UniProtKB - P40318 (DOA10_YEAST)
Protein
ERAD-associated E3 ubiquitin-protein ligase DOA10
Gene
SSM4
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
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 (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). Mediates the degradation of a broad range of substrates, including endoplasmic reticulum membrane proteins (ERQC), soluble nuclear proteins and soluble cytoplasmic proteins (CytoQC) (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). 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 (PubMed:16873066). ERAD-C substrates are ubiquitinated through DOA10 in conjunction with the E2 ubiquitin-conjugating enzymes UBC6 and UBC7-CUE1 (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). 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 (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468). Also recognizes the N-terminally acetylated residue of proteins as degradation signal (degron) (PubMed:20110468). N-terminally acetylated target proteins include MATALPHA2, TBF1, SLK19, YMR090W, HIS3, HSP104, UBP6 and ARO8 (PubMed:20110468). Catalyzes ubiquitination of mislocalized tail-anchored proteins that are extracted from the mitochondrion membrane by MSP1: following extraction, mistargeted proteins are transferred to the endoplasmic retuculum, where they are ubiquitinated by DOA10 and degraded by the proteasome (PubMed:31445887).8 Publications
Catalytic activityi
- S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.1 Publication EC:2.3.2.27
: protein ubiquitination Pathwayi
This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.1 PublicationView all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 31 – 100 | RING-CH-typePROSITE-ProRule annotationAdd BLAST | 70 |
GO - Molecular functioni
- ubiquitin protein ligase activity Source: SGD
- ubiquitin-protein transferase activity Source: SGD
- zinc ion binding Source: InterPro
GO - Biological processi
- retrograde protein transport, ER to cytosol Source: SGD
- ubiquitin-dependent ERAD pathway Source: SGD
Keywordsi
Molecular function | Transferase |
Biological process | Ubl conjugation pathway |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BioCyci | MetaCyc:G3O-31303-MONOMER |
UniPathwayi | UPA00143 |
Protein family/group databases
TCDBi | 3.A.16.1.2, the endoplasmic reticular retrotranslocon (er-rt) family |
Names & Taxonomyi
Protein namesi | Recommended name: ERAD-associated E3 ubiquitin-protein ligase DOA10 (EC:2.3.2.271 Publication)Alternative name(s): RING-type E3 ubiquitin transferase DOA10Curated |
Gene namesi | Name:SSM4 Synonyms:DOA10 Ordered Locus Names:YIL030C ORF Names:YI3299.01C, YI9905.18C |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000001292, SSM4 |
VEuPathDBi | FungiDB:YIL030C |
Subcellular locationi
Nucleus
- Nucleus inner membrane 2 Publications; Multi-pass membrane protein Sequence analysis
Endoplasmic reticulum
- Endoplasmic reticulum membrane 2 Publications; Multi-pass membrane protein Sequence analysis
Endoplasmic reticulum
- Doa10p ubiquitin ligase complex Source: SGD
- endoplasmic reticulum Source: SGD
- integral component of endoplasmic reticulum membrane Source: SGD
Nucleus
- nuclear envelope Source: SGD
- nuclear inner membrane Source: SGD
Other locations
- integral component of membrane Source: ParkinsonsUK-UCL
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 131 | CytoplasmicSequence analysisAdd BLAST | 131 | |
Transmembranei | 132 – 152 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 153 – 203 | LumenalSequence analysisAdd BLAST | 51 | |
Transmembranei | 204 – 224 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 225 – 468 | CytoplasmicSequence analysisAdd BLAST | 244 | |
Transmembranei | 469 – 489 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 490 – 491 | LumenalSequence analysis | 2 | |
Transmembranei | 492 – 512 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 513 – 626 | CytoplasmicSequence analysisAdd BLAST | 114 | |
Transmembranei | 627 – 647 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 648 – 660 | LumenalSequence analysisAdd BLAST | 13 | |
Transmembranei | 661 – 681 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 682 – 739 | CytoplasmicSequence analysisAdd BLAST | 58 | |
Transmembranei | 740 – 760 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 761 – 777 | LumenalSequence analysisAdd BLAST | 17 | |
Transmembranei | 778 – 797 | HelicalSequence analysisAdd BLAST | 20 | |
Topological domaini | 798 – 965 | CytoplasmicSequence analysisAdd BLAST | 168 | |
Transmembranei | 966 – 986 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 987 – 1019 | LumenalSequence analysisAdd BLAST | 33 | |
Transmembranei | 1020 – 1040 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1041 – 1113 | CytoplasmicSequence analysisAdd BLAST | 73 | |
Transmembranei | 1114 – 1134 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1135 – 1168 | LumenalSequence analysisAdd BLAST | 34 | |
Transmembranei | 1169 – 1189 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1190 – 1213 | CytoplasmicSequence analysisAdd BLAST | 24 | |
Transmembranei | 1214 – 1234 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1235 – 1270 | LumenalSequence analysisAdd BLAST | 36 | |
Transmembranei | 1271 – 1291 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1292 – 1319 | CytoplasmicSequence analysisAdd BLAST | 28 |
Keywords - Cellular componenti
Endoplasmic reticulum, Membrane, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000072214 | 1 – 1319 | ERAD-associated E3 ubiquitin-protein ligase DOA10Add BLAST | 1319 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineCombined sources | 1 |
Keywords - PTMi
AcetylationProteomic databases
MaxQBi | P40318 |
PaxDbi | P40318 |
PRIDEi | P40318 |
PTM databases
iPTMneti | P40318 |
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 PublicationsBinary interactionsi
Hide detailsP40318
With | #Exp. | IntAct |
---|---|---|
CDC48 [P25694] | 4 | EBI-18208,EBI-4308 |
CUE1 [P38428] | 2 | EBI-18208,EBI-27580 |
STE6 [P12866] | 3 | EBI-18208,EBI-18383 |
UBX2 [Q04228] | 5 | EBI-18208,EBI-27730 |
Protein-protein interaction databases
BioGRIDi | 34959, 255 interactors |
ComplexPortali | CPX-3074, Doa10 ubiquitin ligase complex |
DIPi | DIP-7286N |
IntActi | P40318, 83 interactors |
MINTi | P40318 |
STRINGi | 4932.YIL030C |
Miscellaneous databases
RNActi | P40318, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
BMRBi | P40318 |
SMRi | P40318 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 288 – 291 | Poly-Ala | 4 | |
Compositional biasi | 293 – 296 | Poly-Asn | 4 | |
Compositional biasi | 332 – 341 | Asp/Gln/Ser-rich (acidic) | 10 | |
Compositional biasi | 369 – 374 | Poly-Gln | 6 |
Domaini
The RING-CH-type zinc finger domain is required for E3 ligase activity.
Sequence similaritiesi
Belongs to the DOA10/MARCH6 family.Curated
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 31 – 100 | RING-CH-typePROSITE-ProRule annotationAdd BLAST | 70 |
Keywords - Domaini
Transmembrane, Transmembrane helix, Zinc-fingerPhylogenomic databases
eggNOGi | KOG1609, Eukaryota |
GeneTreei | ENSGT00940000155171 |
HOGENOMi | CLU_006729_0_0_1 |
InParanoidi | P40318 |
OMAi | LRLSHFI |
Family and domain databases
Gene3Di | 3.30.40.10, 1 hit |
InterProi | View protein in InterPro IPR011016, Znf_RING-CH IPR013083, Znf_RING/FYVE/PHD |
Pfami | View protein in Pfam PF12906, RINGv, 1 hit |
SMARTi | View protein in SMART SM00744, RINGv, 1 hit |
PROSITEi | View protein in PROSITE PS51292, ZF_RING_CH, 1 hit |
i Sequence
Sequence statusi: Complete.
P40318-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 241 | L → F in CAA54133 (PubMed:7816042).Curated | 1 | |
Sequence conflicti | 743 | A → T in CAA54133 (PubMed:7816042).Curated | 1 | |
Sequence conflicti | 1085 | N → D in CAA54133 (PubMed:7816042).Curated | 1 | |
Sequence conflicti | 1186 | Y → F in CAA54133 (PubMed:7816042).Curated | 1 |
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 |
PIRi | S49951 |
RefSeqi | NP_012234.3, NM_001179380.3 |
Genome annotation databases
EnsemblFungii | YIL030C_mRNA; YIL030C; YIL030C |
GeneIDi | 854781 |
KEGGi | sce:YIL030C |
Similar proteinsi
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 |
PIRi | S49951 |
RefSeqi | NP_012234.3, NM_001179380.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2M6M | NMR | - | A | 19-101 | [»] | |
BMRBi | P40318 | |||||
SMRi | P40318 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 34959, 255 interactors |
ComplexPortali | CPX-3074, Doa10 ubiquitin ligase complex |
DIPi | DIP-7286N |
IntActi | P40318, 83 interactors |
MINTi | P40318 |
STRINGi | 4932.YIL030C |
Protein family/group databases
TCDBi | 3.A.16.1.2, the endoplasmic reticular retrotranslocon (er-rt) family |
PTM databases
iPTMneti | P40318 |
Proteomic databases
MaxQBi | P40318 |
PaxDbi | P40318 |
PRIDEi | P40318 |
Genome annotation databases
EnsemblFungii | YIL030C_mRNA; YIL030C; YIL030C |
GeneIDi | 854781 |
KEGGi | sce:YIL030C |
Organism-specific databases
SGDi | S000001292, SSM4 |
VEuPathDBi | FungiDB:YIL030C |
Phylogenomic databases
eggNOGi | KOG1609, Eukaryota |
GeneTreei | ENSGT00940000155171 |
HOGENOMi | CLU_006729_0_0_1 |
InParanoidi | P40318 |
OMAi | LRLSHFI |
Enzyme and pathway databases
UniPathwayi | UPA00143 |
BioCyci | MetaCyc:G3O-31303-MONOMER |
Miscellaneous databases
PROi | PR:P40318 |
RNActi | P40318, protein |
Family and domain databases
Gene3Di | 3.30.40.10, 1 hit |
InterProi | View protein in InterPro IPR011016, Znf_RING-CH IPR013083, Znf_RING/FYVE/PHD |
Pfami | View protein in Pfam PF12906, RINGv, 1 hit |
SMARTi | View protein in SMART SM00744, RINGv, 1 hit |
PROSITEi | View protein in PROSITE PS51292, ZF_RING_CH, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DOA10_YEAST | |
Accessioni | P40318Primary (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: | February 10, 2021 | |
This is version 182 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome IX
Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families