Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P40318 (DOA10_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ERAD-associated E3 ubiquitin-protein ligase DOA10

EC=6.3.2.-
Gene names
Name:SSM4
Synonyms:DOA10
Ordered Locus Names:YIL030C
ORF Names:YI3299.01C, YI9905.18C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1319 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC6 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of a broad range of substrates, inluding endoplasmic reticulum membrane proteins (ERQC), soluble nuclear proteins and soluble cytoplasmic proteins (CytoQC). Component of the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains. ERAD-C substrates are ubiquitinated through DOA10 in conjunction with the E2 ubiquitin-conjugating enzymes UBC6 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex and targeted to the proteasome. Also recognizes the N-terminally acetylated residue of proteins as degradation signal (degron). N-terminally acetylated target proteins include MATALPHA2, TBF1, SLK19, YMR090W, HIS3, HSP104, UBP6 and ARO8. Ref.4 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.14

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Component of the DOA10 complex which contains SSM4/DOA10, CDC48, NPL4, UFD1 AND UBX2/SEL1. The complex is composed of the membrane integral E3 ligase SSM4/DOA10 and the heterotrimeric UFD1-NPL4-CDC48/p97 (UNC) ATPase complex recruited by UBX2/SEL1. Interacts with UBX2/SEL1. Interacts also with its associated ubiquitin conjugating enzymesh UBC6 and UBC7 with its membrane anchor CUE1. Interacts with PEX29. Ref.5 Ref.6 Ref.7 Ref.13

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus inner membrane; Multi-pass membrane protein Ref.4 Ref.10.

Domain

The RING-CH-type zinc finger domain is required for E3 ligase activity.

Sequence similarities

Belongs to the DOA10/MARCH6 family.

Contains 1 RING-CH-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13191319ERAD-associated E3 ubiquitin-protein ligase DOA10
PRO_0000072214

Regions

Topological domain1 – 131131Cytoplasmic Potential
Transmembrane132 – 15221Helical; Potential
Topological domain153 – 20351Lumenal Potential
Transmembrane204 – 22421Helical; Potential
Topological domain225 – 468244Cytoplasmic Potential
Transmembrane469 – 48921Helical; Potential
Topological domain490 – 4912Lumenal Potential
Transmembrane492 – 51221Helical; Potential
Topological domain513 – 626114Cytoplasmic Potential
Transmembrane627 – 64721Helical; Potential
Topological domain648 – 66013Lumenal Potential
Transmembrane661 – 68121Helical; Potential
Topological domain682 – 73958Cytoplasmic Potential
Transmembrane740 – 76021Helical; Potential
Topological domain761 – 77717Lumenal Potential
Transmembrane778 – 79720Helical; Potential
Topological domain798 – 965168Cytoplasmic Potential
Transmembrane966 – 98621Helical; Potential
Topological domain987 – 101933Lumenal Potential
Transmembrane1020 – 104021Helical; Potential
Topological domain1041 – 111373Cytoplasmic Potential
Transmembrane1114 – 113421Helical; Potential
Topological domain1135 – 116834Lumenal Potential
Transmembrane1169 – 118921Helical; Potential
Topological domain1190 – 121324Cytoplasmic Potential
Transmembrane1214 – 123421Helical; Potential
Topological domain1235 – 127036Lumenal Potential
Transmembrane1271 – 129121Helical; Potential
Topological domain1292 – 131928Cytoplasmic Potential
Zinc finger31 – 10070RING-CH-type
Compositional bias288 – 2914Poly-Ala
Compositional bias293 – 2964Poly-Asn
Compositional bias332 – 34110Asp/Gln/Ser-rich (acidic)
Compositional bias369 – 3746Poly-Gln

Amino acid modifications

Modified residue11N-acetylmethionine Ref.15

Experimental info

Sequence conflict2411L → F in CAA54133. Ref.1
Sequence conflict7431A → T in CAA54133. Ref.1
Sequence conflict10851N → D in CAA54133. Ref.1
Sequence conflict11861Y → F in CAA54133. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P40318 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 3EDFF7F9D90A0C8C

FASTA1,319151,455
        10         20         30         40         50         60 
MDVDSDVNVS RLRDELHKVA NEETDTATFN DDAPSGATCR ICRGEATEDN PLFHPCKCRG 

        70         80         90        100        110        120 
SIKYMHESCL LEWVASKNID ISKPGADVKC DICHYPIQFK TIYAENMPEK IPFSLLLSKS 

       130        140        150        160        170        180 
ILTFFEKARL ALTIGLAAVL YIIGVPLVWN MFGKLYTMML DGSSPYPGDF LKSLIYGYDQ 

       190        200        210        220        230        240 
SATPELTTRA IFYQLLQNHS FTSLQFIMIV ILHIALYFQY DMIVREDVFS KMVFHKIGPR 

       250        260        270        280        290        300 
LSPKDLKSRL KERFPMMDDR MVEYLAREMR AHDENRQEQG HDRLNMPAAA ADNNNNVINP 

       310        320        330        340        350        360 
RNDNVPPQDP NDHRNFENLR HVDELDHDEA TEEHENNDSD NSLPSGDDSS RILPGSSSDN 

       370        380        390        400        410        420 
EEDEEAEGQQ QQQQPEEEAD YRDHIEPNPI DMWANRRAQN EFDDLIAAQQ NAINRPNAPV 

       430        440        450        460        470        480 
FIPPPAQNRA GNVDQDEQDF GAAVGVPPAQ ANPDDQGQGP LVINLKLKLL NVIAYFIIAV 

       490        500        510        520        530        540 
VFTAIYLAIS YLFPTFIGFG LLKIYFGIFK VILRGLCHLY YLSGAHIAYN GLTKLVPKVD 

       550        560        570        580        590        600 
VAMSWISDHL IHDIIYLYNG YTENTMKHSI FIRALPALTT YLTSVSIVCA SSNLVSRGYG 

       610        620        630        640        650        660 
RENGMSNPTR RLIFQILFAL KCTFKVFTLF FIELAGFPIL AGVMLDFSLF CPILASNSRM 

       670        680        690        700        710        720 
LWVPSICAIW PPFSLFVYWT IGTLYMYWFA KYIGMIRKNI IRPGVLFFIR SPEDPNIKIL 

       730        740        750        760        770        780 
HDSLIHPMSI QLSRLCLSMF IYAIFIVLGF GFHTRIFFPF MLKSNLLSVP EAYKPTSIIS 

       790        800        810        820        830        840 
WKFNTILLTL YFTKRILESS SYVKPLLERY WKTIFKLCSR KLRLSSFILG KDTPTERGHI 

       850        860        870        880        890        900 
VYRNLFYKYI AAKNAEWSNQ ELFTKPKTLE QAEELFGQVR DVHAYFVPDG VLMRVPSSDI 

       910        920        930        940        950        960 
VSRNYVQTMF VPVTKDDKLL KPLDLERIKE RNKRAAGEFG YLDEQNTEYD QYYIVYVPPD 

       970        980        990       1000       1010       1020 
FRLRYMTLLG LVWLFASILM LGVTFISQAL INFVCSFGFL PVVKLLLGER NKVYVAWKEL 

      1030       1040       1050       1060       1070       1080 
SDISYSYLNI YYVCVGSVCL SKIAKDILHF TEGQNTLDEH AVDENEVEEV EHDIPERDIN 

      1090       1100       1110       1120       1130       1140 
NAPVNNINNV EEGQGIFMAI FNSIFDSMLV KYNLMVFIAI MIAVIRTMVS WVVLTDGILA 

      1150       1160       1170       1180       1190       1200 
CYNYLTIRVF GNSSYTIGNS KWFKYDESLL FVVWIISSMV NFGTGYKSLK LFFRNRNTSK 

      1210       1220       1230       1240       1250       1260 
LNFLKTMALE LFKQGFLHMV IYVLPIIILS LVFLRDVSTK QIIDISHGSR SFTLSLNESF 

      1270       1280       1290       1300       1310 
PTWTRMQDIY FGLLIALESF TFFFQATVLF IQWFKSTVQN VKDEVYTKGR ALENLPDES 

« Hide

References

« Hide 'large scale' references
[1]"Inactivation of SSM4, a new Saccharomyces cerevisiae gene, suppresses mRNA instability due to RNA14 mutations."
Mandart E., Dufour M.-E., Lacroute F.
Mol. Gen. Genet. 245:323-333(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 28383 / FL100 / VTT C-80102.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
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.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation."
Swanson R., Locher M., Hochstrasser M.
Genes Dev. 15:2660-2674(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]"Ubx2 links the Cdc48 complex to ER-associated protein degradation."
Neuber O., Jarosch E., Volkwein C., Walter J., Sommer T.
Nat. Cell Biol. 7:993-998(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBX2; UBC6 AND UBC7, IDENTIFICATION IN COMPLEX WITH UBX2 AND CDC48.
[6]"Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation."
Schuberth C., Buchberger A.
Nat. Cell Biol. 7:999-1006(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH UBX2; CDC48 AND UFD1.
[7]"Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins."
Carvalho P., Goder V., Rapoport T.A.
Cell 126:361-373(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE DOA10 COMPLEX WITH CDC48; NPL4; UFD1 AND UBX2.
[8]"Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways."
Ravid T., Kreft S.G., Hochstrasser M.
EMBO J. 25:533-543(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI)."
Kreft S.G., Wang L., Hochstrasser M.
J. Biol. Chem. 281:4646-4653(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY.
[10]"Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase."
Deng M., Hochstrasser M.
Nature 443:827-831(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[11]"Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery."
Metzger M.B., Maurer M.J., Dancy B.M., Michaelis S.
J. Biol. Chem. 283:32302-32316(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CYTOSOLIC PROTEIN DEGRADATION.
[12]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10 substrates."
Liu C., van Dyk D., Xu P., Choe V., Pan H., Peng J., Andrews B., Rao H.
J. Biol. Chem. 285:10265-10272(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PEX29.
[14]"N-terminal acetylation of cellular proteins creates specific degradation signals."
Hwang C.S., Shemorry A., Varshavsky A.
Science 327:973-977(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN N-ACETYLATED PROTEIN DEGRADATION.
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X76715 Genomic DNA. Translation: CAA54133.1.
Z46881 Genomic DNA. Translation: CAA86961.1.
Z46861 Genomic DNA. Translation: CAA86921.1.
BK006942 Genomic DNA. Translation: DAA08517.1.
PIRS49951.
RefSeqNP_012234.3. NM_001179380.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2M6MNMR-A19-101[»]
ProteinModelPortalP40318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34959. 166 interactions.
DIPDIP-7286N.
IntActP40318. 81 interactions.
MINTMINT-1361830.
STRING4932.YIL030C.

Proteomic databases

MaxQBP40318.
PaxDbP40318.
PeptideAtlasP40318.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL030C; YIL030C; YIL030C.
GeneID854781.
KEGGsce:YIL030C.

Organism-specific databases

CYGDYIL030c.
SGDS000001292. SSM4.

Phylogenomic databases

eggNOGCOG5183.
GeneTreeENSGT00730000110355.
KOK10661.
OMASHFILGK.
OrthoDBEOG7G1VFT.

Enzyme and pathway databases

BioCycYEAST:G3O-31303-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorP40318.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF12906. RINGv. 1 hit.
[Graphical view]
SMARTSM00744. RINGv. 1 hit.
[Graphical view]
PROSITEPS51292. ZF_RING_CH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977562.
PROP40318.

Entry information

Entry nameDOA10_YEAST
AccessionPrimary (citable) accession number: P40318
Secondary accession number(s): D6VVQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways