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P38360

- ATU1_YEAST

UniProt

P38360 - ATU1_YEAST

Protein

P-type cation-transporting ATPase

Gene

PCA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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.7 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi421 – 4211CopperPROSITE-ProRule annotation
    Metal bindingi424 – 4241CopperPROSITE-ProRule annotation
    Active sitei903 – 90314-aspartylphosphate intermediateBy similarity
    Metal bindingi1107 – 11071MagnesiumPROSITE-ProRule annotation
    Metal bindingi1111 – 11111MagnesiumPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism Source: SGD
    2. ATP binding Source: UniProtKB-KW
    3. cadmium-exporting ATPase activity Source: SGD
    4. copper ion binding Source: SGD

    GO - Biological processi

    1. cadmium ion transmembrane transport Source: GOC
    2. cadmium ion transport Source: SGD
    3. cellular iron ion homeostasis Source: SGD
    4. cellular metal ion homeostasis Source: SGD
    5. ion transmembrane transport Source: GOC
    6. response to cadmium ion Source: UniProtKB-KW
    7. transmembrane transport Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cadmium resistance, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Cadmium, Copper, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29213-MONOMER.

    Protein family/group databases

    TCDBi3.A.3.5.14. the p-type atpase (p-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:PCA1
    Synonyms:CAD2, PAY2
    Ordered Locus Names:YBR295W
    ORF Names:YBR2112
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR295w.
    SGDiS000000499. PCA1.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: SGD

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi298 – 2981C → A: Abolishes copper resistance but not cadmium resistance; when associated with A-300. 1 Publication
    Mutagenesisi300 – 3001C → A: Abolishes copper resistance but not cadmium resistance; when associated with A-298. 1 Publication
    Mutagenesisi311 – 3111C → A: Abolishes cadmium resistance yet retains the ability to confer copper resistance; when associated with A-312. 1 Publication
    Mutagenesisi312 – 3121C → A: Abolishes cadmium resistance yet retains the ability to confer copper resistance; when associated with A-311. 1 Publication
    Mutagenesisi970 – 9701R → G: Confers localization to the plasma membrane and cadmium transport function. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12161216P-type cation-transporting ATPasePRO_0000046317Add
    BLAST

    Post-translational modificationi

    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.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiP38360.

    Expressioni

    Gene expression databases

    GenevestigatoriP38360.

    Interactioni

    Protein-protein interaction databases

    BioGridi32988. 23 interactions.
    DIPiDIP-6641N.
    IntActiP38360. 1 interaction.
    MINTiMINT-620940.

    Structurei

    3D structure databases

    ProteinModelPortaliP38360.
    SMRiP38360. Positions 556-1216.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 556556CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini579 – 59214ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini613 – 6208CytoplasmicSequence Analysis
    Topological domaini642 – 65918ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini681 – 808128CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini832 – 84716ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini866 – 1161296CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1182 – 11909ExtracellularSequence Analysis
    Topological domaini1210 – 12167CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei557 – 57822HelicalSequence AnalysisAdd
    BLAST
    Transmembranei593 – 61220HelicalSequence AnalysisAdd
    BLAST
    Transmembranei621 – 64121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei660 – 68021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei809 – 83123HelicalSequence AnalysisAdd
    BLAST
    Transmembranei848 – 86518HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1162 – 118120HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1191 – 120919HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini411 – 47464HMAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni250 – 350101Metal-responding degradation signalAdd
    BLAST

    Sequence similaritiesi

    Contains 1 HMA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2217.
    GeneTreeiENSGT00530000063773.
    HOGENOMiHOG000160566.
    KOiK01533.
    OMAiCTGCENK.
    OrthoDBiEOG73JM3V.

    Family and domain databases

    Gene3Di2.70.150.10. 1 hit.
    3.40.50.1000. 2 hits.
    InterProiIPR018303. 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]
    PfamiPF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    SUPFAMiSSF55008. SSF55008. 1 hit.
    SSF56784. SSF56784. 2 hits.
    TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
    TIGR01494. ATPase_P-type. 1 hit.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    PS50846. HMA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38360-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPEKLFSGL GTSDGEYGVV NSENISIDAM QDNRGECHRR SIEMHANDNL     50
    GLVSQRDCTN RPKITPQECL SETEQICHHG ENRTKAGLDV DDAETGGDHT 100
    NESRVDECCA EKVNDTETGL DVDSCCGDAQ TGGDHTNESC VDGCCVRDSS 150
    VMVEEVTGSC EAVSSKEQLL TSFEVVPSKS EGLQSIHDIR ETTRCNTNSN 200
    QHTGKGRLCI ESSDSTLKKR SCKVSRQKIE VSSKPECCNI SCVERIASRS 250
    CEKRTFKGST NVGISGSSST DSLSEKFFSE QYSRMYNRYS SILKNLGCIC 300
    NYLRTLGKES CCLPKVRFCS GEGASKKTKY SYRNSSGCLT KKKTHGDKER 350
    LSNDNGHADF VCSKSCCTKM KDCAVTSTIS GHSSSEISRI VSMEPIENHL 400
    NLEAGSTGTE HIVLSVSGMS CTGCESKLKK SFGALKCVHG LKTSLILSQA 450
    EFNLDLAQGS VKDVIKHLSK TTEFKYEQIS NHGSTIDVVV PYAAKDFINE 500
    EWPQGVTELK IVERNIIRIY FDPKVIGARD LVNEGWSVPV SIAPFSCHPT 550
    IEVGRKHLVR VGCTTALSII LTIPILVMAW APQLREKIST ISASMVLATI 600
    IQFVIAGPFY LNALKSLIFS RLIEMDLLIV LSTSAAYIFS IVSFGYFVVG 650
    RPLSTEQFFE TSSLLVTLIM VGRFVSELAR HRAVKSISVR SLQASSAILV 700
    DKTGKETEIN IRLLQYGDIF KVLPDSRIPT DGTVISGSSE VDEALITGES 750
    MPVPKKCQSI VVAGSVNGTG TLFVKLSKLP GNNTISTIAT MVDEAKLTKP 800
    KIQNIADKIA SYFVPTIIGI TVVTFCVWIA VGIRVEKQSR SDAVIQAIIY 850
    AITVLIVSCP CVIGLAVPIV FVIASGVAAK RGVIFKSAES IEVAHNTSHV 900
    VFDKTGTLTE GKLTVVHETV RGDRHNSQSL LLGLTEGIKH PVSMAIASYL 950
    KEKGVSAQNV SNTKAVTGKR VEGTSYSGLK LQGGNCRWLG HNNDPDVRKA 1000
    LEQGYSVFCF SVNGSVTAVY ALEDSLRADA VSTINLLRQR GISLHILSGD 1050
    DDGAVRSMAA RLGIESSNIR SHATPAEKSE YIKDIVEGRN CDSSSQSKRP 1100
    VVVFCGDGTN DAIGLTQATI GVHINEGSEV AKLAADVVML KPKLNNILTM 1150
    ITVSQKAMFR VKLNFLWSFT YNLFAILLAA GAFVDFHIPP EYAGLGELVS 1200
    ILPVIFVAIL LRYAKI 1216
    Length:1,216
    Mass (Da):131,875
    Last modified:July 27, 2011 - v2
    Checksum:iE4DCAFB23AA1F138
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti382 – 3821H → T in CAA82529. (PubMed:7754711)Curated
    Sequence conflicti382 – 3821H → T in CAA85260. (PubMed:7813418)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29332 Genomic DNA. Translation: CAA82529.1.
    Z36164 Genomic DNA. Translation: CAA85260.1.
    BK006936 Genomic DNA. Translation: DAA07409.2.
    PIRiS46177.
    RefSeqiNP_009854.2. NM_001178643.2.

    Genome annotation databases

    EnsemblFungiiYBR295W; YBR295W; YBR295W.
    GeneIDi852598.
    KEGGisce:YBR295W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29332 Genomic DNA. Translation: CAA82529.1 .
    Z36164 Genomic DNA. Translation: CAA85260.1 .
    BK006936 Genomic DNA. Translation: DAA07409.2 .
    PIRi S46177.
    RefSeqi NP_009854.2. NM_001178643.2.

    3D structure databases

    ProteinModelPortali P38360.
    SMRi P38360. Positions 556-1216.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32988. 23 interactions.
    DIPi DIP-6641N.
    IntActi P38360. 1 interaction.
    MINTi MINT-620940.

    Protein family/group databases

    TCDBi 3.A.3.5.14. the p-type atpase (p-atpase) superfamily.

    Proteomic databases

    PaxDbi P38360.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR295W ; YBR295W ; YBR295W .
    GeneIDi 852598.
    KEGGi sce:YBR295W.

    Organism-specific databases

    CYGDi YBR295w.
    SGDi S000000499. PCA1.

    Phylogenomic databases

    eggNOGi COG2217.
    GeneTreei ENSGT00530000063773.
    HOGENOMi HOG000160566.
    KOi K01533.
    OMAi CTGCENK.
    OrthoDBi EOG73JM3V.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29213-MONOMER.

    Miscellaneous databases

    NextBioi 971772.

    Gene expression databases

    Genevestigatori P38360.

    Family and domain databases

    Gene3Di 2.70.150.10. 1 hit.
    3.40.50.1000. 2 hits.
    InterProi IPR018303. 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 ]
    Pfami PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    SUPFAMi SSF55008. SSF55008. 1 hit.
    SSF56784. SSF56784. 2 hits.
    TIGRFAMsi TIGR01525. ATPase-IB_hvy. 1 hit.
    TIGR01494. ATPase_P-type. 1 hit.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    PS50846. HMA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiATU1_YEAST
    AccessioniPrimary (citable) accession number: P38360
    Secondary accession number(s): D6VQT9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Caution

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3