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SSU1_CANAL
ID   SSU1_CANAL              Reviewed;         481 AA.
AC   Q5A3Z6; A0A1D8PTW4;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Sulfite efflux pump SSU1;
DE   AltName: Full=Sulfite sensitivity protein SSU1;
GN   Name=SSU1; Synonyms=SSU11; OrderedLocusNames=CAALFM_CR09170CA;
GN   ORFNames=CaO19.7313;
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=12773383; DOI=10.1093/emboj/cdg256;
RA   Uhl M.A., Biery M., Craig N., Johnson A.D.;
RT   "Haploinsufficiency-based large-scale forward genetic analysis of
RT   filamentous growth in the diploid human fungal pathogen C.albicans.";
RL   EMBO J. 22:2668-2678(2003).
RN   [5]
RP   INDUCTION.
RX   PubMed=16215176; DOI=10.1128/ec.4.10.1687-1696.2005;
RA   Tournu H., Tripathi G., Bertram G., Macaskill S., Mavor A., Walker L.,
RA   Odds F.C., Gow N.A., Brown A.J.;
RT   "Global role of the protein kinase Gcn2 in the human pathogen Candida
RT   albicans.";
RL   Eukaryot. Cell 4:1687-1696(2005).
RN   [6]
RP   INDUCTION.
RX   PubMed=16030247; DOI=10.1091/mbc.e05-05-0435;
RA   Hromatka B.S., Noble S.M., Johnson A.D.;
RT   "Transcriptional response of Candida albicans to nitric oxide and the role
RT   of the YHB1 gene in nitrosative stress and virulence.";
RL   Mol. Biol. Cell 16:4814-4826(2005).
RN   [7]
RP   INDUCTION.
RX   PubMed=17614954; DOI=10.1111/j.1365-2958.2007.05788.x;
RA   Wilson D., Tutulan-Cunita A., Jung W., Hauser N.C., Hernandez R.,
RA   Williamson T., Piekarska K., Rupp S., Young T., Stateva L.;
RT   "Deletion of the high-affinity cAMP phosphodiesterase encoded by PDE2
RT   affects stress responses and virulence in Candida albicans.";
RL   Mol. Microbiol. 65:841-856(2007).
RN   [8]
RP   FUNCTION.
RX   PubMed=18083829; DOI=10.1128/ec.00240-07;
RA   Chiranand W., McLeod I., Zhou H., Lynn J.J., Vega L.A., Myers H.,
RA   Yates J.R. III, Lorenz M.C., Gustin M.C.;
RT   "CTA4 transcription factor mediates induction of nitrosative stress
RT   response in Candida albicans.";
RL   Eukaryot. Cell 7:268-278(2008).
RN   [9]
RP   INDUCTION, AND FUNCTION.
RX   PubMed=23285201; DOI=10.1371/journal.pone.0052850;
RA   Miramon P., Dunker C., Windecker H., Bohovych I.M., Brown A.J., Kurzai O.,
RA   Hube B.;
RT   "Cellular responses of Candida albicans to phagocytosis and the
RT   extracellular activities of neutrophils are critical to counteract
RT   carbohydrate starvation, oxidative and nitrosative stress.";
RL   PLoS ONE 7:E52850-E52850(2012).
RN   [10]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23417561; DOI=10.1128/ec.00336-12;
RA   Hennicke F., Grumbt M., Lermann U., Ueberschaar N., Palige K., Bottcher B.,
RA   Jacobsen I.D., Staib C., Morschhauser J., Monod M., Hube B., Hertweck C.,
RA   Staib P.;
RT   "Factors supporting cysteine tolerance and sulfite production in Candida
RT   albicans.";
RL   Eukaryot. Cell 12:604-613(2013).
CC   -!- FUNCTION: Sulfite efflux pump required for the secretion of sulfite as
CC       a reducing agent (By similarity). Plays a role in resistance to
CC       neutrophils during infection. Involved in transition to filamentous
CC       growth, which is believed to be central to the virulence of this human
CC       pathogen. {ECO:0000250, ECO:0000269|PubMed:12773383,
CC       ECO:0000269|PubMed:18083829, ECO:0000269|PubMed:23285201,
CC       ECO:0000269|PubMed:23417561}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated by cysteine, nitic oxide, and in response to
CC       neutrophil phagocytosis. Expression is under the control of GCN2, GCN4
CC       and ZCF2. {ECO:0000269|PubMed:16030247, ECO:0000269|PubMed:16215176,
CC       ECO:0000269|PubMed:17614954, ECO:0000269|PubMed:23285201,
CC       ECO:0000269|PubMed:23417561}.
CC   -!- DISRUPTION PHENOTYPE: Leads to enhanced sensitivity to both cysteine
CC       and sulfite. {ECO:0000269|PubMed:23417561}.
CC   -!- SIMILARITY: Belongs to the tellurite-resistance/dicarboxylate
CC       transporter (TDT) family. {ECO:0000305}.
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DR   EMBL; CP017630; AOW31582.1; -; Genomic_DNA.
DR   RefSeq; XP_716447.1; XM_711354.1.
DR   AlphaFoldDB; Q5A3Z6; -.
DR   STRING; 237561.Q5A3Z6; -.
DR   GeneID; 3641882; -.
DR   KEGG; cal:CAALFM_CR09170CA; -.
DR   CGD; CAL0000176038; SSU1.
DR   VEuPathDB; FungiDB:CR_09170C_A; -.
DR   eggNOG; ENOG502QT02; Eukaryota.
DR   HOGENOM; CLU_030057_6_2_1; -.
DR   InParanoid; Q5A3Z6; -.
DR   OMA; PVQSMFI; -.
DR   OrthoDB; 819178at2759; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0000319; F:sulfite transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR   GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR   GO; GO:0000316; P:sulfite transport; IBA:GO_Central.
DR   Gene3D; 1.50.10.150; -; 1.
DR   InterPro; IPR004695; SLAC1/Mae1/Ssu1/TehA.
DR   InterPro; IPR038665; Voltage-dep_anion_channel_sf.
DR   Pfam; PF03595; SLAC1; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Virulence.
FT   CHAIN           1..481
FT                   /note="Sulfite efflux pump SSU1"
FT                   /id="PRO_0000422069"
FT   TOPO_DOM        1..108
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..137
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..176
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..204
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        226..244
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..273
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        295..312
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        334..353
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        375..438
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        460..481
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   481 AA;  54203 MW;  7317CFF826BE74D9 CRC64;
     MSSSSHNDNK IPPEKTTTPP LSSSNEDIYN PADSSNVLSS NQTLVSTNNN NNNNQNNNQN
     NNQNNDGKDT MDHLSYLSTI DSKRREQSYL KSFYQRFIIE DVVKNFTPAY FVSVMGTGIS
     SSLLYNFPFP AYWLQICGYV MFGLTCTFFI GNIILLIMSC AYYPNRFRDY HVDPSRAVFM
     GAFSMGYITI VNFIALITKG EHIYFVWTLW WLAVFSAMYT SFLIVYLSFM SKLNESDVEA
     KLNATLLLPI VAITVVSSSG HSIELDLPHV HQTVLTMIVS FMLWSLSISM AFMVMTLYMG
     RLIIHKIPPT NLIMTSFLPV GFLGQSSYSI YLFGNNLNKF IPEELLYGKI SLCLSGFVSV
     FLLSFGYFMC FVAVTSVLSK IRPFAKNPNP SHTNRFGLLK LEKSFWSMTF PMGTMSLSNT
     EIGHGGVGNY PLLTFKVMGS IFAAACIFIT VGCSIGVVVY SFKKLREDMT NKNKYRNESM
     V
 
 
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