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UniProtKB/Swiss-Prot entry P38995


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

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Entry information
Entry name ATU2_YEAST
Primary accession number P38995
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 22, 2008 (Entry version 86)
Name and origin of the protein
Protein name Copper-transporting ATPase
Synonyms EC 3.6.3.4
Cu(2+)-ATPase
Gene name
Name: CCC2
OrderedLocusNames: YDR270W
ORFNames: D9954.6
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].
PubMed=7785328 [NCBI, ExPASy, EBI, Israel, Japan]
Fu D., Beeler T.J., Dunn T.M.;
"Sequence, mapping and disruption of CCC2, a gene that cross-complements the Ca(2+)-sensitive phenotype of csg1 mutants and encodes a P-type ATPase belonging to the Cu(2+)-ATPase subfamily.";
Yeast 11:283-292(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
METAL-BINDING SITES.
DOI=10.1074/jbc.M104807200; PubMed=11500502 [NCBI, ExPASy, EBI, Israel, Japan]
Arnesano F., Banci L., Bertini I., Cantini F., Ciofi-Baffoni S., Huffman D.L., O'Halloran T.V.;
"Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase.";
J. Biol. Chem. 276:41365-41376(2001).
[4]
STRUCTURE BY NMR OF 1-72 IN APO AND COPPER-BOUND FORMS.
DOI=10.1074/jbc.M008389200; PubMed=11083871 [NCBI, ExPASy, EBI, Israel, Japan]
Banci L., Bertini I., Ciofi-Baffoni S., Huffman D.L., O'Halloran T.V.;
"Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states.";
J. Biol. Chem. 276:8415-8426(2001).
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
L36317; AAC37425.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U51030; AAB64451.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S55353; S55353.
RefSeq NP_010556.1; -.
3D structure databases
PDB
1FVQ; NMR; -; A=2-72.[ExPASy / RCSB / EBI]
1FVS; NMR; -; A=2-72.[ExPASy / RCSB / EBI]
1UV1; Model; -; B=2-72.[ExPASy / RCSB / EBI]
1UV2; Model; -; B=2-72.[ExPASy / RCSB / EBI]
2GGP; NMR; -; B=2-72.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FVQ; -.
1FVS; -.
1UV1; -.
1UV2; -.
2GGP; -.
ModBase P38995.
Protein-protein interaction databases
DIP DIP:906N; -.
Organism-specific databases
CYGD YDR270w; -.
SGD S000002678; CCC2.
Yeast-GFP YDR270W.
Gene expression databases
ArrayExpress P38995; -.
GermOnline YDR270W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0012510; Cellular component: trans-Golgi network transport vesicle membrane (inferred from direct assay from SGD).
GO:0019829; Molecular function: cation-transporting ATPase activity (inferred from direct assay from SGD).
GO:0005507; Molecular function: copper ion binding (inferred from direct assay from SGD).
GO:0006879; Biological process: cellular iron ion homeostasis (inferred from mutant phenotype from SGD).
GO:0015680; Biological process: intracellular copper ion transport (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR006416; ATPase-IB_hvy.
IPR001757; ATPase_P.
IPR006403; ATPase_P_cat/Cu.
IPR005834; Dehalogen-like_hydro.
IPR008250; E1-E2_ATPase_reg.
IPR006121; HeavyMe_transpt.
Graphical view of domain structure.
PANTHER PTHR11939; ATPase_P; 1.
Pfam PF00122; E1-E2_ATPase; 1.
PF00403; HMA; 2.
PF00702; Hydrolase; 1.
Pfam graphical view of domain structure.
PRINTS PR00119; CATATPASE.
TIGRFAMs TIGR01511; ATPase-IB1_Cu; 1.
TIGR01525; ATPase-IB_hvy; 1.
TIGR01494; ATPase_P-type; 2.
PROSITE PS00154; ATPASE_E1_E2; 1.
PS01047; HMA_1; 2.
PS50846; HMA_2; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS P38995.
Genome annotation databases
Ensembl YDR270W; Saccharomyces cerevisiae. [Contig view]
GeneID 851862; -.
GenomeReviews Z71256_GR; YDR270W.
KEGG sce:YDR270W; -.
NMPDR fig|4932.3.peg.1318; -.
Phylogenomic databases
HOGENOM P38995; -.
Other
LinkHub P38995; -.
ProtoNet P38995.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Complete proteome; Copper; Copper transport; Golgi apparatus; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Repeat; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   1004  1004     Copper-transporting ATPase. PRO_0000046318
TOPO_DOM   1    262  262     Cytoplasmic (Potential). 
TRANSMEM   263    283  21     Potential. 
TOPO_DOM   284    303  20     Lumenal, vesicle (Potential). 
TRANSMEM   304    324  21     Potential. 
TOPO_DOM   325    335  11     Cytoplasmic (Potential). 
TRANSMEM   336    356  21     Potential. 
TOPO_DOM   357    370  14     Lumenal, vesicle (Potential). 
TRANSMEM   371    391  21     Potential. 
TOPO_DOM   392    528  137     Cytoplasmic (Potential). 
TRANSMEM   529    549  21     Potential. 
TOPO_DOM   550    577  28     Lumenal, vesicle (Potential). 
TRANSMEM   578    598  21     Potential. 
TOPO_DOM   599    901  303     Cytoplasmic (Potential). 
TRANSMEM   902    924  23     Potential. 
TOPO_DOM   925    927  3     Lumenal, vesicle (Potential). 
TRANSMEM   928    950  23     Potential. 
TOPO_DOM   951   1004  54     Cytoplasmic (Potential). 
DOMAIN   3     68  66     HMA 1. 
DOMAIN   81    147  67     HMA 2. 
ACT_SITE   627    627        4-aspartylphosphate intermediate (By similarity). 
METAL   13     13        Copper. 
METAL   16     16        Copper. 
METAL   91     91        Copper (Potential). 
METAL   94     94        Copper (Potential). 
METAL   838    838        Magnesium (By similarity). 
METAL   842    842        Magnesium (By similarity). 
STRAND   2      8  7      
HELIX   14     25  12      
STRAND   27     33  7      
TURN   37     40  4      
STRAND   41     46  6      
HELIX   52     62  11      
STRAND   66     70  5      
Sequence information
Length: 1004 AA [This is the length of the unprocessed precursor] Molecular weight: 109829 Da [This is the MW of the unprocessed precursor] CRC64: 571E9F73EA1F599F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MREVILAVHG MTCSACTNTI NTQLRALKGV TKCDISLVTN ECQVTYDNEV TADSIKEIIE 

        70         80         90        100        110        120 
DCGFDCEILR DSEITAISTK EGLLSVQGMT CGSCVSTVTK QVEGIEGVES VVVSLVTEEC 

       130        140        150        160        170        180 
HVIYEPSKTT LETAREMIED CGFDSNIIMD GNGNADMTEK TVILKVTKAF EDESPLILSS 

       190        200        210        220        230        240 
VSERFQFLLD LGVKSIEISD DMHTLTIKYC CNELGIRDLL RHLERTGYKF TVFSNLDNTT 

       250        260        270        280        290        300 
QLRLLSKEDE IRFWKKNSIK STLLAIICML LYMIVPMMWP TIVQDRIFPY KETSFVRGLF 

       310        320        330        340        350        360 
YRDILGVILA SYIQFSVGFY FYKAAWASLK HGSGTMDTLV CVSTTCAYTF SVFSLVHNMF 

       370        380        390        400        410        420 
HPSSTGKLPR IVFDTSIMII SYISIGKYLE TLAKSQTSTA LSKLIQLTPS VCSIISDVER 

       430        440        450        460        470        480 
NETKEIPIEL LQVNDIVEIK PGMKIPADGI ITRGESEIDE SLMTGESILV PKKTGFPVIA 

       490        500        510        520        530        540 
GSVNGPGHFY FRTTTVGEET KLANIIKVMK EAQLSKAPIQ GYADYLASIF VPGILILAVL 

       550        560        570        580        590        600 
TFFIWCFILN ISANPPVAFT ANTKADNFFI CLQTATSVVI VACPCALGLA TPTAIMVGTG 

       610        620        630        640        650        660 
VGAQNGVLIK GGEVLEKFNS ITTFVFDKTG TLTTGFMVVK KFLKDSNWVG NVDEDEVLAC 

       670        680        690        700        710        720 
IKATESISDH PVSKAIIRYC DGLNCNKALN AVVLESEYVL GKGIVSKCQV NGNTYDICIG 

       730        740        750        760        770        780 
NEALILEDAL KKSGFINSNV DQGNTVSYVS VNGHVFGLFE INDEVKHDSY ATVQYLQRNG 

       790        800        810        820        830        840 
YETYMITGDN NSAAKRVARE VGISFENVYS DVSPTGKCDL VKKIQDKEGN NKVAVVGDGI 

       850        860        870        880        890        900 
NDAPALALSD LGIAISTGTE IAIEAADIVI LCGNDLNTNS LRGLANAIDI SLKTFKRIKL 

       910        920        930        940        950        960 
NLFWALCYNI FMIPIAMGVL IPWGITLPPM LAGLAMAFSS VSVVLSSLML KKWTPPDIES 

       970        980        990       1000 
HGISDFKSKF SIGNFWSRLF STRAIAGEQD IESQAGLMSN EEVL 

P38995 in FASTA format

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View entry in raw text format (no links)
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