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Protein

ERAD-associated E3 ubiquitin-protein ligase DOA10

Gene

SSM4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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, including 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 ARO8.7 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri31 – 100RING-CH-typePROSITE-ProRule annotationAdd BLAST70

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: SGD
  • ubiquitin protein ligase activity involved in ERAD pathway Source: ParkinsonsUK-UCL
  • ubiquitin-protein transferase activity Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • ER-associated ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-31303-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
ERAD-associated E3 ubiquitin-protein ligase DOA10 (EC:6.3.2.-)
Gene namesi
Name:SSM4
Synonyms:DOA10
Ordered Locus Names:YIL030C
ORF Names:YI3299.01C, YI9905.18C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL030C.
SGDiS000001292. SSM4.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 131CytoplasmicSequence analysisAdd BLAST131
Transmembranei132 – 152HelicalSequence analysisAdd BLAST21
Topological domaini153 – 203LumenalSequence analysisAdd BLAST51
Transmembranei204 – 224HelicalSequence analysisAdd BLAST21
Topological domaini225 – 468CytoplasmicSequence analysisAdd BLAST244
Transmembranei469 – 489HelicalSequence analysisAdd BLAST21
Topological domaini490 – 491LumenalSequence analysis2
Transmembranei492 – 512HelicalSequence analysisAdd BLAST21
Topological domaini513 – 626CytoplasmicSequence analysisAdd BLAST114
Transmembranei627 – 647HelicalSequence analysisAdd BLAST21
Topological domaini648 – 660LumenalSequence analysisAdd BLAST13
Transmembranei661 – 681HelicalSequence analysisAdd BLAST21
Topological domaini682 – 739CytoplasmicSequence analysisAdd BLAST58
Transmembranei740 – 760HelicalSequence analysisAdd BLAST21
Topological domaini761 – 777LumenalSequence analysisAdd BLAST17
Transmembranei778 – 797HelicalSequence analysisAdd BLAST20
Topological domaini798 – 965CytoplasmicSequence analysisAdd BLAST168
Transmembranei966 – 986HelicalSequence analysisAdd BLAST21
Topological domaini987 – 1019LumenalSequence analysisAdd BLAST33
Transmembranei1020 – 1040HelicalSequence analysisAdd BLAST21
Topological domaini1041 – 1113CytoplasmicSequence analysisAdd BLAST73
Transmembranei1114 – 1134HelicalSequence analysisAdd BLAST21
Topological domaini1135 – 1168LumenalSequence analysisAdd BLAST34
Transmembranei1169 – 1189HelicalSequence analysisAdd BLAST21
Topological domaini1190 – 1213CytoplasmicSequence analysisAdd BLAST24
Transmembranei1214 – 1234HelicalSequence analysisAdd BLAST21
Topological domaini1235 – 1270LumenalSequence analysisAdd BLAST36
Transmembranei1271 – 1291HelicalSequence analysisAdd BLAST21
Topological domaini1292 – 1319CytoplasmicSequence analysisAdd BLAST28

GO - Cellular componenti

  • Doa10p ubiquitin ligase complex Source: SGD
  • integral component of endoplasmic reticulum membrane Source: SGD
  • integral component of membrane Source: ParkinsonsUK-UCL
  • nuclear envelope Source: SGD
  • nuclear inner membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000722141 – 1319ERAD-associated E3 ubiquitin-protein ligase DOA10Add BLAST1319

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP40318.
PRIDEiP40318.

PTM databases

iPTMnetiP40318.

Interactioni

Subunit structurei

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 PEX29.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC48P256944EBI-18208,EBI-4308
CUE1P384282EBI-18208,EBI-27580
STE6P128662EBI-18208,EBI-18383
UBX2Q042285EBI-18208,EBI-27730

Protein-protein interaction databases

BioGridi34959. 166 interactors.
DIPiDIP-7286N.
IntActiP40318. 81 interactors.
MINTiMINT-1361830.

Structurei

Secondary structure

11319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 42Combined sources3
Beta strandi48 – 50Combined sources3
Helixi67 – 76Combined sources10
Beta strandi91 – 93Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M6MNMR-A19-101[»]
ProteinModelPortaliP40318.
SMRiP40318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi288 – 291Poly-Ala4
Compositional biasi293 – 296Poly-Asn4
Compositional biasi332 – 341Asp/Gln/Ser-rich (acidic)10
Compositional biasi369 – 374Poly-Gln6

Domaini

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

Sequence similaritiesi

Belongs to the DOA10/MARCH6 family.Curated
Contains 1 RING-CH-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri31 – 100RING-CH-typePROSITE-ProRule annotationAdd BLAST70

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00730000110355.
InParanoidiP40318.
KOiK10661.
OMAiSHFILGK.
OrthoDBiEOG092C0DLV.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF12906. RINGv. 1 hit.
[Graphical view]
SMARTiSM00744. RINGv. 1 hit.
[Graphical view]
PROSITEiPS51292. ZF_RING_CH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40318-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVDSDVNVS RLRDELHKVA NEETDTATFN DDAPSGATCR ICRGEATEDN
60 70 80 90 100
PLFHPCKCRG SIKYMHESCL LEWVASKNID ISKPGADVKC DICHYPIQFK
110 120 130 140 150
TIYAENMPEK IPFSLLLSKS ILTFFEKARL ALTIGLAAVL YIIGVPLVWN
160 170 180 190 200
MFGKLYTMML DGSSPYPGDF LKSLIYGYDQ SATPELTTRA IFYQLLQNHS
210 220 230 240 250
FTSLQFIMIV ILHIALYFQY DMIVREDVFS KMVFHKIGPR LSPKDLKSRL
260 270 280 290 300
KERFPMMDDR MVEYLAREMR AHDENRQEQG HDRLNMPAAA ADNNNNVINP
310 320 330 340 350
RNDNVPPQDP NDHRNFENLR HVDELDHDEA TEEHENNDSD NSLPSGDDSS
360 370 380 390 400
RILPGSSSDN EEDEEAEGQQ QQQQPEEEAD YRDHIEPNPI DMWANRRAQN
410 420 430 440 450
EFDDLIAAQQ NAINRPNAPV FIPPPAQNRA GNVDQDEQDF GAAVGVPPAQ
460 470 480 490 500
ANPDDQGQGP LVINLKLKLL NVIAYFIIAV VFTAIYLAIS YLFPTFIGFG
510 520 530 540 550
LLKIYFGIFK VILRGLCHLY YLSGAHIAYN GLTKLVPKVD VAMSWISDHL
560 570 580 590 600
IHDIIYLYNG YTENTMKHSI FIRALPALTT YLTSVSIVCA SSNLVSRGYG
610 620 630 640 650
RENGMSNPTR RLIFQILFAL KCTFKVFTLF FIELAGFPIL AGVMLDFSLF
660 670 680 690 700
CPILASNSRM LWVPSICAIW PPFSLFVYWT IGTLYMYWFA KYIGMIRKNI
710 720 730 740 750
IRPGVLFFIR SPEDPNIKIL HDSLIHPMSI QLSRLCLSMF IYAIFIVLGF
760 770 780 790 800
GFHTRIFFPF MLKSNLLSVP EAYKPTSIIS WKFNTILLTL YFTKRILESS
810 820 830 840 850
SYVKPLLERY WKTIFKLCSR KLRLSSFILG KDTPTERGHI VYRNLFYKYI
860 870 880 890 900
AAKNAEWSNQ ELFTKPKTLE QAEELFGQVR DVHAYFVPDG VLMRVPSSDI
910 920 930 940 950
VSRNYVQTMF VPVTKDDKLL KPLDLERIKE RNKRAAGEFG YLDEQNTEYD
960 970 980 990 1000
QYYIVYVPPD FRLRYMTLLG LVWLFASILM LGVTFISQAL INFVCSFGFL
1010 1020 1030 1040 1050
PVVKLLLGER NKVYVAWKEL SDISYSYLNI YYVCVGSVCL SKIAKDILHF
1060 1070 1080 1090 1100
TEGQNTLDEH AVDENEVEEV EHDIPERDIN NAPVNNINNV EEGQGIFMAI
1110 1120 1130 1140 1150
FNSIFDSMLV KYNLMVFIAI MIAVIRTMVS WVVLTDGILA CYNYLTIRVF
1160 1170 1180 1190 1200
GNSSYTIGNS KWFKYDESLL FVVWIISSMV NFGTGYKSLK LFFRNRNTSK
1210 1220 1230 1240 1250
LNFLKTMALE LFKQGFLHMV IYVLPIIILS LVFLRDVSTK QIIDISHGSR
1260 1270 1280 1290 1300
SFTLSLNESF PTWTRMQDIY FGLLIALESF TFFFQATVLF IQWFKSTVQN
1310
VKDEVYTKGR ALENLPDES
Length:1,319
Mass (Da):151,455
Last modified:February 1, 1995 - v1
Checksum:i3EDFF7F9D90A0C8C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti241L → F in CAA54133 (PubMed:7816042).Curated1
Sequence conflicti743A → T in CAA54133 (PubMed:7816042).Curated1
Sequence conflicti1085N → D in CAA54133 (PubMed:7816042).Curated1
Sequence conflicti1186Y → F in CAA54133 (PubMed:7816042).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76715 Genomic DNA. Translation: CAA54133.1.
Z46881 Genomic DNA. Translation: CAA86961.1.
Z46861 Genomic DNA. Translation: CAA86921.1.
BK006942 Genomic DNA. Translation: DAA08517.1.
PIRiS49951.
RefSeqiNP_012234.3. NM_001179380.3.

Genome annotation databases

EnsemblFungiiYIL030C; YIL030C; YIL030C.
GeneIDi854781.
KEGGisce:YIL030C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76715 Genomic DNA. Translation: CAA54133.1.
Z46881 Genomic DNA. Translation: CAA86961.1.
Z46861 Genomic DNA. Translation: CAA86921.1.
BK006942 Genomic DNA. Translation: DAA08517.1.
PIRiS49951.
RefSeqiNP_012234.3. NM_001179380.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M6MNMR-A19-101[»]
ProteinModelPortaliP40318.
SMRiP40318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34959. 166 interactors.
DIPiDIP-7286N.
IntActiP40318. 81 interactors.
MINTiMINT-1361830.

PTM databases

iPTMnetiP40318.

Proteomic databases

MaxQBiP40318.
PRIDEiP40318.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL030C; YIL030C; YIL030C.
GeneIDi854781.
KEGGisce:YIL030C.

Organism-specific databases

EuPathDBiFungiDB:YIL030C.
SGDiS000001292. SSM4.

Phylogenomic databases

GeneTreeiENSGT00730000110355.
InParanoidiP40318.
KOiK10661.
OMAiSHFILGK.
OrthoDBiEOG092C0DLV.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciYEAST:G3O-31303-MONOMER.

Miscellaneous databases

PROiP40318.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF12906. RINGv. 1 hit.
[Graphical view]
SMARTiSM00744. RINGv. 1 hit.
[Graphical view]
PROSITEiPS51292. ZF_RING_CH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDOA10_YEAST
AccessioniPrimary (citable) accession number: P40318
Secondary accession number(s): D6VVQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.