CAN2_CANAL
ID CAN2_CANAL Reviewed; 568 AA.
AC Q59WU0;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable lysine/arginine permease CAN2 {ECO:0000250|UniProtKB:A0A1D8PPI5};
DE AltName: Full=Basic amino acids permease CAN2 {ECO:0000305};
GN Name=CAN2 {ECO:0000303|PubMed:15917516};
GN OrderedLocusNames=CAALFM_C601060CA;
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=11532938; DOI=10.1093/emboj/20.17.4742;
RA Murad A.M., Leng P., Straffon M., Wishart J., Macaskill S., MacCallum D.,
RA Schnell N., Talibi D., Marechal D., Tekaia F., d'Enfert C., Gaillardin C.,
RA Odds F.C., Brown A.J.;
RT "NRG1 represses yeast-hypha morphogenesis and hypha-specific gene
RT expression in Candida albicans.";
RL EMBO J. 20:4742-4752(2001).
RN [5]
RP INDUCTION.
RX PubMed=11737641; DOI=10.1046/j.1365-2958.2001.02713.x;
RA Murad A.M., d'Enfert C., Gaillardin C., Tournu H., Tekaia F., Talibi D.,
RA Marechal D., Marchais V., Cottin J., Brown A.J.;
RT "Transcript profiling in Candida albicans reveals new cellular functions
RT for the transcriptional repressors CaTup1, CaMig1 and CaNrg1.";
RL Mol. Microbiol. 42:981-993(2001).
RN [6]
RP INDUCTION.
RX PubMed=15917516; DOI=10.1128/aac.49.6.2226-2236.2005;
RA Liu T.T., Lee R.E., Barker K.S., Lee R.E., Wei L., Homayouni R.,
RA Rogers P.D.;
RT "Genome-wide expression profiling of the response to azole, polyene,
RT echinocandin, and pyrimidine antifungal agents in Candida albicans.";
RL Antimicrob. Agents Chemother. 49:2226-2236(2005).
RN [7]
RP INDUCTION.
RX PubMed=15814841; DOI=10.1091/mbc.e05-01-0071;
RA Garcia-Sanchez S., Mavor A.L., Russell C.L., Argimon S., Dennison P.,
RA Enjalbert B., Brown A.J.;
RT "Global roles of Ssn6 in Tup1- and Nrg1-dependent gene regulation in the
RT fungal pathogen, Candida albicans.";
RL Mol. Biol. Cell 16:2913-2925(2005).
RN [8]
RP INDUCTION.
RX PubMed=19527170; DOI=10.1086/599838;
RA Nett J.E., Lepak A.J., Marchillo K., Andes D.R.;
RT "Time course global gene expression analysis of an in vivo Candida
RT biofilm.";
RL J. Infect. Dis. 200:307-313(2009).
RN [9]
RP INDUCTION.
RX PubMed=21592964; DOI=10.1074/jbc.m111.233569;
RA Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.;
RT "Cap2-HAP complex is a critical transcriptional regulator that has dual but
RT contrasting roles in regulation of iron homeostasis in Candida albicans.";
RL J. Biol. Chem. 286:25154-25170(2011).
RN [10]
RP INDUCTION.
RX PubMed=22265407; DOI=10.1016/j.cell.2011.10.048;
RA Nobile C.J., Fox E.P., Nett J.E., Sorrells T.R., Mitrovich Q.M.,
RA Hernday A.D., Tuch B.B., Andes D.R., Johnson A.D.;
RT "A recently evolved transcriptional network controls biofilm development in
RT Candida albicans.";
RL Cell 148:126-138(2012).
CC -!- FUNCTION: Probable permease for arginine and lysine.
CC {ECO:0000250|UniProtKB:A0A1D8PPI5}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A0A1D8PPI5};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is negatively regulated by the transcriptional
CC repressors NRG1 and TUP1 (PubMed:11532938, PubMed:11737641). Expression
CC is also regulated by SSN6 (PubMed:15814841). Expression is repressed by
CC HAP43 (PubMed:21592964). Expression is induced by antifungal agents
CC caspofungin and flucytosine (PubMed:15917516). Finally, expression is
CC also induced during biofilm development (PubMed:19527170,
CC PubMed:22265407). {ECO:0000269|PubMed:11532938,
CC ECO:0000269|PubMed:11737641, ECO:0000269|PubMed:15814841,
CC ECO:0000269|PubMed:15917516, ECO:0000269|PubMed:19527170,
CC ECO:0000269|PubMed:21592964, ECO:0000269|PubMed:22265407}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
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DR EMBL; CP017628; AOW30052.1; -; Genomic_DNA.
DR RefSeq; XP_714319.1; XM_709226.1.
DR AlphaFoldDB; Q59WU0; -.
DR SMR; Q59WU0; -.
DR STRING; 237561.Q59WU0; -.
DR PRIDE; Q59WU0; -.
DR EnsemblFungi; KHC73259; KHC73259; W5Q_04696.
DR EnsemblFungi; KHC84933; KHC84933; I503_04671.
DR GeneID; 3644017; -.
DR KEGG; cal:CAALFM_C601060CA; -.
DR CGD; CAL0000192410; CAN2.
DR VEuPathDB; FungiDB:C6_01060C_A; -.
DR HOGENOM; CLU_007946_12_1_1; -.
DR InParanoid; Q59WU0; -.
DR OMA; RTVIFFI; -.
DR OrthoDB; 621852at2759; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..568
FT /note="Probable lysine/arginine permease CAN2"
FT /id="PRO_0000439804"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 568 AA; 63145 MW; C26883D760DF45AC CRC64;
MFEVGEKYPV ESSSSSNDIE SRGVQPITSL KDNKSIGMIE KDNDDLSCEQ YSTCDEVKRD
LKARHVSMIA IGGTIGTGLF ISTGSLLHTT GPVMSLISFL FVTTLAYSVT QSLGEMTTYI
PVSGSFAQFI TRWVSKSCGA ANGWLYWFSW AITFALELSV VGQVIQYWTD AVPLAGWISI
FFVLLTTFNL FPVKYYGEVE FWIASTKVIA IVGWLIYAFC MVCGAGKTGP VGFRYWRNGY
AWGDGMIVSN NGKYAISFIN GLINAVFTFQ GTELVAVTAG EASPRAIRSA IKKVMFRILV
FYVLCMLFIG LLVPYNDPKL TQDGGFTRNS PFLIAMENSG TKVLPHIFNA VIVTTIISAG
NSNVYSGSRI LYGLAQAGVA PKFFLKTNKG GVPYFAVLFT AAFGALGYLA CSEDGNKAFT
WLLNIIATAG LIAWGFISVS HVRFMNVLRK RGLSRDILPY KAFFMPYSAY YAIIIIFIVV
LIQGFTVFWD FNASDFFTAY ISVILFVVLW IGFHFFFYGF GKDSFKWENI LIPLDDCDID
SGVRDINDAE FDVPEPKNVW ERFWLLIA
