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P38360

- ATU1_YEAST

UniProt

P38360 - ATU1_YEAST

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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

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
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 1 Publication; Multi-pass membrane protein 1 Publication

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 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 408-480, 567-1212.
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.
InParanoidiP38360.
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

        10         20         30         40         50
MKPEKLFSGL GTSDGEYGVV NSENISIDAM QDNRGECHRR SIEMHANDNL
60 70 80 90 100
GLVSQRDCTN RPKITPQECL SETEQICHHG ENRTKAGLDV DDAETGGDHT
110 120 130 140 150
NESRVDECCA EKVNDTETGL DVDSCCGDAQ TGGDHTNESC VDGCCVRDSS
160 170 180 190 200
VMVEEVTGSC EAVSSKEQLL TSFEVVPSKS EGLQSIHDIR ETTRCNTNSN
210 220 230 240 250
QHTGKGRLCI ESSDSTLKKR SCKVSRQKIE VSSKPECCNI SCVERIASRS
260 270 280 290 300
CEKRTFKGST NVGISGSSST DSLSEKFFSE QYSRMYNRYS SILKNLGCIC
310 320 330 340 350
NYLRTLGKES CCLPKVRFCS GEGASKKTKY SYRNSSGCLT KKKTHGDKER
360 370 380 390 400
LSNDNGHADF VCSKSCCTKM KDCAVTSTIS GHSSSEISRI VSMEPIENHL
410 420 430 440 450
NLEAGSTGTE HIVLSVSGMS CTGCESKLKK SFGALKCVHG LKTSLILSQA
460 470 480 490 500
EFNLDLAQGS VKDVIKHLSK TTEFKYEQIS NHGSTIDVVV PYAAKDFINE
510 520 530 540 550
EWPQGVTELK IVERNIIRIY FDPKVIGARD LVNEGWSVPV SIAPFSCHPT
560 570 580 590 600
IEVGRKHLVR VGCTTALSII LTIPILVMAW APQLREKIST ISASMVLATI
610 620 630 640 650
IQFVIAGPFY LNALKSLIFS RLIEMDLLIV LSTSAAYIFS IVSFGYFVVG
660 670 680 690 700
RPLSTEQFFE TSSLLVTLIM VGRFVSELAR HRAVKSISVR SLQASSAILV
710 720 730 740 750
DKTGKETEIN IRLLQYGDIF KVLPDSRIPT DGTVISGSSE VDEALITGES
760 770 780 790 800
MPVPKKCQSI VVAGSVNGTG TLFVKLSKLP GNNTISTIAT MVDEAKLTKP
810 820 830 840 850
KIQNIADKIA SYFVPTIIGI TVVTFCVWIA VGIRVEKQSR SDAVIQAIIY
860 870 880 890 900
AITVLIVSCP CVIGLAVPIV FVIASGVAAK RGVIFKSAES IEVAHNTSHV
910 920 930 940 950
VFDKTGTLTE GKLTVVHETV RGDRHNSQSL LLGLTEGIKH PVSMAIASYL
960 970 980 990 1000
KEKGVSAQNV SNTKAVTGKR VEGTSYSGLK LQGGNCRWLG HNNDPDVRKA
1010 1020 1030 1040 1050
LEQGYSVFCF SVNGSVTAVY ALEDSLRADA VSTINLLRQR GISLHILSGD
1060 1070 1080 1090 1100
DDGAVRSMAA RLGIESSNIR SHATPAEKSE YIKDIVEGRN CDSSSQSKRP
1110 1120 1130 1140 1150
VVVFCGDGTN DAIGLTQATI GVHINEGSEV AKLAADVVML KPKLNNILTM
1160 1170 1180 1190 1200
ITVSQKAMFR VKLNFLWSFT YNLFAILLAA GAFVDFHIPP EYAGLGELVS
1210
ILPVIFVAIL LRYAKI
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 408-480, 567-1212.
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.
InParanoidi P38360.
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: October 29, 2014
This is version 136 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