MAC1_YEAST
ID MAC1_YEAST Reviewed; 417 AA.
AC P35192; D6VZJ5; E9P8Z5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Metal-binding activator 1;
GN Name=MAC1; Synonyms=CUA1; OrderedLocusNames=YMR021C; ORFNames=YM9711.11C;
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], AND MUTAGENESIS.
RX PubMed=8262047; DOI=10.1002/j.1460-2075.1993.tb06198.x;
RA Jungmann J., Reins H.-A., Lee J., Romeo A., Hassett R., Kosman D.,
RA Jentsch S.;
RT "MAC1, a nuclear regulatory protein related to Cu-dependent transcription
RT factors is involved in Cu/Fe utilization and stress resistance in yeast.";
RL EMBO J. 12:5051-5056(1993).
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 FUNCTION.
RX PubMed=12011036; DOI=10.1074/jbc.c200203200;
RA Yonkovich J., McKenndry R., Shi X., Zhu Z.;
RT "Copper ion-sensing transcription factor Mac1p post-translationally
RT controls the degradation of its target gene product Ctr1p.";
RL J. Biol. Chem. 277:23981-23984(2002).
RN [6]
RP PHOSPHORYLATION.
RX PubMed=11134042; DOI=10.1074/jbc.m008179200;
RA Heredia J., Crooks M., Zhu Z.;
RT "Phosphorylation and Cu+ coordination-dependent DNA binding of the
RT transcription factor Mac1p in the regulation of copper transport.";
RL J. Biol. Chem. 276:8793-8797(2001).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Regulatory protein involved in Cu/Fe utilization and stress
CC resistance. Involved in basal level transcription of FRE1 and H(2)O(2)-
CC induced transcription of CTT1. Regulates the transcription of CTR1 and
CC CTR3 via the copper ion responsive elements in their promoters.
CC Required for degradation of CTR1. {ECO:0000269|PubMed:12011036}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 14800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X74551; CAA52645.1; -; Genomic_DNA.
DR EMBL; Z49211; CAA89124.1; -; Genomic_DNA.
DR EMBL; AY692934; AAT92953.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09919.1; -; Genomic_DNA.
DR PIR; S54023; S54023.
DR RefSeq; NP_013734.1; NM_001182517.1.
DR AlphaFoldDB; P35192; -.
DR SMR; P35192; -.
DR BioGRID; 35192; 284.
DR DIP; DIP-4851N; -.
DR IntAct; P35192; 6.
DR STRING; 4932.YMR021C; -.
DR iPTMnet; P35192; -.
DR MaxQB; P35192; -.
DR PaxDb; P35192; -.
DR PRIDE; P35192; -.
DR EnsemblFungi; YMR021C_mRNA; YMR021C; YMR021C.
DR GeneID; 855035; -.
DR KEGG; sce:YMR021C; -.
DR SGD; S000004623; MAC1.
DR VEuPathDB; FungiDB:YMR021C; -.
DR eggNOG; ENOG502QQ0T; Eukaryota.
DR HOGENOM; CLU_034774_0_0_1; -.
DR InParanoid; P35192; -.
DR OMA; CLIHRKE; -.
DR BioCyc; YEAST:G3O-32726-MON; -.
DR PRO; PR:P35192; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P35192; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IMP:SGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR Gene3D; 3.90.430.10; -; 1.
DR InterPro; IPR001083; Cu_fist_DNA-bd_dom.
DR InterPro; IPR036395; Cu_fist_DNA-bd_dom_sf.
DR Pfam; PF00649; Copper-fist; 1.
DR PRINTS; PR00617; COPPERFIST.
DR SMART; SM01090; Copper-fist; 1.
DR SMART; SM00412; Cu_FIST; 1.
DR SUPFAM; SSF57879; SSF57879; 1.
DR PROSITE; PS01119; COPPER_FIST_1; 1.
DR PROSITE; PS50073; COPPER_FIST_2; 1.
PE 1: Evidence at protein level;
KW Activator; Copper; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..417
FT /note="Metal-binding activator 1"
FT /id="PRO_0000194928"
FT REPEAT 264..279
FT /note="1"
FT REPEAT 322..337
FT /note="2"
FT DNA_BIND 1..40
FT /note="Copper-fist"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT REGION 128..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..337
FT /note="2 X 16 AA repeat of C-X-C-X(4)-C-X-C-X-X-C-X-X-H"
FT COMPBIAS 150..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 279
FT /note="H->Q: Gain of function."
FT /evidence="ECO:0000269|PubMed:8262047"
FT CONFLICT 198
FT /note="P -> A (in Ref. 1; CAA52645)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="K -> R (in Ref. 4; AAT92953)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 46516 MW; 2D665168F04BEC5D CRC64;
MIIFNGNKYA CASCIRGHRS STCRHSHRML IKVRTRGRPS PMAIRDAILV DSTSQSTEYE
NGAQIEGDCC SAMNQQPILF VRASAVRKAR MINGKLHILM EEGFTAHEPK DISTFTDDGN
KYITETEFLR KHSPKAPATG TISPDSTKSS SSSEKKERSR LQQEPIRHFS NCCKKDKSQN
PASNGKTNKA PSDDIFTPYG SLESTSAFND ILQENYNSSV PGAHDSSETL TPQSTTTIAA
PHSSDVASKV EVLTHKGIFL STQCSCEDES CPCVNCLIHR SEEELNSYIQ QSGVPLTNIG
EAQITDKMMD YLDDCKCTDK ECICPPDNCT CDGCFSHSTN IIPFEKFFFY GILNARLTRK
TQIKFKGKLV PSKYWWDFLK LQVPLMTDAQ LELLDIHAWF QKLVSNYAPH LSDATTS
