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Protein DOA1 (Degradation of alpha protein 1) (Ubiquitin fusion degradation protein 3)

 DOA1_YEAST              Reviewed;         715 AA.
P36037; D6VWZ0;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
25-MAY-2022, entry version 193.
RecName: Full=Protein DOA1 {ECO:0000303|PubMed:2111732};
AltName: Full=Degradation of alpha protein 1 {ECO:0000303|PubMed:2111732};
AltName: Full=Ubiquitin fusion degradation protein 3 {ECO:0000303|PubMed:7615550};
Name=DOA1 {ECO:0000303|PubMed:2111732, ECO:0000312|SGD:S000001696};
Synonyms=UFD3 {ECO:0000303|PubMed:7615550,
ECO:0000312|SGD:S000001696}, ZZZ4 {ECO:0000312|SGD:S000001696};
OrderedLocusNames=YKL213C {ECO:0000312|SGD:S000001696};
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Hochstrasser M., Gang G.;
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7941750; DOI=10.1002/yea.320100511;
Tzermia M., Horaitis O., Alexandraki D.;
"The complete sequencing of a 24.6 kb segment of yeast chromosome XI
identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open
reading frames including homologues to the threonine dehydratases, membrane
transporters, hydantoinases and the phospholipase A2-activating protein.";
Yeast 10:663-679(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
G3 (Bethesda) 4:389-398(2014).
[5]
PROTEIN SEQUENCE OF 126-144; 173-183; 215-227; 316-335; 345-361; 384-420;
534-541; 598-613; 654-685 AND 700-706, FUNCTION, AND INTERACTION WITH
UBIQUITIN.
PubMed=15096053; DOI=10.1021/bi035626r;
Russell N.S., Wilkinson K.D.;
"Identification of a novel 29-linked polyubiquitin binding protein, Ufd3,
using polyubiquitin chain analogues.";
Biochemistry 43:4844-4854(2004).
[6]
FUNCTION.
PubMed=2111732; DOI=10.1016/0092-8674(90)90481-s;
Hochstrasser M., Varshavsky A.;
"In vivo degradation of a transcriptional regulator: the yeast alpha 2
repressor.";
Cell 61:697-708(1990).
[7]
FUNCTION.
PubMed=7615550; DOI=10.1074/jbc.270.29.17442;
Johnson E.S., Ma P.C.M., Ota I.M., Varshavsky A.;
"A proteolytic pathway that recognizes ubiquitin as a degradation signal.";
J. Biol. Chem. 270:17442-17456(1995).
[8]
FUNCTION, INTERACTION WITH CDC48, AND MUTAGENESIS OF CYS-237.
PubMed=8890162; DOI=10.1002/j.1460-2075.1996.tb00869.x;
Ghislain M., Dohmen R.J., Levy F., Varshavsky A.;
"Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-
mediated proteolysis in Saccharomyces cerevisiae.";
EMBO J. 15:4884-4899(1996).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH NPL4; UFD1; CDC48; OTU1 AND
SHP1, INTERACTION WITH OTU1; UBIQUITIN AND CDC48, DOMAIN, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF 2-GLY--PHE-287; 2-GLY--SER-359;
2-GLY--MET-425; 426-SER--SER-715 AND 495-LYS--SER-715.
PubMed=16427015; DOI=10.1016/j.molcel.2005.12.014;
Rumpf S., Jentsch S.;
"Functional division of substrate processing cofactors of the ubiquitin-
selective Cdc48 chaperone.";
Mol. Cell 21:261-269(2006).
[12]
FUNCTION, INTERACTION WITH UBIQUITIN AND CDC48, DOMAIN, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF 2-GLY--HIS-253; 2-GLY--LEU-253; PHE-417;
426-SER--SER-715; PHE-434 AND 451-ALA--SER-715.
PubMed=16428438; DOI=10.1128/mcb.26.3.822-830.2006;
Mullally J.E., Chernova T., Wilkinson K.D.;
"Doa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domain.";
Mol. Cell. Biol. 26:822-830(2006).
[13]
FUNCTION, INTERACTION WITH HSE1, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF 434-PHE--ASN-440 AND 434-PHE--SER-443.
PubMed=18508771; DOI=10.1074/jbc.m802982200;
Ren J., Pashkova N., Winistorfer S., Piper R.C.;
"DOA1/UFD3 plays a role in sorting ubiquitinated membrane proteins into
multivesicular bodies.";
J. Biol. Chem. 283:21599-21611(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome
analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides insights
into evolution.";
Science 325:1682-1686(2009).
[16]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH UBP3; BRE5 AND CDC48, AND
INTERACTION WITH UBP3 AND CDC48.
PubMed=20508643; DOI=10.1038/embor.2010.74;
Ossareh-Nazari B., Bonizec M., Cohen M., Dokudovskaya S., Delalande F.,
Schaeffer C., Van Dorsselaer A., Dargemont C.;
"Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required
for ribophagy.";
EMBO Rep. 11:548-554(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
FUNCTION.
PubMed=23525333; DOI=10.1534/genetics.113.149898;
Au W.C., Dawson A.R., Rawson D.W., Taylor S.B., Baker R.E., Basrai M.A.;
"A novel role of the N terminus of budding yeast histone H3 variant Cse4 in
ubiquitin-mediated proteolysis.";
Genetics 194:513-518(2013).
[19]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDC48 AND FZO1, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF ASP-15; PHE-222; TRP-265; PHE-417; PHE-434;
ARG-541 AND ARG-669.
PubMed=27044889; DOI=10.1083/jcb.201510098;
Wu X., Li L., Jiang H.;
"Doa1 targets ubiquitinated substrates for mitochondria-associated
degradation.";
J. Cell Biol. 213:49-63(2016).
[20]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 464-715, FUNCTION, INTERACTION
WITH CDC48, DOMAIN, ARM REPEATS, AND MUTAGENESIS OF ARG-541 AND ARG-669.
PubMed=19805280; DOI=10.1073/pnas.0908321106;
Zhao G., Li G., Schindelin H., Lennarz W.J.;
"An Armadillo motif in Ufd3 interacts with Cdc48 and is involved in
ubiquitin homeostasis and protein degradation.";
Proc. Natl. Acad. Sci. U.S.A. 106:16197-16202(2009).
[21]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 354-715, AND ARM REPEATS.
PubMed=21063153;
Nishimasu R., Komori H., Higuchi Y., Nishimasu H., Hiroaki H.;
"Crystal structure of a PFU-PUL domain pair of Saccharomyces cerevisiae
Doa1/Ufd3.";
Kobe J. Med. Sci. 56:E125-E139(2010).
[22]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 2-300, INTERACTION WITH
UBIQUITIN, DOMAIN, AND MUTAGENESIS OF LEU-5; ASP-15; ALA-158; PHE-222;
TRP-265 AND ASP-281.
PubMed=21070969; DOI=10.1016/j.molcel.2010.10.018;
Pashkova N., Gakhar L., Winistorfer S.C., Yu L., Ramaswamy S., Piper R.C.;
"WD40 repeat propellers define a ubiquitin-binding domain that regulates
turnover of F box proteins.";
Mol. Cell 40:433-443(2010).
[23]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 325-715.
Liu Y., Sun J.;
"Crystal structure of PUL and PFU domain.";
Submitted (DEC-2010) to the PDB data bank.
-!- FUNCTION: Ubiquitin-binding protein involved in protein ubiquitination,
sorting and degradation (PubMed:2111732, PubMed:8890162,
PubMed:19805280, PubMed:18508771, PubMed:20508643, PubMed:27044889).
Acts as a ubiquitinated substrate-recruiting adapter for chaperone
ATPase CDC48 by binding mono- or polyubiquitin chains (PubMed:15096053,
PubMed:16427015, PubMed:16428438, PubMed:27044889). Depending on the
context, promotes or prevents proteasomal degradation of ubiquitinated
proteins (PubMed:2111732, PubMed:8890162, PubMed:19805280,
PubMed:27044889). Involved in the ubiquitin fusion degradation (UFD)
pathway by promoting the degradation of ubiquitinated proteins
(PubMed:2111732, PubMed:8890162, PubMed:19805280, PubMed:27044889).
Involved in the mitochondria-associated degradation pathway (MAD) by
promoting the degradation of several ubiquitinated membrane proteins
(PubMed:27044889). By competing with UFD2 to bind CDC48, prevents the
multi-ubiquitination and subsequent degradation of UFD2-dependent
substrates (PubMed:16427015). Required for ribophagy, a process which
relocalizes ribosomal particles into the vacuole for degradation in
response to starvation (PubMed:20508643). Involved in the ubiquitin-
mediated sorting of membrane proteins into multivesicular bodies (MVBs)
(PubMed:18508771). In addition, plays an essential role in maintaining
cellular ubiquitin levels (PubMed:7615550, PubMed:16427015,
PubMed:16428438, PubMed:18508771, PubMed:19805280). May affect
indirectly the degradation of ubiquitinylated proteins by regulating
cellular ubiquitin levels (PubMed:7615550, PubMed:23525333).
{ECO:0000269|PubMed:15096053, ECO:0000269|PubMed:16427015,
ECO:0000269|PubMed:16428438, ECO:0000269|PubMed:18508771,
ECO:0000269|PubMed:19805280, ECO:0000269|PubMed:20508643,
ECO:0000269|PubMed:2111732, ECO:0000269|PubMed:23525333,
ECO:0000269|PubMed:27044889, ECO:0000269|PubMed:7615550,
ECO:0000269|PubMed:8890162}.
-!- SUBUNIT: Forms a complex composed of CDC48, NPL4, UFD1, DOA1, SHP1 and
deubiquitinase OTU1; within the complex interacts with CDC48
(PubMed:16427015). Interacts (via PUL domain) with CDC48 (via C-
terminus); the interaction is direct (PubMed:8890162, PubMed:16427015,
PubMed:16428438, PubMed:27044889, PubMed:19805280, PubMed:20508643).
Forms a complex composed of CDC48, DOA1, deubiquitinase UBP3 and
probably BRE5; within the complex interacts with CDC48 and UBP3
(PubMed:20508643). May form a complex composed of VPS27, HSE1 and DOA1
(PubMed:18508771). Interacts with HSE1 (via SH3 domain)
(PubMed:18508771). Interacts (via WD repeats and PFU domain) with
ubiquitin; the interaction is direct (PubMed:15096053, PubMed:16427015,
PubMed:16428438, PubMed:21070969). Interacts with ubiquitinated FZO1
but not unmodified FZO1; the interaction recruits FZO1 to CDC48 and
promotes FZO1 proteasomal degradation (PubMed:27044889).
{ECO:0000269|PubMed:15096053, ECO:0000269|PubMed:16427015,
ECO:0000269|PubMed:16428438, ECO:0000269|PubMed:18508771,
ECO:0000269|PubMed:19805280, ECO:0000269|PubMed:20508643,
ECO:0000269|PubMed:21070969, ECO:0000269|PubMed:27044889,
ECO:0000269|PubMed:8890162}.
-!- INTERACTION:
P36037; P25694: CDC48; NbExp=6; IntAct=EBI-6017, EBI-4308;
P36037; P38753: HSE1; NbExp=3; IntAct=EBI-6017, EBI-1382;
P36037; Q01477: UBP3; NbExp=4; IntAct=EBI-6017, EBI-19834;
P36037; Q01853: Vcp; Xeno; NbExp=2; IntAct=EBI-6017, EBI-80597;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:18508771, ECO:0000269|PubMed:27044889}. Cytoplasm
{ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18508771,
ECO:0000269|PubMed:27044889}. Mitochondrion outer membrane
{ECO:0000269|PubMed:27044889}; Peripheral membrane protein
{ECO:0000269|PubMed:27044889}; Cytoplasmic side
{ECO:0000269|PubMed:27044889}. Endosome membrane
{ECO:0000269|PubMed:18508771}; Peripheral membrane protein
{ECO:0000269|PubMed:18508771}; Cytoplasmic side
{ECO:0000269|PubMed:18508771}. Note=Predominantly localizes to the
cytoplasm. Probably localizes to endosomes and mitochondria in a
transient manner. {ECO:0000269|PubMed:18508771,
ECO:0000269|PubMed:27044889}.
-!- DOMAIN: The WD repeats mediate interaction with ubiquitin.
{ECO:0000269|PubMed:21070969}.
-!- DOMAIN: The PUL domain is composed of 6 armadillo-like repeats and
mediates the interaction with CDC48 C-terminus.
{ECO:0000269|PubMed:16427015, ECO:0000269|PubMed:16428438,
ECO:0000269|PubMed:19805280}.
-!- DOMAIN: The PFU domain mediates interaction with ubiquitin.
{ECO:0000269|PubMed:16428438, ECO:0000269|PubMed:18508771}.
-!- DISRUPTION PHENOTYPE: Severely reduces cell growth in response to
misfolded protein, translation inhibition-induced, heat or
mitochondrial oxidative stresses but not in response to ER stress
(PubMed:16427015, PubMed:18508771, PubMed:16428438, PubMed:27044889).
{ECO:0000269|PubMed:16427015, ECO:0000269|PubMed:16428438,
ECO:0000269|PubMed:18508771, ECO:0000269|PubMed:27044889}.
-!- MISCELLANEOUS: Present with 6800 molecules/cell in log phase SD medium.
{ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the WD repeat PLAP family. {ECO:0000305}.
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EMBL; U39947; AAA82258.1; -; Genomic_DNA.
EMBL; X75951; CAA53560.1; -; Genomic_DNA.
EMBL; Z28213; CAA82058.1; -; Genomic_DNA.
EMBL; BK006944; DAA08956.1; -; Genomic_DNA.
PIR; S38051; S38051.
RefSeq; NP_012709.1; NM_001179778.1.
PDB; 3GAE; X-ray; 1.60 A; A/B=464-715.
PDB; 3L3F; X-ray; 1.90 A; X=354-715.
PDB; 3ODT; X-ray; 1.35 A; A/B=2-300.
PDB; 3PSP; X-ray; 2.42 A; A=325-715.
PDB; 3PST; X-ray; 2.00 A; A=325-715.
PDBsum; 3GAE; -.
PDBsum; 3L3F; -.
PDBsum; 3ODT; -.
PDBsum; 3PSP; -.
PDBsum; 3PST; -.
AlphaFoldDB; P36037; -.
SMR; P36037; -.
BioGRID; 33952; 701.
DIP; DIP-6274N; -.
IntAct; P36037; 10.
MINT; P36037; -.
STRING; 4932.YKL213C; -.
TCDB; 3.A.16.1.6; the endoplasmic reticular retrotranslocon (er-rt) family.
iPTMnet; P36037; -.
MaxQB; P36037; -.
PaxDb; P36037; -.
PRIDE; P36037; -.
EnsemblFungi; YKL213C_mRNA; YKL213C; YKL213C.
GeneID; 853667; -.
KEGG; sce:YKL213C; -.
SGD; S000001696; DOA1.
VEuPathDB; FungiDB:YKL213C; -.
eggNOG; KOG0301; Eukaryota.
GeneTree; ENSGT00550000074944; -.
HOGENOM; CLU_011791_2_0_1; -.
InParanoid; P36037; -.
OMA; WSKVGDV; -.
Reactome; R-SCE-8951664; Neddylation.
Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
EvolutionaryTrace; P36037; -.
PRO; PR:P36037; -.
Proteomes; UP000002311; Chromosome XI.
RNAct; P36037; protein.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0032473; C:cytoplasmic side of mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IMP:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
GO; GO:0140036; F:ubiquitin-dependent protein binding; IPI:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
GO; GO:0034517; P:ribophagy; IMP:SGD.
GO; GO:0010992; P:ubiquitin recycling; IMP:SGD.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 3.10.20.870; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015155; PFU.
InterPro; IPR038122; PFU_sf.
InterPro; IPR013535; PUL_dom.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF09070; PFU; 1.
Pfam; PF08324; PUL; 1.
Pfam; PF00400; WD40; 4.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 6.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS51394; PFU; 1.
PROSITE; PS51396; PUL; 1.
PROSITE; PS50082; WD_REPEATS_2; 4.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Cytoplasm; Direct protein sequencing; Endosome; Membrane;
Mitochondrion; Mitochondrion outer membrane; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
CHAIN 1..715
/note="Protein DOA1"
/id="PRO_0000050958"
REPEAT 11..40
/note="WD 1"
/evidence="ECO:0000255"
REPEAT 53..82
/note="WD 2"
/evidence="ECO:0000255"
REPEAT 97..125
/note="WD 3"
/evidence="ECO:0000255"
REPEAT 135..166
/note="WD 4"
/evidence="ECO:0000255"
REPEAT 177..206
/note="WD 5"
/evidence="ECO:0000255"
REPEAT 218..247
/note="WD 6"
/evidence="ECO:0000255"
REPEAT 259..288
/note="WD 7"
/evidence="ECO:0000255"
DOMAIN 352..449
/note="PFU"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00727"
DOMAIN 465..715
/note="PUL"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00729"
REPEAT 478..512
/note="ARM 1"
/evidence="ECO:0000269|PubMed:21063153,
ECO:0000305|PubMed:19805280"
REPEAT 513..543
/note="ARM 2"
/evidence="ECO:0000269|PubMed:21063153,
ECO:0000305|PubMed:19805280"
REPEAT 544..582
/note="ARM 3"
/evidence="ECO:0000269|PubMed:21063153,
ECO:0000305|PubMed:19805280"
REPEAT 583..635
/note="ARM 4"
/evidence="ECO:0000269|PubMed:21063153,
ECO:0000305|PubMed:19805280"
REPEAT 636..680
/note="ARM 5"
/evidence="ECO:0000269|PubMed:21063153,
ECO:0000305|PubMed:19805280"
REPEAT 681..715
/note="ARM 6"
/evidence="ECO:0000269|PubMed:21063153,
ECO:0000305|PubMed:19805280"
REGION 434..440
/note="Interaction with HSE1"
/evidence="ECO:0000269|PubMed:18508771"
MOD_RES 332
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18407956,
ECO:0007744|PubMed:19779198"
MUTAGEN 2..425
/note="Missing: No binding to ubiquitin but does not affect
the interaction with CDC48."
/evidence="ECO:0000269|PubMed:16427015"
MUTAGEN 2..359
/note="Missing: No binding to ubiquitin."
/evidence="ECO:0000269|PubMed:16427015"
MUTAGEN 2..353
/note="Missing: No binding to ubiquitin."
/evidence="ECO:0000269|PubMed:16428438"
MUTAGEN 2..330
/note="Missing: Does not affect binding to ubiquitin."
/evidence="ECO:0000269|PubMed:16428438"
MUTAGEN 2..287
/note="Missing: No binding to ubiquitin."
/evidence="ECO:0000269|PubMed:16427015"
MUTAGEN 5
/note="L->S: No binding to ubiquitin."
/evidence="ECO:0000269|PubMed:21070969"
MUTAGEN 15
/note="D->S: No binding to ubiquitin. Reduces cell growth
at high temperatures (37 degrees Celsius). Inhibits cell
growth at high temperatures and prevents the degradation of
mitochondrial proteins FZO1, MDM34 and MSP1 without
affecting the interaction with CDC48 and UFD1; when
associated with A-222 and A-265."
/evidence="ECO:0000269|PubMed:21070969,
ECO:0000269|PubMed:27044889"
MUTAGEN 158
/note="A->E: No binding to ubiquitin."
/evidence="ECO:0000269|PubMed:21070969"
MUTAGEN 222
/note="F->A: No binding to ubiquitin. Inhibits cell growth
at high temperatures and prevents the degradation of
mitochondrial proteins FZO1, MDM34 and MSP1 without
affecting the interaction with CDC48 and UFD1; when
associated with S-15 and A-265."
/evidence="ECO:0000269|PubMed:21070969,
ECO:0000269|PubMed:27044889"
MUTAGEN 237
/note="C->Y: In ufd3-2; severe reduction in the degradation
of short-lived ubiquitin-fusion proteins. No defect in the
interaction with CDC48."
/evidence="ECO:0000269|PubMed:8890162"
MUTAGEN 265
/note="W->A: No binding to ubiquitin. Inhibits cell growth
at high temperatures and prevents the degradation of
mitochondrial proteins FZO1, MDM34 and MSP1 without
affecting the interaction with CDC48 and UFD1; when
associated with S-15 and A-222."
/evidence="ECO:0000269|PubMed:21070969,
ECO:0000269|PubMed:27044889"
MUTAGEN 281
/note="D->S: No binding to ubiquitin."
/evidence="ECO:0000269|PubMed:21070969"
MUTAGEN 289..715
/note="Missing: No binding to ubiquitin."
/evidence="ECO:0000269|PubMed:16427015"
MUTAGEN 417
/note="F->D: Prevents binding to mono-ubiquitin, reduces
levels of free ubiquitin, prevents the degradation of
mitochondrial proteins FZO1, MDM34 and MSP1 and is
partially sensitive to misfolded protein or translation
inhibition-induced stresses; when associated with D-434."
/evidence="ECO:0000269|PubMed:16428438,
ECO:0000269|PubMed:27044889"
MUTAGEN 426..715
/note="Missing: No binding to ubiquitin and no interaction
with CDC48."
/evidence="ECO:0000269|PubMed:16427015,
ECO:0000269|PubMed:16428438"
MUTAGEN 434..443
/note="Missing: Loss of interaction with HSE1 and ubiquitin
without affecting general ubquitination levels. Prevents
protease CSP1 sorting into the vacuole."
/evidence="ECO:0000269|PubMed:18508771"
MUTAGEN 434..440
/note="FILKNTN->AAAKAAA: Loss of interaction with HSE1
without affecting binding to ubiquitin or general
ubquitination levels. Prevents protease CSP1 sorting into
the vacuole."
/evidence="ECO:0000269|PubMed:18508771"
MUTAGEN 434
/note="F->D: Prevents binding to mono-ubiquitin, reduces
levels of free ubiquitin, prevents the degradation of
mitochondrial proteins FZO1, MDM34 and MSP1 and is
partially sensitive to misfolded protein or translation
inhibition-induced stresses; when associated with D-417."
/evidence="ECO:0000269|PubMed:16428438,
ECO:0000269|PubMed:27044889"
MUTAGEN 451..715
/note="Missing: Does not affect binding to ubiquitin."
/evidence="ECO:0000269|PubMed:16428438"
MUTAGEN 495..715
/note="Missing: Loss of interaction with CDC48 without
affecting binding to ubiquitin."
/evidence="ECO:0000269|PubMed:16427015"
MUTAGEN 541
/note="R->A: Depletion of cellular ubiquitin pools and
reduced activity of the ubiquitin fusion degradation
pathway. Prevents the interaction with CDC48 and UFD1 and
thus the degradation of mitochondrial proteins FZO1, MDM34
and MSP1; when associated with A-669."
/evidence="ECO:0000269|PubMed:19805280,
ECO:0000269|PubMed:27044889"
MUTAGEN 669
/note="R->A: Depletion of cellular ubiquitin pools and
reduced activity of the ubiquitin fusion degradation
pathway. Prevents the interaction with CDC48 and UFD1 and
thus the degradation of mitochondrial proteins FZO1, MDM34
and MSP1; when associated with A-541."
/evidence="ECO:0000269|PubMed:19805280,
ECO:0000269|PubMed:27044889"
CONFLICT 180
/note="D -> DI (in Ref. 5; AA sequence)"
/evidence="ECO:0000305"
STRAND 4..9
/evidence="ECO:0007829|PDB:3ODT"
STRAND 16..23
/evidence="ECO:0007829|PDB:3ODT"
STRAND 26..31
/evidence="ECO:0007829|PDB:3ODT"
STRAND 34..52
/evidence="ECO:0007829|PDB:3ODT"
STRAND 57..63
/evidence="ECO:0007829|PDB:3ODT"
TURN 64..67
/evidence="ECO:0007829|PDB:3ODT"
STRAND 68..73
/evidence="ECO:0007829|PDB:3ODT"
STRAND 78..82
/evidence="ECO:0007829|PDB:3ODT"
STRAND 102..108
/evidence="ECO:0007829|PDB:3ODT"
STRAND 111..116
/evidence="ECO:0007829|PDB:3ODT"
STRAND 119..125
/evidence="ECO:0007829|PDB:3ODT"
STRAND 128..134
/evidence="ECO:0007829|PDB:3ODT"
STRAND 140..147
/evidence="ECO:0007829|PDB:3ODT"
TURN 148..151
/evidence="ECO:0007829|PDB:3ODT"
STRAND 152..157
/evidence="ECO:0007829|PDB:3ODT"
STRAND 162..166
/evidence="ECO:0007829|PDB:3ODT"
STRAND 169..174
/evidence="ECO:0007829|PDB:3ODT"
STRAND 182..189
/evidence="ECO:0007829|PDB:3ODT"
STRAND 192..197
/evidence="ECO:0007829|PDB:3ODT"
STRAND 200..206
/evidence="ECO:0007829|PDB:3ODT"
TURN 207..209
/evidence="ECO:0007829|PDB:3ODT"
STRAND 212..217
/evidence="ECO:0007829|PDB:3ODT"
STRAND 223..228
/evidence="ECO:0007829|PDB:3ODT"
STRAND 234..238
/evidence="ECO:0007829|PDB:3ODT"
STRAND 241..246
/evidence="ECO:0007829|PDB:3ODT"
TURN 248..250
/evidence="ECO:0007829|PDB:3ODT"
STRAND 253..258
/evidence="ECO:0007829|PDB:3ODT"
STRAND 260..262
/evidence="ECO:0007829|PDB:3ODT"
STRAND 264..269
/evidence="ECO:0007829|PDB:3ODT"
STRAND 275..279
/evidence="ECO:0007829|PDB:3ODT"
STRAND 284..289
/evidence="ECO:0007829|PDB:3ODT"
HELIX 291..293
/evidence="ECO:0007829|PDB:3ODT"
STRAND 378..380
/evidence="ECO:0007829|PDB:3L3F"
STRAND 383..391
/evidence="ECO:0007829|PDB:3L3F"
STRAND 400..404
/evidence="ECO:0007829|PDB:3L3F"
HELIX 410..420
/evidence="ECO:0007829|PDB:3L3F"
HELIX 425..427
/evidence="ECO:0007829|PDB:3L3F"
HELIX 428..438
/evidence="ECO:0007829|PDB:3L3F"
HELIX 480..494
/evidence="ECO:0007829|PDB:3GAE"
HELIX 499..509
/evidence="ECO:0007829|PDB:3GAE"
HELIX 512..529
/evidence="ECO:0007829|PDB:3GAE"
HELIX 534..543
/evidence="ECO:0007829|PDB:3GAE"
HELIX 544..546
/evidence="ECO:0007829|PDB:3GAE"
HELIX 550..553
/evidence="ECO:0007829|PDB:3GAE"
HELIX 554..560
/evidence="ECO:0007829|PDB:3GAE"
HELIX 566..579
/evidence="ECO:0007829|PDB:3GAE"
TURN 583..585
/evidence="ECO:0007829|PDB:3GAE"
HELIX 586..590
/evidence="ECO:0007829|PDB:3GAE"
HELIX 593..596
/evidence="ECO:0007829|PDB:3GAE"
HELIX 599..602
/evidence="ECO:0007829|PDB:3GAE"
STRAND 608..610
/evidence="ECO:0007829|PDB:3PSP"
HELIX 612..634
/evidence="ECO:0007829|PDB:3GAE"
HELIX 642..651
/evidence="ECO:0007829|PDB:3GAE"
TURN 652..656
/evidence="ECO:0007829|PDB:3GAE"
HELIX 658..662
/evidence="ECO:0007829|PDB:3GAE"
HELIX 664..680
/evidence="ECO:0007829|PDB:3GAE"
HELIX 682..685
/evidence="ECO:0007829|PDB:3GAE"
TURN 688..690
/evidence="ECO:0007829|PDB:3GAE"
HELIX 692..701
/evidence="ECO:0007829|PDB:3GAE"
HELIX 705..714
/evidence="ECO:0007829|PDB:3GAE"
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


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