MRR2_CANAL
ID MRR2_CANAL Reviewed; 710 AA.
AC Q59MJ1; A0A1D8PKW3;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=multidrug resistance regulator 2 {ECO:0000303|PubMed:23844834};
GN Name=MRR2 {ECO:0000303|PubMed:23844834};
GN Synonyms=ZCF34 {ECO:0000303|PubMed:22073120};
GN OrderedLocusNames=CAALFM_C307860CA; ORFNames=CaO19.6182;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP IDENTIFICATION.
RX PubMed=18629206; DOI=10.1002/cfg.492;
RA Maicas S., Moreno I., Nieto A., Gomez M., Sentandreu R., Valentin E.;
RT "In silico analysis for transcription factors with Zn(II)(2)C(6) binuclear
RT cluster DNA-binding domains in Candida albicans.";
RL Comp. Funct. Genomics 6:345-356(2005).
RN [5]
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22073120; DOI=10.1371/journal.pone.0026962;
RA Vandeputte P., Ischer F., Sanglard D., Coste A.T.;
RT "In vivo systematic analysis of Candida albicans Zn2-Cys6 transcription
RT factors mutants for mice organ colonization.";
RL PLoS ONE 6:E26962-E26962(2011).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22359502; DOI=10.1371/journal.ppat.1002525;
RA Finkel J.S., Xu W., Huang D., Hill E.M., Desai J.V., Woolford C.A.,
RA Nett J.E., Taff H., Norice C.T., Andes D.R., Lanni F., Mitchell A.P.;
RT "Portrait of Candida albicans adherence regulators.";
RL PLoS Pathog. 8:E1002525-E1002525(2012).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23844834; DOI=10.1111/mmi.12327;
RA Schillig R., Morschhauser J.;
RT "Analysis of a fungus-specific transcription factor family, the Candida
RT albicans zinc cluster proteins, by artificial activation.";
RL Mol. Microbiol. 89:1003-1017(2013).
CC -!- FUNCTION: Transcription factor that controls the expression of CDR1,
CC the major multidrug efflux pump. Required for yeast cell adherence to
CC silicone substrate and plays a role in virulence.
CC {ECO:0000269|PubMed:22073120, ECO:0000269|PubMed:22359502,
CC ECO:0000269|PubMed:23844834}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Leads to increased drug susceptibility. Displays
CC decreased colonization of mouse kidneys. Shows decreased yeast cell
CC adherence to silicone substrate. {ECO:0000269|PubMed:22073120,
CC ECO:0000269|PubMed:22359502, ECO:0000269|PubMed:23844834}.
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DR EMBL; CP017625; AOW28784.1; -; Genomic_DNA.
DR RefSeq; XP_710938.1; XM_705846.1.
DR AlphaFoldDB; Q59MJ1; -.
DR EnsemblFungi; KHC79319; KHC79319; W5Q_03293.
DR EnsemblFungi; KHC87083; KHC87083; I503_03294.
DR GeneID; 3647468; -.
DR KEGG; cal:CAALFM_C307860CA; -.
DR CGD; CAL0000180700; MRR2.
DR VEuPathDB; FungiDB:C3_07860C_A; -.
DR HOGENOM; CLU_334333_0_0_1; -.
DR InParanoid; Q59MJ1; -.
DR OMA; IMSGVEN; -.
DR OrthoDB; 1003612at2759; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:CGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:CGD.
DR GO; GO:1900189; P:positive regulation of cell adhesion involved in single-species biofilm formation; IMP:CGD.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:CGD.
DR GO; GO:2001040; P:positive regulation of cellular response to drug; IMP:CGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:CGD.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Membrane; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..710
FT /note="multidrug resistance regulator 2"
FT /id="PRO_0000431800"
FT TRANSMEM 475..495
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT DNA_BIND 11..37
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
SQ SEQUENCE 710 AA; 82103 MW; E449624B2C350E3A CRC64;
MTKRDRTIYS CDACRSRKIK CNRQTPCASC HKSKRDCVYT VSRQRDAQIT NRKLDKKTYH
QISAIEKKIS ALEGKKGLLQ VETINFNKSF TDQTPLVELQ SLFPYLLLSK QDPGCVLVRH
HCHHLLEKDP RYFEYSQLLA DLSLTKRHHL TARAKALLGE AYIPSPQEGH TIDQLKHVLS
LNPNFRFAGN FADPLTSFFS LIPPAWANKQ LVDTFFQHIY PVIPIIDETD FNTSINRVLG
PQIDGHYINS FPSIGSADDL PFLALFLLVL RISYMYTPGA CPVSYDTLRA AETIMKEFDI
TKTHSLTALQ AEIMLRFYKI VAPESYTQSN YVQVSVGVLI QNCYSLALHR DPEYIGEHNP
KQQHLRRKIW HLLLRMEVID SAIFQTILSS NPDASDTKLP QLIDQAPPME QSIVKHIWRS
TDLFVSLRKL VEINSKTSED TPLETVLELL VEVETKLQAF LATIDSEAST VFYNDLVIFS
VNFLLVYMYY SLYLFKGPTP LGNKYLLKSA QILFVDLART RSTSLFLAYF NLNYIHLVLM
ITNFLRMRVD CIIHRHLRAQ DSSVQDLQCC RYFLKIIFFS HVKELGNYSS SHKYAWQMRK
VYLTLAKIME RSSDVLISND PELVKSAAVD IPVKEINKLL EQYINFKGFT PTTLFDPTDN
ELIDEMQHEN LWNAMENIEY SEKVYSGWID AIKNVPSNWD WDYWDFLKIS
