CAN1_CANAW
ID CAN1_CANAW Reviewed; 571 AA.
AC P43059;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Lysine/arginine permease;
DE AltName: Full=Basic amino acids permease;
GN Name=CAN1;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=7725800; DOI=10.1002/yea.320101214;
RA Sychorova H., Souciet J.-L.;
RT "CAN1, a gene encoding a permease for basic amino acids in Candida
RT albicans.";
RL Yeast 10:1647-1651(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: High-affinity permease for arginine and lysine.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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; X76689; CAA54122.1; -; Genomic_DNA.
DR EMBL; CM000312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S50711; S50711.
DR AlphaFoldDB; P43059; -.
DR SMR; P43059; -.
DR STRING; 5476.P43059; -.
DR TCDB; 2.A.3.10.20; the amino acid-polyamine-organocation (apc) family.
DR Proteomes; UP000001429; Chromosome 6.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IEA:UniProt.
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 3: Inferred from homology;
KW Amino-acid transport; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..571
FT /note="Lysine/arginine permease"
FT /id="PRO_0000054149"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
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 260..280
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..36
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 CONFLICT 20
FT /note="L -> S (in Ref. 1; CAA54122)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="T -> S (in Ref. 1; CAA54122)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 571 AA; 63358 MW; 7049DB4E8172C9D6 CRC64;
MPEDYEKYRM GSSNESHQKL 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 NAWDKFWANV A