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P38360

- ATU1_YEAST

UniProt

P38360 - ATU1_YEAST

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Protein
P-type cation-transporting ATPase
Gene
PCA1, CAD2, PAY2, YBR295W, YBR2112
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 4211Copper Reviewed prediction
Metal bindingi424 – 4241Copper Reviewed prediction
Active sitei903 – 90314-aspartylphosphate intermediate By similarity
Metal bindingi1107 – 11071Magnesium By similarity
Metal bindingi1111 – 11111Magnesium By similarity

GO - Molecular functioni

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

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
Complete GO annotation...

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; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 556556Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei557 – 57822Helical; Reviewed prediction
Add
BLAST
Topological domaini579 – 59214Extracellular Reviewed prediction
Add
BLAST
Transmembranei593 – 61220Helical; Reviewed prediction
Add
BLAST
Topological domaini613 – 6208Cytoplasmic Reviewed prediction
Transmembranei621 – 64121Helical; Reviewed prediction
Add
BLAST
Topological domaini642 – 65918Extracellular Reviewed prediction
Add
BLAST
Transmembranei660 – 68021Helical; Reviewed prediction
Add
BLAST
Topological domaini681 – 808128Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei809 – 83123Helical; Reviewed prediction
Add
BLAST
Topological domaini832 – 84716Extracellular Reviewed prediction
Add
BLAST
Transmembranei848 – 86518Helical; Reviewed prediction
Add
BLAST
Topological domaini866 – 1161296Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei1162 – 118120Helical; Reviewed prediction
Add
BLAST
Topological domaini1182 – 11909Extracellular Reviewed prediction
Transmembranei1191 – 120919Helical; Reviewed prediction
Add
BLAST
Topological domaini1210 – 12167Cytoplasmic Reviewed prediction

GO - Cellular componenti

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

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 ATPase
PRO_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.

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini411 – 47464HMA
Add
BLAST

Region

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

Sequence similaritiesi

Contains 1 HMA domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti382 – 3821H → T in CAA82529. 1 Publication
Sequence conflicti382 – 3821H → T in CAA85260. 1 Publication

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...

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 134 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 (1 Publication), 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.

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

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