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CTR1_CANAL
ID   CTR1_CANAL              Reviewed;         251 AA.
AC   Q59NP1; A0A1D8PPG9;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Copper transport protein CTR1;
GN   Name=CTR1; OrderedLocusNames=CAALFM_C600790CA;
GN   ORFNames=CaO19.11130, CaO19.3646;
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   INDUCTION.
RX   PubMed=11595734; DOI=10.1074/jbc.m104484200;
RA   Lane S., Birse C., Zhou S., Matson R., Liu H.;
RT   "DNA array studies demonstrate convergent regulation of virulence factors
RT   by Cph1, Cph2, and Efg1 in Candida albicans.";
RL   J. Biol. Chem. 276:48988-48996(2001).
RN   [5]
RP   INDUCTION.
RX   PubMed=12388749; DOI=10.1091/mbc.e02-05-0272;
RA   Nantel A., Dignard D., Bachewich C., Harcus D., Marcil A., Bouin A.P.,
RA   Sensen C.W., Hogues H., van het Hoog M., Gordon P., Rigby T., Benoit F.,
RA   Tessier D.C., Thomas D.Y., Whiteway M.;
RT   "Transcription profiling of Candida albicans cells undergoing the yeast-to-
RT   hyphal transition.";
RL   Mol. Biol. Cell 13:3452-3465(2002).
RN   [6]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12777486; DOI=10.1099/mic.0.26172-0;
RA   Marvin M.E., Williams P.H., Cashmore A.M.;
RT   "The Candida albicans CTR1 gene encodes a functional copper transporter.";
RL   Microbiology 149:1461-1474(2003).
RN   [7]
RP   INDUCTION.
RX   PubMed=15470236; DOI=10.1128/ec.3.5.1076-1087.2004;
RA   Lorenz M.C., Bender J.A., Fink G.R.;
RT   "Transcriptional response of Candida albicans upon internalization by
RT   macrophages.";
RL   Eukaryot. Cell 3:1076-1087(2004).
RN   [8]
RP   FUNCTION, AND INDUCTION.
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   [9]
RP   INDUCTION.
RX   PubMed=15554973; DOI=10.1111/j.1365-2958.2004.04350.x;
RA   Bensen E.S., Martin S.J., Li M., Berman J., Davis D.A.;
RT   "Transcriptional profiling in Candida albicans reveals new adaptive
RT   responses to extracellular pH and functions for Rim101p.";
RL   Mol. Microbiol. 54:1335-1351(2004).
RN   [10]
RP   INDUCTION.
RX   PubMed=16039996; DOI=10.1016/j.bbrc.2005.07.018;
RA   Singh V., Sinha I., Sadhale P.P.;
RT   "Global analysis of altered gene expression during morphogenesis of Candida
RT   albicans in vitro.";
RL   Biochem. Biophys. Res. Commun. 334:1149-1158(2005).
RN   [11]
RP   INDUCTION.
RX   PubMed=16400181; DOI=10.1128/ec.5.1.180-191.2006;
RA   Cheng G., Yeater K.M., Hoyer L.L.;
RT   "Cellular and molecular biology of Candida albicans estrogen response.";
RL   Eukaryot. Cell 5:180-191(2006).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=19824013; DOI=10.1002/pmic.200800988;
RA   Cabezon V., Llama-Palacios A., Nombela C., Monteoliva L., Gil C.;
RT   "Analysis of Candida albicans plasma membrane proteome.";
RL   Proteomics 9:4770-4786(2009).
RN   [13]
RP   INDUCTION.
RX   PubMed=21414038; DOI=10.1111/j.1365-2958.2011.07626.x;
RA   Bonhomme J., Chauvel M., Goyard S., Roux P., Rossignol T., d'Enfert C.;
RT   "Contribution of the glycolytic flux and hypoxia adaptation to efficient
RT   biofilm formation by Candida albicans.";
RL   Mol. Microbiol. 80:995-1013(2011).
RN   [14]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=23584994; DOI=10.1128/ec.00344-12;
RA   Schwartz J.A., Olarte K.T., Michalek J.L., Jandu G.S., Michel S.L.,
RA   Bruno V.M.;
RT   "Regulation of copper toxicity by Candida albicans GPA2.";
RL   Eukaryot. Cell 12:954-961(2013).
CC   -!- FUNCTION: Required for high affinity copper (probably reduced Cu I)
CC       transport into the cell. {ECO:0000269|PubMed:12777486,
CC       ECO:0000269|PubMed:15256562, ECO:0000269|PubMed:23584994}.
CC   -!- SUBUNIT: Oligomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19824013};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:19824013}.
CC   -!- INDUCTION: Expressed in limited copper conditions. Expression is
CC       positively controlled by MAC1 and TYE7. Induced during biofilm
CC       formation and contact with macrophages as well as by alkaline pH via
CC       RIM101. Expression is down-regulated by 17-beta-estradiol.
CC       {ECO:0000269|PubMed:11595734, ECO:0000269|PubMed:12388749,
CC       ECO:0000269|PubMed:12777486, ECO:0000269|PubMed:15256562,
CC       ECO:0000269|PubMed:15470236, ECO:0000269|PubMed:15554973,
CC       ECO:0000269|PubMed:16039996, ECO:0000269|PubMed:16400181,
CC       ECO:0000269|PubMed:21414038, ECO:0000269|PubMed:23584994}.
CC   -!- DISRUPTION PHENOTYPE: Impairs growth on solid low-copper and low-iron
CC       medium and displays altered morphology in response to copper-depleted
CC       conditions. {ECO:0000269|PubMed:12777486}.
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DR   EMBL; CP017628; AOW30025.1; -; Genomic_DNA.
DR   RefSeq; XP_711319.1; XM_706227.1.
DR   AlphaFoldDB; Q59NP1; -.
DR   STRING; 237561.Q59NP1; -.
DR   PRIDE; Q59NP1; -.
DR   GeneID; 3647077; -.
DR   KEGG; cal:CAALFM_C600790CA; -.
DR   CGD; CAL0000196962; CTR1.
DR   VEuPathDB; FungiDB:C6_00790C_A; -.
DR   HOGENOM; CLU_093528_0_0_1; -.
DR   InParanoid; Q59NP1; -.
DR   OMA; YLEEVVW; -.
DR   OrthoDB; 1335284at2759; -.
DR   PHI-base; PHI:6485; -.
DR   PRO; PR:Q59NP1; -.
DR   Proteomes; UP000000559; Chromosome 6.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR   GO; GO:0005375; F:copper ion transmembrane transporter activity; IGI:CGD.
DR   GO; GO:0006878; P:cellular copper ion homeostasis; IBA:GO_Central.
DR   GO; GO:0015677; P:copper ion import; IMP:CGD.
DR   GO; GO:0006825; P:copper ion transport; IGI:CGD.
DR   GO; GO:0034755; P:iron ion transmembrane transport; IMP:CGD.
DR   InterPro; IPR007274; Cop_transporter.
DR   PANTHER; PTHR12483; PTHR12483; 1.
DR   Pfam; PF04145; Ctr; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Copper; Copper transport; Ion transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..251
FT                   /note="Copper transport protein CTR1"
FT                   /id="PRO_0000422812"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          157..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   251 AA;  27859 MW;  07DEEC1675196F64 CRC64;
     MEFLKRHEGH MHMSDSATSM VTSATSAVMD MASATMSMTM SSSTSSSSGM AMEGMDHGSS
     HMAMNMWLTA SFKDYPVVFK DLRASTKAQA FGIFVLLFFV AFLARMLEFV RNYLEEIVWK
     NNNYAEVEQG ISQHSANLQS PPVKSCCDDN AKEVVSDESI DKQNSPQHEE TTKARGTGKS
     LSLASTISRD IIRLALCIIP DLFAYSLMLA AMTYTLTYFF AVVIGSGVGR FVAERLMEHY
     RIKRGPPRNC C
 
 
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