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MAC1_CANAL
ID   MAC1_CANAL              Reviewed;         431 AA.
AC   Q5AFK0; A0A1D8PQK8; Q3MPS9;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Metal-binding activator 1;
GN   Name=MAC1; OrderedLocusNames=CAALFM_C700510WA; ORFNames=CaO19.7068;
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   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15256562; DOI=10.1099/mic.0.27004-0;
RA   Marvin M.E., Mason R.P., Cashmore A.M.;
RT   "The CaCTR1 gene is required for high-affinity iron uptake and is
RT   transcriptionally controlled by a copper-sensing transactivator encoded by
RT   CaMAC1.";
RL   Microbiology 150:2197-2208(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=16518547; DOI=10.1111/j.1745-7270.2006.00146.x;
RA   Huang G.H., Nie X.Y., Chen J.Y.;
RT   "CaMac1, a Candida albicans copper ion-sensing transcription factor,
RT   promotes filamentous and invasive growth in Saccharomyces cerevisiae.";
RL   Acta Biochim. Biophys. Sin. 38:213-217(2006).
RN   [6]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=19367594; DOI=10.1002/jbio.200910004;
RA   Hauser N.C., Dukalska M., Fellenberg K., Rupp S.;
RT   "From experimental setup to data analysis in transcriptomics: copper
RT   metabolism in the human pathogen Candida albicans.";
RL   J. Biophotonics 2:262-268(2009).
RN   [7]
RP   INDUCTION.
RX   PubMed=20608978; DOI=10.1111/j.1574-695x.2010.00710.x;
RA   Peters B.M., Jabra-Rizk M.A., Scheper M.A., Leid J.G., Costerton J.W.,
RA   Shirtliff M.E.;
RT   "Microbial interactions and differential protein expression in
RT   Staphylococcus aureus -Candida albicans dual-species biofilms.";
RL   FEMS Immunol. Med. Microbiol. 59:493-503(2010).
CC   -!- FUNCTION: Copper ion-sensing transcription factor which activates
CC       transcription of the CTR1 copper transporter under low-copper
CC       conditions. Promotes filamentous and invasive growth.
CC       {ECO:0000269|PubMed:15256562, ECO:0000269|PubMed:16518547,
CC       ECO:0000269|PubMed:19367594}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- INDUCTION: Expression is inhibited in the presence of copper.
CC       Expression is increased in polymicrobial biofilms during coinfection
CC       with S.aureus. {ECO:0000269|PubMed:19367594,
CC       ECO:0000269|PubMed:20608978}.
CC   -!- DISRUPTION PHENOTYPE: Results in reduced growth on copper or iron
CC       depleted media and the inability to grow on media with a non-
CC       fermentable carbon source. {ECO:0000269|PubMed:15256562}.
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DR   EMBL; CP017629; AOW30430.1; -; Genomic_DNA.
DR   RefSeq; XP_720360.1; XM_715267.1.
DR   AlphaFoldDB; Q5AFK0; -.
DR   PRIDE; Q5AFK0; -.
DR   GeneID; 3637985; -.
DR   KEGG; cal:CAALFM_C700510WA; -.
DR   CGD; CAL0000188166; MAC1.
DR   VEuPathDB; FungiDB:C7_00510W_A; -.
DR   eggNOG; ENOG502QQ0T; Eukaryota.
DR   HOGENOM; CLU_031396_0_0_1; -.
DR   InParanoid; Q5AFK0; -.
DR   OMA; CTNCETH; -.
DR   OrthoDB; 1312294at2759; -.
DR   Proteomes; UP000000559; Chromosome 7.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:CGD.
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:CGD.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR   GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:CGD.
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; PS50073; COPPER_FIST_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; Copper; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..431
FT                   /note="Metal-binding activator 1"
FT                   /id="PRO_0000422811"
FT   DNA_BIND        1..40
FT                   /note="Copper-fist"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
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"
SQ   SEQUENCE   431 AA;  47737 MW;  C12244998DED6E8F CRC64;
     MILIDDIKYA CMECVRGHRS SSCKHHERPL LQVRSKGRPG VYANGNPNHR VAIFAEEIAK
     SDKPSTNGTK RCKSEPIIVL KASSKQVIDC SSGVIIGPYD ETKTKPSTVE KRTPSPPIIS
     DESFINTSAC CTPKISKGKS CGCCNNKRKA VNKSKILQNY IKNKLNQKIN NNETLVFMNK
     SHTTNNEQKE DHQLYGMVPV PSCSIPGTCC CDDACSCQGC VVHGNSKYQI PLPTSKQQVT
     DTTNPFENEE KFIFNSMPQT DKSDLFFNTI STSSNVPPAD SSSECSCPPN ACDCTNCETH
     GILNGFRLDD YFKDQSKLMN VLDFNFSELL GTIPEQPIPT EFMQPPSENT LLTSLSSENS
     FIPNQTKELS TQPPILPLDA QNVCNELDQL EPLVPSLQPC DKKATKWVNN RDTLEDVSDN
     RVKSCCSKKT K
 
 
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