P-type cation-transporting ATPase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38360 (ATU1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 112. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	PCA1
Synonyms:	CAD2, PAY2
Ordered Locus Names:	YBR295W
ORF Names:	YBR2112

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1216 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Cadmium resistance Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Cadmium Copper Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro cellular iron ion homeostasis Inferred from expression pattern Ref.6. Source: SGD response to cadmium ion Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.7. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cadmium-exporting ATPase activity Inferred from mutant phenotype Ref.5 Ref.7. Source: SGD copper ion binding Inferred from mutant phenotype Ref.7. Source: SGD copper-exporting ATPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1216

1216

P-type cation-transporting ATPase

PRO_0000046317

Regions

Topological domain

1 – 556

556

Cytoplasmic Potential

Transmembrane

557 – 578

Helical; Potential

Topological domain

579 – 592

Extracellular Potential

Transmembrane

593 – 612

Helical; Potential

Topological domain

613 – 620

Cytoplasmic Potential

Transmembrane

621 – 641

Helical; Potential

Topological domain

642 – 659

Extracellular Potential

Transmembrane

660 – 680

Helical; Potential

Topological domain

681 – 808

128

Cytoplasmic Potential

Transmembrane

809 – 831

Helical; Potential

Topological domain

832 – 847

Extracellular Potential

Transmembrane

848 – 865

Helical; Potential

Topological domain

866 – 1161

296

Cytoplasmic Potential

Transmembrane

1162 – 1181

Helical; Potential

Topological domain

1182 – 1190

Extracellular Potential

Transmembrane

1191 – 1209

Helical; Potential

Topological domain

1210 – 1216

Cytoplasmic Potential

Domain

411 – 474

HMA

Region

250 – 350

101

Metal-responding degradation signal

Sites

Active site

903

4-aspartylphosphate intermediate By similarity

Metal binding

421

Copper Potential

Metal binding

424

Copper Potential

Metal binding

1107

Magnesium By similarity

Metal binding

1111

Magnesium By similarity

Experimental info

Mutagenesis

298

C → A: Abolishes copper resistance but not cadmium resistance; when associated with A-300. Ref.8

Mutagenesis

300

C → A: Abolishes copper resistance but not cadmium resistance; when associated with A-298. Ref.8

Mutagenesis

311

C → A: Abolishes cadmium resistance yet retains the ability to confer copper resistance; when associated with A-312. Ref.8

Mutagenesis

312

C → A: Abolishes cadmium resistance yet retains the ability to confer copper resistance; when associated with A-311. Ref.8

Mutagenesis

970

R → G: Confers localization to the plasma membrane and cadmium transport function. Ref.5 Ref.7

Sequence conflict

382

H → T in CAA82529. Ref.1

Sequence conflict

382

H → T in CAA85260. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P38360 [UniParc].

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

FASTA

1,216

131,875

        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' referencesShow '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: 7754711] [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. Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases 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: 2249249] [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: 10743563] [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: 14534306] [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: 17107946] [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: 18753133] [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: 21483812] [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.
PIR	S46177.
RefSeq	NP_009854.2. NM_001178643.2.
3D structure databases
ProteinModelPortal	P38360.
SMR	P38360. Positions 11-46, 410-481, 556-1216.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6641N.
IntAct	P38360. 1 interaction.
MINT	MINT-620940.
STRING	P38360.
Protein family/group databases
TCDB	3.A.3.5.14. P-type ATPase (P-ATPase) superfamily.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	852598.
KEGG	sce:YBR295W.
NMPDR	fig\|4932.3.peg.570.
Organism-specific databases
CYGD	YBR295w.
SGD	S000000499. PCA1.
Phylogenomic databases
eggNOG	fuNOG07674.
HOGENOM	HBG204237.
OMA	AISCPCA.
OrthoDB	EOG4SJ8NW.
Gene expression databases
ArrayExpress	P38360.
Genevestigator	P38360.
GermOnline	YBR295W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR006403. ATPase_P-typ_cat/Cu-transptr. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR006416. ATPase_P-typ_heavy-metal. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. IPR006121. HeavyMe-assoc_HMA. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit. G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KO	K01533.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00943. CUATPASE.
SUPFAM	SSF56784. HAD-like_dom. 1 hit. SSF55008. HeavyMe_transpt. 1 hit.
TIGRFAMs	TIGR01511. ATPase-IB1_Cu. 1 hit. TIGR01525. ATPase-IB_hvy. 1 hit. TIGR01494. ATPase_P-type. 1 hit.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. PS01047. HMA_1. False negative. PS50846. HMA_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	971772.

Entry information

Entry name

ATU1_YEAST

Accession

Primary (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:	December 14, 2011
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome II

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents