CAN3_CANAL
ID CAN3_CANAL Reviewed; 566 AA.
AC A0A1D8PPG4;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Probable lysine/arginine permease CAN3 {ECO:0000250|UniProtKB:A0A1D8PPI5};
DE AltName: Full=Basic amino acids permease CAN3 {ECO:0000305};
GN Name=CAN3 {ECO:0000303|PubMed:12397174};
GN OrderedLocusNames=CAALFM_C600830CA;
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=12397174; DOI=10.1073/pnas.232566499;
RA Lan C.Y., Newport G., Murillo L.A., Jones T., Scherer S., Davis R.W.,
RA Agabian N.;
RT "Metabolic specialization associated with phenotypic switching in
RT Candidaalbicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14907-14912(2002).
RN [5]
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).
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 regulated upon white-opaque switch
CC (PubMed:12397174). Expression is repressed by HAP43 (PubMed:21592964).
CC {ECO:0000269|PubMed:12397174, ECO:0000269|PubMed:21592964}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017628; AOW30029.1; -; Genomic_DNA.
DR RefSeq; XP_019330993.1; XM_019475448.1.
DR AlphaFoldDB; A0A1D8PPG4; -.
DR SMR; A0A1D8PPG4; -.
DR STRING; 237561.A0A1D8PPG4; -.
DR GeneID; 3647066; -.
DR KEGG; cal:CAALFM_C600830CA; -.
DR CGD; CAL0000197464; CAN3.
DR VEuPathDB; FungiDB:C6_00830C_A; -.
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..566
FT /note="Probable lysine/arginine permease CAN3"
FT /id="PRO_0000439805"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 566 AA; 62895 MW; 7CC290C5BCE04232 CRC64;
MVLLKEKPRT IGTDSDNSIY KDIEQSITPP SDKNEIFIDQ INNDRITEYD SHGEVKRDLK
ARHVAMIGIG STIGTGLFIS TGHLLSQTGP VMSLISFLFV TTICFSVTQS LGEMATYIPV
SGSFVQFITR WVSKSCGAAN GWLYGWSWAI TFGLELSIVG QVIQFWTDAI PLAAWISIFF
VLLTALNLFP VKFYGEIEFW MASIKLTAVI GWIIYAFCMV CGAGKTGPVG FRYWRNGYAW
GDGMIVSNNG KYAIAFINGL INAVFTFQGT ELVAITAGEA SPKALKSAIR KVMFRILVFY
VLCMLFIGLL VPYNDPKLTE DGGFTRNSPF LIAMENSGTK VLPHIFNAVI VTTIISAGNS
TVYAGSRIFY GLAESGVAPK IFLSTTKAGV PYVAVLFTAA FGALGYLVVS NDGTVVFNWL
LNIAATAGLV AWGFISVSHI RFMQVLKQRG ISRDTLPFKA FFMPYSAYYA AIVVFTVALI
QGFTVFWDFN ATDFFTAYVS LIVFVVWWIM FHFFFFGFGK QAWKWSNVLI PLEECDIDTG
VRDINDIEFD VPPPKNLWQK FWLIIA