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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}.
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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
 
 
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