ZRC1_YEAST
ID ZRC1_YEAST Reviewed; 442 AA.
AC P20107; D6W070;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Zinc/cadmium resistance protein;
GN Name=ZRC1; OrderedLocusNames=YMR243C; ORFNames=YM9408.05C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DKD-5D-H;
RX PubMed=2693940; DOI=10.1007/bf00261172;
RA Kamizono A., Nishizawa M., Teranishi Y., Murata K., Kimura A.;
RT "Identification of a gene conferring resistance to zinc and cadmium ions in
RT the yeast Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 219:161-167(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-393 AND SER-397, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-393 AND SER-397, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-357, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Probably responsible for the uptake of zinc and cadmium ions.
CC -!- INTERACTION:
CC P20107; P53756: PDR18; NbExp=2; IntAct=EBI-29667, EBI-28581;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC protein.
CC -!- MISCELLANEOUS: Present with 8200 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
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DR EMBL; X17537; CAB56542.1; -; Genomic_DNA.
DR EMBL; Z48756; CAA88653.1; -; Genomic_DNA.
DR EMBL; AY693213; AAT93232.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10144.1; -; Genomic_DNA.
DR PIR; S56057; S56057.
DR RefSeq; NP_013970.1; NM_001182750.1.
DR AlphaFoldDB; P20107; -.
DR SMR; P20107; -.
DR BioGRID; 35422; 173.
DR DIP; DIP-2030N; -.
DR IntAct; P20107; 17.
DR MINT; P20107; -.
DR STRING; 4932.YMR243C; -.
DR TCDB; 2.A.4.2.2; the cation diffusion facilitator (cdf) family.
DR iPTMnet; P20107; -.
DR MaxQB; P20107; -.
DR PaxDb; P20107; -.
DR PRIDE; P20107; -.
DR EnsemblFungi; YMR243C_mRNA; YMR243C; YMR243C.
DR GeneID; 855284; -.
DR KEGG; sce:YMR243C; -.
DR SGD; S000004856; ZRC1.
DR VEuPathDB; FungiDB:YMR243C; -.
DR eggNOG; KOG1483; Eukaryota.
DR GeneTree; ENSGT00940000172026; -.
DR HOGENOM; CLU_013430_4_3_1; -.
DR InParanoid; P20107; -.
DR OMA; HADMGMN; -.
DR BioCyc; YEAST:G3O-32923-MON; -.
DR Reactome; R-SCE-425410; Metal ion SLC transporters.
DR Reactome; R-SCE-435368; Zinc efflux and compartmentalization by the SLC30 family.
DR PRO; PR:P20107; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P20107; protein.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IMP:SGD.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:SGD.
DR GO; GO:0046686; P:response to cadmium ion; IEA:UniProtKB-KW.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1510.10; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR036837; Cation_efflux_CTD_sf.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF160240; SSF160240; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW Cadmium; Cadmium resistance; Ion transport; Isopeptide bond; Membrane;
KW Mitochondrion; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Zinc; Zinc transport.
FT CHAIN 1..442
FT /note="Zinc/cadmium resistance protein"
FT /id="PRO_0000206103"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..41
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..112
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..269
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 141..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 414
FT /note="R -> S (in Ref. 1; CAB56542)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="T -> I (in Ref. 1; CAB56542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 48345 MW; CBE6AA9716C0CEBE CRC64;
MITGKELRII SLLTLDTVFF LLEITIGYMS HSLALIADSF HMLNDIISLL VALWAVDVAK
NRGPDAKYTY GWKRAEILGA LINAVFLIAL CFSIMIEALQ RLIEPQEIQN PRLVLYVGVA
GLISNVVGLF LFHDHGSDSL HSHSHGSVES GNNDLDIESN ATHSHSHASL PNDNLAIDED
AISSPGPSGQ IGEVLPQSVV NRLSNESQPL LNHDDHDHSH ESKKPGHRSL NMHGVFLHVL
GDALGNIGVI AAALFIWKTE YSWRYYSDPI VSLIITIIIF SSALPLSRRA SRILLQATPS
TISADQIQRE ILAVPGVIAV HDFHVWNLTE SIYIASIHVQ IDCAPDKFMS SAKLIRKIFH
QHGIHSATVQ PEFVSGDVNE DIRRRFSIIA GGSPSSSQEA FDSHGNTEHG RKKRSPTAYG
ATTASSNCIV DDAVNCNTSN CL
