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P38360 (ATU1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
P-type cation-transporting ATPase

EC=3.6.3.3
Alternative name(s):
Cadmium resistance protein 2
Cadmium-translocating P-type ATPase
Cd(2+)-exporting ATPase
Gene names
Name:PCA1
Synonyms:CAD2, PAY2
Ordered Locus Names:YBR295W
ORF Names:YBR2112
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1216 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cadmium transporting P-type ATPase which plays a critical role in cadmium resistance by extruding intracellular cadmium. Capable of high affinity copper ion binding, but not active copper ion transport. May play a role in copper resistance by chelating and sequestering copper ions. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Catalytic activity

ATP + H2O + Cd2+(In) = ADP + phosphate + Cd2+(Out).

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.7.

Post-translational modification

In the absence of cadmium, is ubiquitinated and targeted for degradation before reaching the plasma membrane. This allows a rapid and specific cellular response to cadmium.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]

Contains 1 HMA domain.

Caution

Although initial characterizations described PCA1 as a copper-transporting ATPase (Ref.1), subsequent experiments have demonstrated that PCA1 is capable of high affinity copper ion binding, but not active copper ion transport.

Strain S288C, as well as other laboratory cadmium-sensitive strains, contain a natural Gly-970-Arg mutation which eliminates cadmium transport function. Loss of cadmium resistance provides a fitness advantage under cadmium-free conditions.

Ontologies

Keywords
   Biological processCadmium resistance
Ion transport
Transport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Cadmium
Copper
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcadmium ion transmembrane transport

Inferred from mutant phenotype Ref.5Ref.7. Source: GOC

cadmium ion transport

Inferred from mutant phenotype Ref.7. Source: SGD

cellular iron ion homeostasis

Inferred from expression pattern Ref.6. Source: SGD

cellular metal ion homeostasis

Inferred from mutant phenotype Ref.5. Source: SGD

ion transmembrane transport

Inferred from sequence or structural similarity Ref.1. Source: GOC

response to cadmium ion

Inferred from electronic annotation. Source: UniProtKB-KW

transmembrane transport

Inferred from mutant phenotype Ref.7. Source: SGD

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay Ref.7. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism

Inferred from sequence or structural similarity Ref.1. Source: SGD

cadmium-exporting ATPase activity

Inferred from mutant phenotype Ref.5Ref.7. Source: SGD

copper ion binding

Inferred from mutant phenotype Ref.7. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12161216P-type cation-transporting ATPase
PRO_0000046317

Regions

Topological domain1 – 556556Cytoplasmic Potential
Transmembrane557 – 57822Helical; Potential
Topological domain579 – 59214Extracellular Potential
Transmembrane593 – 61220Helical; Potential
Topological domain613 – 6208Cytoplasmic Potential
Transmembrane621 – 64121Helical; Potential
Topological domain642 – 65918Extracellular Potential
Transmembrane660 – 68021Helical; Potential
Topological domain681 – 808128Cytoplasmic Potential
Transmembrane809 – 83123Helical; Potential
Topological domain832 – 84716Extracellular Potential
Transmembrane848 – 86518Helical; Potential
Topological domain866 – 1161296Cytoplasmic Potential
Transmembrane1162 – 118120Helical; Potential
Topological domain1182 – 11909Extracellular Potential
Transmembrane1191 – 120919Helical; Potential
Topological domain1210 – 12167Cytoplasmic Potential
Domain411 – 47464HMA
Region250 – 350101Metal-responding degradation signal

Sites

Active site90314-aspartylphosphate intermediate By similarity
Metal binding4211Copper Potential
Metal binding4241Copper Potential
Metal binding11071Magnesium By similarity
Metal binding11111Magnesium By similarity

Experimental info

Mutagenesis2981C → A: Abolishes copper resistance but not cadmium resistance; when associated with A-300. Ref.8
Mutagenesis3001C → A: Abolishes copper resistance but not cadmium resistance; when associated with A-298. Ref.8
Mutagenesis3111C → A: Abolishes cadmium resistance yet retains the ability to confer copper resistance; when associated with A-312. Ref.8
Mutagenesis3121C → A: Abolishes cadmium resistance yet retains the ability to confer copper resistance; when associated with A-311. Ref.8
Mutagenesis9701R → G: Confers localization to the plasma membrane and cadmium transport function. Ref.5 Ref.7
Sequence conflict3821H → T in CAA82529. Ref.1
Sequence conflict3821H → T in CAA85260. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P38360 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: E4DCAFB23AA1F138

FASTA1,216131,875
        10         20         30         40         50         60 
MKPEKLFSGL GTSDGEYGVV NSENISIDAM QDNRGECHRR SIEMHANDNL GLVSQRDCTN 

        70         80         90        100        110        120 
RPKITPQECL SETEQICHHG ENRTKAGLDV DDAETGGDHT NESRVDECCA EKVNDTETGL 

       130        140        150        160        170        180 
DVDSCCGDAQ TGGDHTNESC VDGCCVRDSS VMVEEVTGSC EAVSSKEQLL TSFEVVPSKS 

       190        200        210        220        230        240 
EGLQSIHDIR ETTRCNTNSN QHTGKGRLCI ESSDSTLKKR SCKVSRQKIE VSSKPECCNI 

       250        260        270        280        290        300 
SCVERIASRS CEKRTFKGST NVGISGSSST DSLSEKFFSE QYSRMYNRYS SILKNLGCIC 

       310        320        330        340        350        360 
NYLRTLGKES CCLPKVRFCS GEGASKKTKY SYRNSSGCLT KKKTHGDKER LSNDNGHADF 

       370        380        390        400        410        420 
VCSKSCCTKM KDCAVTSTIS GHSSSEISRI VSMEPIENHL NLEAGSTGTE HIVLSVSGMS 

       430        440        450        460        470        480 
CTGCESKLKK SFGALKCVHG LKTSLILSQA EFNLDLAQGS VKDVIKHLSK TTEFKYEQIS 

       490        500        510        520        530        540 
NHGSTIDVVV PYAAKDFINE EWPQGVTELK IVERNIIRIY FDPKVIGARD LVNEGWSVPV 

       550        560        570        580        590        600 
SIAPFSCHPT IEVGRKHLVR VGCTTALSII LTIPILVMAW APQLREKIST ISASMVLATI 

       610        620        630        640        650        660 
IQFVIAGPFY LNALKSLIFS RLIEMDLLIV LSTSAAYIFS IVSFGYFVVG RPLSTEQFFE 

       670        680        690        700        710        720 
TSSLLVTLIM VGRFVSELAR HRAVKSISVR SLQASSAILV DKTGKETEIN IRLLQYGDIF 

       730        740        750        760        770        780 
KVLPDSRIPT DGTVISGSSE VDEALITGES MPVPKKCQSI VVAGSVNGTG TLFVKLSKLP 

       790        800        810        820        830        840 
GNNTISTIAT MVDEAKLTKP KIQNIADKIA SYFVPTIIGI TVVTFCVWIA VGIRVEKQSR 

       850        860        870        880        890        900 
SDAVIQAIIY AITVLIVSCP CVIGLAVPIV FVIASGVAAK RGVIFKSAES IEVAHNTSHV 

       910        920        930        940        950        960 
VFDKTGTLTE GKLTVVHETV RGDRHNSQSL LLGLTEGIKH PVSMAIASYL KEKGVSAQNV 

       970        980        990       1000       1010       1020 
SNTKAVTGKR VEGTSYSGLK LQGGNCRWLG HNNDPDVRKA LEQGYSVFCF SVNGSVTAVY 

      1030       1040       1050       1060       1070       1080 
ALEDSLRADA VSTINLLRQR GISLHILSGD DDGAVRSMAA RLGIESSNIR SHATPAEKSE 

      1090       1100       1110       1120       1130       1140 
YIKDIVEGRN CDSSSQSKRP VVVFCGDGTN DAIGLTQATI GVHINEGSEV AKLAADVVML 

      1150       1160       1170       1180       1190       1200 
KPKLNNILTM ITVSQKAMFR VKLNFLWSFT YNLFAILLAA GAFVDFHIPP EYAGLGELVS 

      1210 
ILPVIFVAIL LRYAKI 

« Hide

References

« Hide 'large scale' references
[1]"A putative P-type Cu(2+)-transporting ATPase gene on chromosome II of Saccharomyces cerevisiae."
Rad M.R., Kirchrath L., Hollenberg C.
Yeast 10:1217-1225(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: ATCC 204508 / S288c.
[2]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [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, SEQUENCE REVISION TO 382.
Strain: ATCC 204508 / S288c.
[4]"Resistance to cadmium is under control of the CAD2 gene in the yeast Saccharomyces cerevisiae."
Tohoyama H., Inouhe M., Joho M., Murayama T.
Curr. Genet. 18:181-185(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"The cadmium-resistant gene, CAD2, which is a mutated putative copper-transporter gene (PCA1), controls the intracellular cadmium-level in the yeast S. cerevisiae."
Shiraishi E., Inouhe M., Joho M., Tohoyama H.
Curr. Genet. 37:79-86(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-970.
[6]"Exploratory and confirmatory gene expression profiling of mac1Delta."
De Freitas J.M., Kim J.H., Poynton H., Su T., Wintz H., Fox T., Holman P., Loguinov A., Keles S., van der Laan M., Vulpe C.
J. Biol. Chem. 279:4450-4458(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"A cadmium-transporting P1B-type ATPase in yeast Saccharomyces cerevisiae."
Adle D.J., Sinani D., Kim H., Lee J.
J. Biol. Chem. 282:947-955(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-970.
[8]"Expressional control of a cadmium-transporting P1B-type ATPase by a metal sensing degradation signal."
Adle D.J., Lee J.
J. Biol. Chem. 283:31460-31468(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MOTIF, UBIQUITINATION, MUTAGENESIS OF CYS-298; CYS-300; CYS-311 AND CYS-312.
[9]"A tradeoff drives the evolution of reduced metal resistance in natural populations of yeast."
Chang S.L., Leu J.Y.
PLoS Genet. 7:E1002034-E1002034(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z29332 Genomic DNA. Translation: CAA82529.1.
Z36164 Genomic DNA. Translation: CAA85260.1.
BK006936 Genomic DNA. Translation: DAA07409.2.
PIRS46177.
RefSeqNP_009854.2. NM_001178643.2.

3D structure databases

ProteinModelPortalP38360.
SMRP38360. Positions 556-1216.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32988. 23 interactions.
DIPDIP-6641N.
IntActP38360. 1 interaction.
MINTMINT-620940.

Protein family/group databases

TCDB3.A.3.5.14. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbP38360.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR295W; YBR295W; YBR295W.
GeneID852598.
KEGGsce:YBR295W.

Organism-specific databases

CYGDYBR295w.
SGDS000000499. PCA1.

Phylogenomic databases

eggNOGCOG2217.
GeneTreeENSGT00530000063773.
HOGENOMHOG000160566.
KOK01533.
OMACTGCENK.
OrthoDBEOG73JM3V.

Enzyme and pathway databases

BioCycYEAST:G3O-29213-MONOMER.

Gene expression databases

GenevestigatorP38360.

Family and domain databases

Gene3D2.70.150.10. 1 hit.
3.40.50.1000. 2 hits.
InterProIPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR027256. Cation_transp_P-typ_ATPase_IB.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF55008. SSF55008. 1 hit.
SSF56784. SSF56784. 2 hits.
TIGRFAMsTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971772.

Entry information

Entry nameATU1_YEAST
AccessionPrimary (citable) accession number: P38360
Secondary accession number(s): D6VQT9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: June 11, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

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

Yeast

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

SIMILARITY comments

Index of protein domains and families