CAN1_CANAL
ID CAN1_CANAL Reviewed; 571 AA.
AC A0A1D8PPI5;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Lysine/arginine permease CAN1 {ECO:0000303|PubMed:8299168};
DE AltName: Full=Basic amino acids permease CAN1 {ECO:0000305};
GN Name=CAN1 {ECO:0000303|PubMed:8299168}; OrderedLocusNames=CAALFM_C600960WA;
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.
RX PubMed=8299168; DOI=10.1007/bf00351710;
RA Sychrova H., Chevallier M.R.;
RT "Transport properties of a C. albicans amino-acid permease whose putative
RT gene was cloned and expressed in S. cerevisiae.";
RL Curr. Genet. 24:487-490(1993).
RN [5]
RP FUNCTION.
RX PubMed=9180275; DOI=10.1016/s0014-5793(97)00396-7;
RA Matijekova A., Sychrova H.;
RT "Biogenesis of Candida albicans Can1 permease expressed in Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 408:89-93(1997).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10418152; DOI=10.1111/j.1574-6968.1999.tb13670.x;
RA Matejckova-Forejtova A., Kinclova O., Sychrova H.;
RT "Degradation of Candida albicans Can1 permease expressed in Saccharomyces
RT cerevisiae.";
RL FEMS Microbiol. Lett. 176:257-262(1999).
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 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=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 [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: High-affinity permease for basic amino acids arginine, lysine
CC and histidine (PubMed:8299168, PubMed:9180275).
CC {ECO:0000269|PubMed:8299168, ECO:0000269|PubMed:9180275}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10418152};
CC Multi-pass membrane protein {ECO:0000255}. Note=Degraded in the vacuole
CC after internalization by endocytosis in a ubiquitin-dependent manner
CC when expressed in S.cereviae (PubMed:10418152).
CC {ECO:0000269|PubMed:10418152}.
CC -!- INDUCTION: Expression is induced during phagocytosis by host
CC macrophages (PubMed:15470236). Expression is also induced during
CC biofilm development (PubMed:19527170, PubMed:21414038,
CC PubMed:22265407). {ECO:0000269|PubMed:15470236,
CC ECO:0000269|PubMed:19527170, ECO:0000269|PubMed:21414038,
CC 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; AOW30042.1; -; Genomic_DNA.
DR RefSeq; XP_714306.1; XM_709213.1.
DR AlphaFoldDB; A0A1D8PPI5; -.
DR SMR; A0A1D8PPI5; -.
DR STRING; 237561.A0A1D8PPI5; -.
DR GeneID; 3644035; -.
DR KEGG; cal:CAALFM_C600960WA; -.
DR CGD; CAL0000201116; CAN1.
DR VEuPathDB; FungiDB:C6_00960W_A; -.
DR eggNOG; KOG1286; Eukaryota.
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; IGI:CGD.
DR GO; GO:0016597; F:amino acid binding; NAS:CGD.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; ISS:CGD.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; IDA:CGD.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; IDA:CGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015802; P:basic amino acid transport; IDA:CGD.
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..571
FT /note="Lysine/arginine permease CAN1"
FT /id="PRO_0000439803"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 571 AA; 63331 MW; 7AB5E7B7B272C9D1 CRC64;
MPEDYEKYRM GSSNESHQKS VQPISSSISK SNKKTKHQTD FVQDSDIIEA SSINDEFGEV
KRDLKARHVS MIAIGGTIGT GLFISTGSLL HTTGPVMSLI SFLFVTTICF SVTQSLGEMA
TYIPISGSFA QFVTRWVSKS CGAANGWLYW FSWAVTFGLE LSVVGQVIQF WTDAVPLAAW
ISIFFVILTI FNFFPVKFYG EVEFWIASIK IIAVFGWIIY AFIMVCGAGK TGPVGFRYWR
NGYAWGDGIL VNNNGKYVAA FVSGLINSIF TFQGTELVAV TAGEASPRAL RSAIRKVMFR
ILVFYVLCML FMGLLVPYND PKLTQDGGFT RNSPFLIAME NSGTKVLPHI FNAVIVTTII
SAGNSNIYSG SRILYGLAQA GVAPKFFLRT NKGGVPFFAV AFTAAFGALG YLACSSQGNK
AFTWLLNITA TAGLISWGFI SVSHIRFMKT LQRRGISRDT LPFKAFFMPF SAYYGMVVCF
IVVLIQGFTV FWDFNASDFF TAYISVILFV VLWVGFHFFF YGFGKDSFKM SNILVPLDEC
DIDSGVRDIN DAEFDIPPPK NAWDKFWAIV A
