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UniProtKB/Swiss-Prot entry P40318

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SSM4_YEAST
Primary accession number P40318
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 1, 1995 (Sequence version 1)
Annotations were last modified on    July 1, 2008 (Entry version 68)
Name and origin of the protein
Protein name E3 ubiquitin-protein ligase Doa10
Synonym EC 6.3.2.-
Gene name
Name: SSM4
Synonyms: DOA10
OrderedLocusNames: YIL030C
ORFNames: YI3299.01C, YI9905.18C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 28383 / FL100 / VTT C-80102;
DOI=10.1007/BF00290112; PubMed=7816042 [NCBI, ExPASy, EBI, Israel, Japan]
Mandart E., Dufour M.-E., Lacroute F.;
"Inactivation of SSM4, a new Saccharomyces cerevisiae gene, suppresses mRNA instability due to RNA14 mutations.";
Mol. Gen. Genet. 245:323-333(1994).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169870 [NCBI, ExPASy, EBI, Israel, Japan]
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., Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
Nature 387:84-87(1997).
[3]
 FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1101/gad.933301; PubMed=11641273 [NCBI, ExPASy, EBI, Israel, Japan]
Swanson R., Locher M., Hochstrasser M.;
"A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation.";
Genes Dev. 15:2660-2674(2001).
[4]
 INTERACTION WITH SEL1; UBC6 AND UBC7, AND IDENTIFICATION IN COMPLEX WITH SEL1 AND CDC48.
DOI=10.1038/ncb1298; PubMed=16179953 [NCBI, ExPASy, EBI, Israel, Japan]
Neuber O., Jarosch E., Volkwein C., Walter J., Sommer T.;
"Ubx2 links the Cdc48 complex to ER-associated protein degradation.";
Nat. Cell Biol. 7:993-998(2005).
[5]
 FUNCTION, AND IDENTIFICATION IN COMPLEX WITH SEL1; CDC48 AND UFD1.
DOI=10.1038/ncb1299; PubMed=16179952 [NCBI, ExPASy, EBI, Israel, Japan]
Schuberth C., Buchberger A.;
"Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation.";
Nat. Cell Biol. 7:999-1006(2005).
[6]
 FUNCTION, AND IDENTIFICATION IN THE ERAD-C COMPLEX WITH UBC7; CUE1; CDC48, NPL4 AND SEL1.
DOI=10.1016/j.cell.2006.05.043; PubMed=16873066 [NCBI, ExPASy, EBI, Israel, Japan]
Carvalho P., Goder V., Rapoport T.A.;
"Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins.";
Cell 126:361-373(2006).
[7]
 FUNCTION.
DOI=10.1038/sj.emboj.7600946; PubMed=16437165 [NCBI, ExPASy, EBI, Israel, Japan]
Ravid T., Kreft S.G., Hochstrasser M.;
"Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways.";
EMBO J. 25:533-543(2006).
[8]
 TOPOLOGY.
DOI=10.1074/jbc.M512215200; PubMed=16373356 [NCBI, ExPASy, EBI, Israel, Japan]
Kreft S.G., Wang L., Hochstrasser M.;
"Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI).";
J. Biol. Chem. 281:4646-4653(2006).
[9]
 SUBCELLULAR LOCATION, AND FUNCTION.
DOI=10.1038/nature05170; PubMed=17051211 [NCBI, ExPASy, EBI, Israel, Japan]
Deng M., Hochstrasser M.;
"Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase.";
Nature 443:827-831(2006).
[10]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-897, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
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 0:0-0(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X76715; CAA54133.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46881; CAA86961.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46861; CAA86921.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S49951; S49951.
RefSeq NP_012234.1; -.
3D structure databases
ModBase P40318.
Protein-protein interaction databases
DIP DIP:7286N; -.
IntAct P40318; -.
Organism-specific databases
CYGD YIL030c; -.
SGD S000001292; SSM4.
Yeast-GFP YIL030C.
Gene expression databases
ArrayExpress P40318; -.
GermOnline YIL030C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0000837; Cellular component: Doa10p ubiquitin ligase complex (inferred from direct assay from SGD).
GO:0030176; Cellular component: integral to endoplasmic reticulum membrane (inferred from direct assay from SGD).
GO:0005637; Cellular component: nuclear inner membrane (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004842; Molecular function: ubiquitin-protein ligase activity (inferred from direct assay from SGD).
GO:0030433; Biological process: ER-associated protein catabolic process (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR001841; Znf_RING.
IPR013083; Znf_RING/FYVE/PHD.
IPR011016; ZnF_var-RING.
Graphical view of domain structure.
Gene3D G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
Pfam PF00097; zf-C3HC4; 1.
Pfam graphical view of domain structure.
SMART SM00744; RINGv; 1.
SMART graphical view of domain structure.
PROSITE PS51292; ZF_RING_CH; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P40318.
Proteomic databases
PeptideAtlas P40318; -.
Genome annotation databases
Ensembl YIL030C; Saccharomyces cerevisiae. [Contig view]
GeneID 854781; -.
GenomeReviews Z47047_GR; YIL030C.
KEGG sce:YIL030C; -.
NMPDR fig|4932.3.peg.1768; -.
Phylogenomic databases
HOGENOM P40318; -.
Other
LinkHub P40318; -.
ProtoNet P40318.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Endoplasmic reticulum; Ligase; Membrane; Metal-binding; Nucleus; Phosphoprotein; Transmembrane; Ubl conjugation pathway; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1319  1319     E3 ubiquitin-protein ligase Doa10. PRO_0000072214
TOPO_DOM   1    131  131     Cytoplasmic (Potential). 
TRANSMEM   132    152  21     Potential. 
TOPO_DOM   153    203  51     Extracellular (Potential). 
TRANSMEM   204    224  21     Potential. 
TOPO_DOM   225    468  244     Cytoplasmic (Potential). 
TRANSMEM   469    489  21     Potential. 
TOPO_DOM   490    491  2     Extracellular (Potential). 
TRANSMEM   492    512  21     Potential. 
TOPO_DOM   513    626  114     Cytoplasmic (Potential). 
TRANSMEM   627    647  21     Potential. 
TOPO_DOM   648    660  13     Extracellular (Potential). 
TRANSMEM   661    681  21     Potential. 
TOPO_DOM   682    739  58     Cytoplasmic (Potential). 
TRANSMEM   740    760  21     Potential. 
TOPO_DOM   761    965  205     Extracellular (Potential). 
TRANSMEM   966    986  21     Potential. 
TOPO_DOM   987    988  2     Cytoplasmic (Potential). 
TRANSMEM   989   1009  21     Potential. 
TOPO_DOM   1010   1019  10     Extracellular (Potential). 
TRANSMEM   1020   1040  21     Potential. 
TOPO_DOM   1041   1113  73     Cytoplasmic (Potential). 
TRANSMEM   1114   1134  21     Potential. 
TOPO_DOM   1135   1168  34     Extracellular (Potential). 
TRANSMEM   1169   1189  21     Potential. 
TOPO_DOM   1190   1213  24     Cytoplasmic (Potential). 
TRANSMEM   1214   1234  21     Potential. 
TOPO_DOM   1235   1270  36     Extracellular (Potential). 
TRANSMEM   1271   1291  21     Potential. 
TOPO_DOM   1292   1319  28     Cytoplasmic (Potential). 
ZN_FING   31    100  70     RING-CH-type. 
COMPBIAS   288    291  4     Poly-Ala. 
COMPBIAS   293    296  4     Poly-Asn. 
COMPBIAS   332    341  10     Asp/Gln/Ser-rich (acidic). 
COMPBIAS   369    374  6     Poly-Gln. 
MOD_RES   897    897        Phosphoserine. 
CONFLICT   241    241        L -> F (in Ref. 1; CAA54133). 
CONFLICT   743    743        A -> T (in Ref. 1; CAA54133). 
CONFLICT   1085   1085        N -> D (in Ref. 1; CAA54133). 
CONFLICT   1186   1186        Y -> F (in Ref. 1; CAA54133). 
Sequence information
Length: 1319 AA [This is the length of the unprocessed precursor] Molecular weight: 151455 Da [This is the MW of the unprocessed precursor] CRC64: 3EDFF7F9D90A0C8C [This is a checksum on the sequence] 
        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
P40318 in FASTA format

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