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2.A.4.2.2 Vacuolar Zn²⁺, Cd²⁺ uptake (into vacuoles) permease (Zn²⁺/Cd²⁺:H⁺ antiporter). A single mutation (N44I) changes the specificity from Zn²⁺ to Fe²⁺ (Lin et al., 2008). Lin et al. (2009) have identified transmembrane residues that determine metal specificity.
Accession Number:	P20107
Protein Name:	ZRC1 aka ZnrP aka YMR243C aka YM9408.05C
Length:	442
Molecular Weight:	48345.00
Species:	Saccharomyces cerevisiae (Baker's yeast) [4932]
Number of TMSs:	7
Location¹ / Topology² / Orientation³:	Mitochondrion membrane¹ / Multi-pass membrane protein²
Substrate	cadmium(2+), zinc(2+), hydron

DIP:	DIP-2030N
RefSeq:	NP_013970.1
Entrez Gene ID:	855284
Pfam:	PF01545
KEGG:	sce:YMR243C
Gene Ontology GO:0000324 C:fungal-type vacuole GO:0016021 C:integral to membrane GO:0031966 C:mitochondrial membrane GO:0005385 F:zinc ion transmembrane transporter activity GO:0006882 P:cellular zinc ion homeostasis GO:0006824 P:cobalt ion transport GO:0006749 P:glutathione metabolic process GO:0046686 P:response to cadmium ion GO:0055085 P:transmembrane transport GO:0006829 P:zinc ion transport
References (7) [1] “Identification of a gene conferring resistance to zinc and cadmium ions in the yeast Saccharomyces cerevisiae.” Kamizono A.et.al. 2693940 [2] “The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.” Bowman S.et.al. 9169872 [3] “Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.” Hu Y.et.al. 17322287 [4] “Global analysis of protein expression in yeast.” Ghaemmaghami S.et.al. 14562106 [5] “A global topology map of the Saccharomyces cerevisiae membrane proteome.” Kim H.et.al. 16847258 [6] “Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.” Li X.et.al. 17330950 [7] “Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.” Smolka M.B.et.al. 17563356

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FASTA formatted sequence

1:	MITGKELRII SLLTLDTVFF LLEITIGYMS HSLALIADSF HMLNDIISLL VALWAVDVAK 
61:	NRGPDAKYTY GWKRAEILGA LINAVFLIAL CFSIMIEALQ RLIEPQEIQN PRLVLYVGVA 
121:	GLISNVVGLF LFHDHGSDSL HSHSHGSVES GNNDLDIESN ATHSHSHASL PNDNLAIDED 
181:	AISSPGPSGQ IGEVLPQSVV NRLSNESQPL LNHDDHDHSH ESKKPGHRSL NMHGVFLHVL 
241:	GDALGNIGVI AAALFIWKTE YSWRYYSDPI VSLIITIIIF SSALPLSRRA SRILLQATPS 
301:	TISADQIQRE ILAVPGVIAV HDFHVWNLTE SIYIASIHVQ IDCAPDKFMS SAKLIRKIFH 
361:	QHGIHSATVQ PEFVSGDVNE DIRRRFSIIA GGSPSSSQEA FDSHGNTEHG RKKRSPTAYG 
421:	ATTASSNCIV DDAVNCNTSN CL

2.A.4.2.2
Vacuolar Zn²⁺, Cd²⁺ uptake (into vacuoles) permease (Zn²⁺/Cd²⁺:H⁺ antiporter). A single mutation (N44I) changes the specificity from Zn²⁺ to Fe²⁺ (Lin et al., 2008). Lin et al. (2009) have identified transmembrane residues that determine metal specificity.

Cross database links:

Gene Ontology

References (7)

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2.A.4.2.2Vacuolar Zn2+, Cd2+ uptake (into vacuoles) permease (Zn2+/Cd2+:H+ antiporter). A single mutation (N44I) changes the specificity from Zn2+ to Fe2+ (Lin et al., 2008). Lin et al. (2009) have identified transmembrane residues that determine metal specificity.

Cross database links:

Gene Ontology

References (7)

External Searches:

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2.A.4.2.2
Vacuolar Zn²⁺, Cd²⁺ uptake (into vacuoles) permease (Zn²⁺/Cd²⁺:H⁺ antiporter). A single mutation (N44I) changes the specificity from Zn²⁺ to Fe²⁺ (Lin et al., 2008). Lin et al. (2009) have identified transmembrane residues that determine metal specificity.