000001696};
GN Synonyms=UFD3 {ECO:0000303|PubMed:7615550, ECO:0000312|SGD:S000001696},
GN ZZZ4 {ECO:0000312|SGD:S000001696};
GN OrderedLocusNames=YKL213C {ECO:0000312|SGD:S000001696};
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].
RA Hochstrasser M., Gang G.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7941750; DOI=10.1002/yea.320100511;
RA Tzermia M., Horaitis O., Alexandraki D.;
RT "The complete sequencing of a 24.6 kb segment of yeast chromosome XI
RT identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open
RT reading frames including homologues to the threonine dehydratases, membrane
RT transporters, hydantoinases and the phospholipase A2-activating protein.";
RL Yeast 10:663-679(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 126-144; 173-183; 215-227; 316-335; 345-361; 384-420;
RP 534-541; 598-613; 654-685 AND 700-706, FUNCTION, AND INTERACTION WITH
RP UBIQUITIN.
RX PubMed=15096053; DOI=10.1021/bi035626r;
RA Russell N.S., Wilkinson K.D.;
RT "Identification of a novel 29-linked polyubiquitin binding protein, Ufd3,
RT using polyubiquitin chain analogues.";
RL Biochemistry 43:4844-4854(2004).
RN [6]
RP FUNCTION.
RX PubMed=2111732; DOI=10.1016/0092-8674(90)90481-s;
RA Hochstrasser M., Varshavsky A.;
RT "In vivo degradation of a transcriptional regulator: the yeast alpha 2
RT repressor.";
RL Cell 61:697-708(1990).
RN [7]
RP FUNCTION.
RX PubMed=7615550; DOI=10.1074/jbc.270.29.17442;
RA Johnson E.S., Ma P.C.M., Ota I.M., Varshavsky A.;
RT "A proteolytic pathway that recognizes ubiquitin as a degradation signal.";
RL J. Biol. Chem. 270:17442-17456(1995).
RN [8]
RP FUNCTION, INTERACTION WITH CDC48, AND MUTAGENESIS OF CYS-237.
RX PubMed=8890162; DOI=10.1002/j.1460-2075.1996.tb00869.x;
RA Ghislain M., Dohmen R.J., Levy F., Varshavsky A.;
RT "Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-
RT mediated proteolysis in Saccharomyces cerevisiae.";
RL EMBO J. 15:4884-4899(1996).
RN [9]
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 [10]
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 [11]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH NPL4; UFD1; CDC48; OTU1 AND
RP SHP1, INTERACTION WITH OTU1; UBIQUITIN AND CDC48, DOMAIN, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 2-GLY--PHE-287; 2-GLY--SER-359;
RP 2-GLY--MET-425; 426-SER--SER-715 AND 495-LYS--SER-715.
RX PubMed=16427015; DOI=10.1016/j.molcel.2005.12.014;
RA Rumpf S., Jentsch S.;
RT "Functional division of substrate processing cofactors of the ubiquitin-
RT selective Cdc48 chaperone.";
RL Mol. Cell 21:261-269(2006).
RN [12]
RP FUNCTION, INTERACTION WITH UBIQUITIN AND CDC48, DOMAIN, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 2-GLY--HIS-253; 2-GLY--LEU-253; PHE-417;
RP 426-SER--SER-715; PHE-434 AND 451-ALA--SER-715.
RX PubMed=16428438; DOI=10.1128/mcb.26.3.822-830.2006;
RA Mullally J.E., Chernova T., Wilkinson K.D.;
RT "Doa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domain.";
RL Mol. Cell. Biol. 26:822-830(2006).
RN [13]
RP FUNCTION, INTERACTION WITH HSE1, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 434-PHE--ASN-440 AND 434-PHE--SER-443.
RX PubMed=18508771; DOI=10.1074/jbc.m802982200;
RA Ren J., Pashkova N., Winistorfer S., Piper R.C.;
RT "DOA1/UFD3 plays a role in sorting ubiquitinated membrane proteins into
RT multivesicular bodies.";
RL J. Biol. Chem. 283:21599-21611(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, 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 [16]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH UBP3; BRE5 AND CDC48, AND
RP INTERACTION WITH UBP3 AND CDC48.
RX PubMed=20508643; DOI=10.1038/embor.2010.74;
RA Ossareh-Nazari B., Bonizec M., Cohen M., Dokudovskaya S., Delalande F.,
RA Schaeffer C., Van Dorsselaer A., Dargemont C.;
RT "Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required
RT for ribophagy.";
RL EMBO Rep. 11:548-554(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP FUNCTION.
RX PubMed=23525333; DOI=10.1534/genetics.113.149898;
RA Au W.C., Dawson A.R., Rawson D.W., Taylor S.B., Baker R.E., Basrai M.A.;
RT "A novel role of the N terminus of budding yeast histone H3 variant Cse4 in
RT ubiquitin-mediated proteolysis.";
RL Genetics 194:513-518(2013).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDC48 AND FZO1, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ASP-15; PHE-222; TRP-265; PHE-417; PHE-434;
RP ARG-541 AND ARG-669.
RX PubMed=27044889; DOI=10.1083/jcb.201510098;
RA Wu X., Li L., Jiang H.;
RT "Doa1 targets ubiquitinated substrates for mitochondria-associated
RT degradation.";
RL J. Cell Biol. 213:49-63(2016).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 464-715, FUNCTION, INTERACTION
RP WITH CDC48, DOMAIN, ARM REPEATS, AND MUTAGENESIS OF ARG-541 AND ARG-669.
RX PubMed=19805280; DOI=10.1073/pnas.0908321106;
RA Zhao G., Li G., Schindelin H., Lennarz W.J.;
RT "An Armadillo motif in Ufd3 interacts with Cdc48 and is involved in
RT ubiquitin homeostasis and protein degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16197-16202(2009).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 354-715, AND ARM REPEATS.
RX PubMed=21063153;
RA Nishimasu R., Komori H., Higuchi Y., Nishimasu H., Hiroaki H.;
RT "Crystal structure of a PFU-PUL domain pair of Saccharomyces cerevisiae
RT Doa1/Ufd3.";
RL Kobe J. Med. Sci. 56:E125-E139(2010).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 2-300, INTERACTION WITH
RP UBIQUITIN, DOMAIN, AND MUTAGENESIS OF LEU-5; ASP-15; ALA-158; PHE-222;
RP TRP-265 AND ASP-281.
RX PubMed=21070969; DOI=10.1016/j.molcel.2010.10.018;
RA Pashkova N., Gakhar L., Winistorfer S.C., Yu L., Ramaswamy S., Piper R.C.;
RT "WD40 repeat propellers define a ubiquitin-binding domain that regulates
RT turnover of F box proteins.";
RL Mol. Cell 40:433-443(2010).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 325-715.
RA Liu Y., Sun J.;
RT "Crystal structure of PUL and PFU domain.";
RL Submitted (DEC-2010) to the PDB data bank.
CC -!- FUNCTION: Ubiquitin-binding protein involved in protein ubiquitination,
CC sorting and degradation (PubMed:2111732, PubMed:8890162,
CC PubMed:19805280, PubMed:18508771, PubMed:20508643, PubMed:27044889).
CC Acts as a ubiquitinated substrate-recruiting adapter for chaperone
CC ATPase CDC48 by binding mono- or polyubiquitin chains (PubMed:15096053,
CC PubMed:16427015, PubMed:16428438, PubMed:27044889). Depending on the
CC context, promotes or prevents proteasomal degradation of ubiquitinated
CC proteins (PubMed:2111732, PubMed:8890162, PubMed:19805280,
CC PubMed:27044889). Involved in the ubiquitin fusion degradation (UFD)
CC pathway by promoting the degradation of ubiquitinated proteins
CC (PubMed:2111732, PubMed:8890162, PubMed:19805280, PubMed:27044889).
CC Involved in the mitochondria-associated degradation pathway (MAD) by
CC promoting the degradation of several ubiquitinated membrane proteins
CC (PubMed:27044889). By competing with UFD2 to bind CDC48, prevents the
CC multi-ubiquitination and subsequent degradation of UFD2-dependent
CC substrates (PubMed:16427015). Required for ribophagy, a process which
CC relocalizes ribosomal particles into the vacuole for degradation in
CC response to starvation (PubMed:20508643). Involved in the ubiquitin-
CC mediated sorting of membrane proteins into multivesicular bodies (MVBs)
CC (PubMed:18508771). In addition, plays an essential role in maintaining
CC cellular ubiquitin levels (PubMed:7615550, PubMed:16427015,
CC PubMed:16428438, PubMed:18508771, PubMed:19805280). May affect
CC indirectly the degradation of ubiquitinylated proteins by regulating
CC cellular ubiquitin levels (PubMed:7615550, PubMed:23525333).
CC {ECO:0000269|PubMed:15096053, ECO:0000269|PubMed:16427015,
CC ECO:0000269|PubMed:16428438, ECO:0000269|PubMed:18508771,
CC ECO:0000269|PubMed:19805280, ECO:0000269|PubMed:20508643,
CC ECO:0000269|PubMed:2111732, ECO:0000269|PubMed:23525333,
CC ECO:0000269|PubMed:27044889, ECO:0000269|PubMed:7615550,
CC ECO:0000269|PubMed:8890162}.
CC -!- SUBUNIT: Forms a complex composed of CDC48, NPL4, UFD1, DOA1, SHP1 and
CC deubiquitinase OTU1; within the complex interacts with CDC48
CC (PubMed:16427015). Interacts (via PUL domain) with CDC48 (via C-
CC terminus); the interaction is direct (PubMed:8890162, PubMed:16427015,
CC PubMed:16428438, PubMed:27044889, PubMed:19805280, PubMed:20508643).
CC Forms a complex composed of CDC48, DOA1, deubiquitinase UBP3 and
CC probably BRE5; within the complex interacts with CDC48 and UBP3
CC (PubMed:20508643). May form a complex composed of VPS27, HSE1 and DOA1
CC (PubMed:18508771). Interacts with HSE1 (via SH3 domain)
CC (PubMed:18508771). Interacts (via WD repeats and PFU domain) with
CC ubiquitin; the interaction is direct (PubMed:15096053, PubMed:16427015,
CC PubMed:16428438, PubMed:21070969). Interacts with ubiquitinated FZO1
CC but not unmodified FZO1; the interaction recruits FZO1 to CDC48 and
CC promotes FZO1 proteasomal degradation (PubMed:27044889).
CC {ECO:0000269|PubMed:15096053, ECO:0000269|PubMed:16427015,
CC ECO:0000269|PubMed:16428438, ECO:0000269|PubMed:18508771,
CC ECO:0000269|PubMed:19805280, ECO:0000269|PubMed:20508643,
CC ECO:0000269|PubMed:21070969, ECO:0000269|PubMed:27044889,
CC ECO:0000269|PubMed:8890162}.
CC -!- INTERACTION:
CC P36037; P25694: CDC48; NbExp=6; IntAct=EBI-6017, EBI-4308;
CC P36037; P38753: HSE1; NbExp=3; IntAct=EBI-6017, EBI-1382;
CC P36037; Q01477: UBP3; NbExp=4; IntAct=EBI-6017, EBI-19834;
CC P36037; Q01853: Vcp; Xeno; NbExp=2; IntAct=EBI-6017, EBI-80597;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:18508771, ECO:0000269|PubMed:27044889}. Cytoplasm
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18508771,
CC ECO:0000269|PubMed:27044889}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:27044889}; Peripheral membrane protein
CC {ECO:0000269|PubMed:27044889}; Cytoplasmic side
CC {ECO:0000269|PubMed:27044889}. Endosome membrane
CC {ECO:0000269|PubMed:18508771}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18508771}; Cytoplasmic side
CC {ECO:0000269|PubMed:18508771}. Note=Predominantly localizes to the
CC cytoplasm. Probably localizes to endosomes and mitochondria in a
CC transient manner. {ECO:0000269|PubMed:18508771,
CC ECO:0000269|PubMed:27044889}.
CC -!- DOMAIN: The WD repeats mediate interaction with ubiquitin.
CC {ECO:0000269|PubMed:21070969}.
CC -!- DOMAIN: The PUL domain is composed of 6 armadillo-like repeats and
CC mediates the interaction with CDC48 C-terminus.
CC {ECO:0000269|PubMed:16427015, ECO:0000269|PubMed:16428438,
CC ECO:0000269|PubMed:19805280}.
CC -!- DOMAIN: The PFU domain mediates interaction with ubiquitin.
CC {ECO:0000269|PubMed:16428438, ECO:0000269|PubMed:18508771}.
CC -!- DISRUPTION PHENOTYPE: Severely reduces cell growth in response to
CC misfolded protein, translation inhibition-induced, heat or
CC mitochondrial oxidative stresses but not in response to ER stress
CC (PubMed:16427015, PubMed:18508771, PubMed:16428438, PubMed:27044889).
CC {ECO:0000269|PubMed:16427015, ECO:0000269|PubMed:16428438,
CC ECO:0000269|PubMed:18508771, ECO:0000269|PubMed:27044889}.
CC -!- MISCELLANEOUS: Present with 6800 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat PLAP family. {ECO:0000305}.
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DR EMBL; U39947; AAA82258.1; -; Genomic_DNA.
DR EMBL; X75951; CAA53560.1; -; Genomic_DNA.
DR EMBL; Z28213; CAA82058.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08956.1; -; Genomic_DNA.
DR PIR; S38051; S38051.
DR RefSeq; NP_012709.1; NM_001179778.1.
DR PDB; 3GAE; X-ray; 1.60 A; A/B=464-715.
DR PDB; 3L3F; X-ray; 1.90 A; X=354-715.
DR PDB; 3ODT; X-ray; 1.35 A; A/B=2-300.
DR PDB; 3PSP; X-ray; 2.42 A; A=325-715.
DR PDB; 3PST; X-ray; 2.00 A; A=325-715.
DR PDBsum; 3GAE; -.
DR PDBsum; 3L3F; -.
DR PDBsum; 3ODT; -.
DR PDBsum; 3PSP; -.
DR PDBsum; 3PST; -.
DR AlphaFoldDB; P36037; -.
DR SMR; P36037; -.
DR BioGRID; 33952; 701.
DR DIP; DIP-6274N; -.
DR IntAct; P36037; 10.
DR MINT; P36037; -.
DR STRING; 4932.YKL213C; -.
DR TCDB; 3.A.16.1.6; the endoplasmic reticular retrotranslocon (er-rt) family.
DR iPTMnet; P36037; -.
DR MaxQB; P36037; -.
DR PaxDb; P36037; -.
DR PRIDE; P36037; -.
DR EnsemblFungi; YKL213C_mRNA; YKL213C; YKL213C.
DR GeneID; 853667; -.
DR KEGG; sce:YKL213C; -.
DR SGD; S000001696; DOA1.
DR VEuPathDB; FungiDB:YKL213C; -.
DR eggNOG; KOG0301; Eukaryota.
DR GeneTree; ENSGT00550000074944; -.
DR HOGENOM; CLU_011791_2_0_1; -.
DR InParanoid; P36037; -.
DR OMA; WSKVGDV; -.
DR BioCyc; YEAST:G3O-31971-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR EvolutionaryTrace; P36037; -.
DR PRO; PR:P36037; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36037; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0032473; C:cytoplasmic side of mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IMP:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0140036; F:ubiquitin-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
DR GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0034517; P:ribophagy; IMP:SGD.
DR GO; GO:0010992; P:ubiquitin recycling; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.10.20.870; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015155; PFU.
DR InterPro; IPR038122; PFU_sf.
DR InterPro; IPR013535; PUL_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF09070; PFU; 1.
DR Pfam; PF08324; PUL; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51394; PFU; 1.
DR PROSITE; PS51396; PUL; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Endosome; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..715
FT /note="Protein DOA1"
FT /id="PRO_0000050958"
FT REPEAT 11..40
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 53..82
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 97..125
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 135..166
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 177..206
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 218..247
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 259..288
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT DOMAIN 352..449
FT /note="PFU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00727"
FT DOMAIN 465..715
FT /note="PUL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00729"
FT REPEAT 478..512
FT /note="ARM 1"
FT /evidence="ECO:0000269|PubMed:21063153,
FT ECO:0000305|PubMed:19805280"
FT REPEAT 513..543
FT /note="ARM 2"
FT /evidence="ECO:0000269|PubMed:21063153,
FT ECO:0000305|PubMed:19805280"
FT REPEAT 544..582
FT /note="ARM 3"
FT /evidence="ECO:0000269|PubMed:21063153,
FT ECO:0000305|PubMed:19805280"
FT REPEAT 583..635
FT /note="ARM 4"
FT /evidence="ECO:0000269|PubMed:21063153,
FT ECO:0000305|PubMed:19805280"
FT REPEAT 636..680
FT /note="ARM 5"
FT /evidence="ECO:0000269|PubMed:21063153,
FT ECO:0000305|PubMed:19805280"
FT REPEAT 681..715
FT /note="ARM 6"
FT /evidence="ECO:0000269|PubMed:21063153,
FT ECO:0000305|PubMed:19805280"
FT REGION 434..440
FT /note="Interaction with HSE1"
FT /evidence="ECO:0000269|PubMed:18508771"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 2..425
FT /note="Missing: No binding to ubiquitin but does not affect
FT the interaction with CDC48."
FT /evidence="ECO:0000269|PubMed:16427015"
FT MUTAGEN 2..359
FT /note="Missing: No binding to ubiquitin."
FT /evidence="ECO:0000269|PubMed:16427015"
FT MUTAGEN 2..353
FT /note="Missing: No binding to ubiquitin."
FT /evidence="ECO:0000269|PubMed:16428438"
FT MUTAGEN 2..330
FT /note="Missing: Does not affect binding to ubiquitin."
FT /evidence="ECO:0000269|PubMed:16428438"
FT MUTAGEN 2..287
FT /note="Missing: No binding to ubiquitin."
FT /evidence="ECO:0000269|PubMed:16427015"
FT MUTAGEN 5
FT /note="L->S: No binding to ubiquitin."
FT /evidence="ECO:0000269|PubMed:21070969"
FT MUTAGEN 15
FT /note="D->S: No binding to ubiquitin. Reduces cell growth
FT at high temperatures (37 degrees Celsius). Inhibits cell
FT growth at high temperatures and prevents the degradation of
FT mitochondrial proteins FZO1, MDM34 and MSP1 without
FT affecting the interaction with CDC48 and UFD1; when
FT associated with A-222 and A-265."
FT /evidence="ECO:0000269|PubMed:21070969,
FT ECO:0000269|PubMed:27044889"
FT MUTAGEN 158
FT /note="A->E: No binding to ubiquitin."
FT /evidence="ECO:0000269|PubMed:21070969"
FT MUTAGEN 222
FT /note="F->A: No binding to ubiquitin. Inhibits cell growth
FT at high temperatures and prevents the degradation of
FT mitochondrial proteins FZO1, MDM34 and MSP1 without
FT affecting the interaction with CDC48 and UFD1; when
FT associated with S-15 and A-265."
FT /evidence="ECO:0000269|PubMed:21070969,
FT ECO:0000269|PubMed:27044889"
FT MUTAGEN 237
FT /note="C->Y: In ufd3-2; severe reduction in the degradation
FT of short-lived ubiquitin-fusion proteins. No defect in the
FT interaction with CDC48."
FT /evidence="ECO:0000269|PubMed:8890162"
FT MUTAGEN 265
FT /note="W->A: No binding to ubiquitin. Inhibits cell growth
FT at high temperatures and prevents the degradation of
FT mitochondrial proteins FZO1, MDM34 and MSP1 without
FT affecting the interaction with CDC48 and UFD1; when
FT associated with S-15 and A-222."
FT /evidence="ECO:0000269|PubMed:21070969,
FT ECO:0000269|PubMed:27044889"
FT MUTAGEN 281
FT /note="D->S: No binding to ubiquitin."
FT /evidence="ECO:0000269|PubMed:21070969"
FT MUTAGEN 289..715
FT /note="Missing: No binding to ubiquitin."
FT /evidence="ECO:0000269|PubMed:16427015"
FT MUTAGEN 417
FT /note="F->D: Prevents binding to mono-ubiquitin, reduces
FT levels of free ubiquitin, prevents the degradation of
FT mitochondrial proteins FZO1, MDM34 and MSP1 and is
FT partially sensitive to misfolded protein or translation
FT inhibition-induced stresses; when associated with D-434."
FT /evidence="ECO:0000269|PubMed:16428438,
FT ECO:0000269|PubMed:27044889"
FT MUTAGEN 426..715
FT /note="Missing: No binding to ubiquitin and no interaction
FT with CDC48."
FT /evidence="ECO:0000269|PubMed:16427015,
FT ECO:0000269|PubMed:16428438"
FT MUTAGEN 434..443
FT /note="Missing: Loss of interaction with HSE1 and ubiquitin
FT without affecting general ubquitination levels. Prevents
FT protease CSP1 sorting into the vacuole."
FT /evidence="ECO:0000269|PubMed:18508771"
FT MUTAGEN 434..440
FT /note="FILKNTN->AAAKAAA: Loss of interaction with HSE1
FT without affecting binding to ubiquitin or general
FT ubquitination levels. Prevents protease CSP1 sorting into
FT the vacuole."
FT /evidence="ECO:0000269|PubMed:18508771"
FT MUTAGEN 434
FT /note="F->D: Prevents binding to mono-ubiquitin, reduces
FT levels of free ubiquitin, prevents the degradation of
FT mitochondrial proteins FZO1, MDM34 and MSP1 and is
FT partially sensitive to misfolded protein or translation
FT inhibition-induced stresses; when associated with D-417."
FT /evidence="ECO:0000269|PubMed:16428438,
FT ECO:0000269|PubMed:27044889"
FT MUTAGEN 451..715
FT /note="Missing: Does not affect binding to ubiquitin."
FT /evidence="ECO:0000269|PubMed:16428438"
FT MUTAGEN 495..715
FT /note="Missing: Loss of interaction with CDC48 without
FT affecting binding to ubiquitin."
FT /evidence="ECO:0000269|PubMed:16427015"
FT MUTAGEN 541
FT /note="R->A: Depletion of cellular ubiquitin pools and
FT reduced activity of the ubiquitin fusion degradation
FT pathway. Prevents the interaction with CDC48 and UFD1 and
FT thus the degradation of mitochondrial proteins FZO1, MDM34
FT and MSP1; when associated with A-669."
FT /evidence="ECO:0000269|PubMed:19805280,
FT ECO:0000269|PubMed:27044889"
FT MUTAGEN 669
FT /note="R->A: Depletion of cellular ubiquitin pools and
FT reduced activity of the ubiquitin fusion degradation
FT pathway. Prevents the interaction with CDC48 and UFD1 and
FT thus the degradation of mitochondrial proteins FZO1, MDM34
FT and MSP1; when associated with A-541."
FT /evidence="ECO:0000269|PubMed:19805280,
FT ECO:0000269|PubMed:27044889"
FT CONFLICT 180
FT /note="D -> DI (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 34..52
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:3ODT"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:3ODT"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:3ODT"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:3ODT"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:3ODT"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:3ODT"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:3L3F"
FT STRAND 383..391
FT /evidence="ECO:0007829|PDB:3L3F"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:3L3F"
FT HELIX 410..420
FT /evidence="ECO:0007829|PDB:3L3F"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:3L3F"
FT HELIX 428..438
FT /evidence="ECO:0007829|PDB:3L3F"
FT HELIX 480..494
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 499..509
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 512..529
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 534..543
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 544..546
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 550..553
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 554..560
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 566..579
FT /evidence="ECO:0007829|PDB:3GAE"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 586..590
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 593..596
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 599..602
FT /evidence="ECO:0007829|PDB:3GAE"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:3PSP"
FT HELIX 612..634
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 642..651
FT /evidence="ECO:0007829|PDB:3GAE"
FT TURN 652..656
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 658..662
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 664..680
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 682..685
FT /evidence="ECO:0007829|PDB:3GAE"
FT TURN 688..690
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 692..701
FT /evidence="ECO:0007829|PDB:3GAE"
FT HELIX 705..714
FT /evidence="ECO:0007829|PDB:3GAE"
SQ SEQUENCE 715 AA; 79506 MW; 593B808169283B5F CRC64;
MGYQLSATLK GHDQDVRDVV AVDDSKVASV SRDGTVRLWS KDDQWLGTVV YTGQGFLNSV
CYDSEKELLL FGGKDTMING VPLFATSGED PLYTLIGHQG NVCSLSFQDG VVISGSWDKT
AKVWKEGSLV YNLQAHNASV WDAKVVSFSE NKFLTASADK TIKLWQNDKV IKTFSGIHND
VVRHLAVVDD GHFISCSNDG LIKLVDMHTG DVLRTYEGHE SFVYCIKLLP NGDIVSCGED
RTVRIWSKEN GSLKQVITLP AISIWSVDCM SNGDIIVGSS DNLVRIFSQE KSRWASEDEI
NELSTQVEKS TISSKTIEFD ESKLSPYEIL QSPGRKEGQI VVVKSPQGTI EAHQFSNSSW
KKVGDVVGAG ATGNDKKIEF EGKTYDYVFD VDIEDGKPPL KLPINVSDNP YTAADNFLAR
YELPMSYRDQ VVQFILKNTN GISLDQPNDN ASSSAVSPSK TSVMKVLPVK QYLIMENYNP
DTIFNGIVKI NSNEKTFDDE ILAQIGGALH DIDESWELLL SFANTIRSNW EIKTPAYDIV
RLIVKKLPYS SDIKDYIEEG LGNKNITLTM LTVRILVNCF NNENWGVKLL ESNQVYKSIF
ETIDTEFSQA SAKQSQNLAI AVSTLIFNYS ALVTKGNSDL ELLPIVADAI NTKYGPLEEY
QECEEAAYRL TVAYGNLATV EPTLRQFANS VTWLANIKRS YGNVPRFKDI FDDLS
