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RBE1_CANAL
ID   RBE1_CANAL              Reviewed;         271 AA.
AC   Q59ZX3; A0A1D8PFU5;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Repressed by EFG1 protein 1;
DE   AltName: Full=PRY family cell wall protein 2;
DE   Flags: Precursor;
GN   Name=RBE1; Synonyms=PRY2; OrderedLocusNames=CAALFM_C114120CA;
GN   ORFNames=CaO19.7218;
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=12492856; DOI=10.1046/j.1365-2958.2003.03300.x;
RA   Sohn K., Urban C., Brunner H., Rupp S.;
RT   "EFG1 is a major regulator of cell wall dynamics in Candida albicans as
RT   revealed by DNA microarrays.";
RL   Mol. Microbiol. 47:89-102(2003).
RN   [5]
RP   INDUCTION.
RX   PubMed=15554973; DOI=10.1111/j.1365-2958.2004.04350.x;
RA   Bensen E.S., Martin S.J., Li M., Berman J., Davis D.A.;
RT   "Transcriptional profiling in Candida albicans reveals new adaptive
RT   responses to extracellular pH and functions for Rim101p.";
RL   Mol. Microbiol. 54:1335-1351(2004).
RN   [6]
RP   INDUCTION.
RX   PubMed=15814841; DOI=10.1091/mbc.e05-01-0071;
RA   Garcia-Sanchez S., Mavor A.L., Russell C.L., Argimon S., Dennison P.,
RA   Enjalbert B., Brown A.J.;
RT   "Global roles of Ssn6 in Tup1- and Nrg1-dependent gene regulation in the
RT   fungal pathogen, Candida albicans.";
RL   Mol. Biol. Cell 16:2913-2925(2005).
RN   [7]
RP   INDUCTION.
RX   PubMed=20870877; DOI=10.1128/ec.00159-10;
RA   Synnott J.M., Guida A., Mulhern-Haughey S., Higgins D.G., Butler G.;
RT   "Regulation of the hypoxic response in Candida albicans.";
RL   Eukaryot. Cell 9:1734-1746(2010).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=20167299; DOI=10.1016/j.jprot.2010.02.008;
RA   Hernaez M.L., Ximenez-Embun P., Martinez-Gomariz M.,
RA   Gutierrez-Blazquez M.D., Nombela C., Gil C.;
RT   "Identification of Candida albicans exposed surface proteins in vivo by a
RT   rapid proteomic approach.";
RL   J. Proteomics 73:1404-1409(2010).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=20641015; DOI=10.1002/yea.1775;
RA   Sorgo A.G., Heilmann C.J., Dekker H.L., Brul S., de Koster C.G., Klis F.M.;
RT   "Mass spectrometric analysis of the secretome of Candida albicans.";
RL   Yeast 27:661-672(2010).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=21622905; DOI=10.1128/ec.05011-11;
RA   Sorgo A.G., Heilmann C.J., Dekker H.L., Bekker M., Brul S., de Koster C.G.,
RA   de Koning L.J., Klis F.M.;
RT   "Effects of fluconazole on the secretome, the wall proteome, and wall
RT   integrity of the clinical fungus Candida albicans.";
RL   Eukaryot. Cell 10:1071-1081(2011).
RN   [11]
RP   INDUCTION.
RX   PubMed=21843869; DOI=10.1016/j.chom.2011.07.005;
RA   Chen C., Pande K., French S.D., Tuch B.B., Noble S.M.;
RT   "An iron homeostasis regulatory circuit with reciprocal roles in Candida
RT   albicans commensalism and pathogenesis.";
RL   Cell Host Microbe 10:118-135(2011).
RN   [12]
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).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION, AND
RP   INDUCTION.
RX   PubMed=23136884; DOI=10.1111/mmi.12087;
RA   Rohm M., Lindemann E., Hiller E., Ermert D., Lemuth K., Trkulja D.,
RA   Sogukpinar O., Brunner H., Rupp S., Urban C.F., Sohn K.;
RT   "A family of secreted pathogenesis-related proteins in Candida albicans.";
RL   Mol. Microbiol. 87:132-151(2013).
CC   -!- FUNCTION: Cell wall protein involved in cell wall integrity and which
CC       plays a role in virulence. {ECO:0000269|PubMed:23136884}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:20167299,
CC       ECO:0000269|PubMed:20641015, ECO:0000269|PubMed:21622905,
CC       ECO:0000269|PubMed:23136884}.
CC   -!- INDUCTION: Induced by ketoconazoland fluconazole; and repressed by
CC       EFG1, RIM101, SSN6, and alkaline conditions. Enriched in the media of
CC       yeast form-containing cultures. Expression is also regulated by HAP43,
CC       SEF1, and SFU1. {ECO:0000269|PubMed:12492856,
CC       ECO:0000269|PubMed:15554973, ECO:0000269|PubMed:15814841,
CC       ECO:0000269|PubMed:20641015, ECO:0000269|PubMed:20870877,
CC       ECO:0000269|PubMed:21592964, ECO:0000269|PubMed:21622905,
CC       ECO:0000269|PubMed:21843869, ECO:0000269|PubMed:23136884}.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; CP017623; AOW27012.1; -; Genomic_DNA.
DR   RefSeq; XP_715019.1; XM_709926.1.
DR   AlphaFoldDB; Q59ZX3; -.
DR   SMR; Q59ZX3; -.
DR   STRING; 237561.Q59ZX3; -.
DR   GeneID; 3643317; -.
DR   KEGG; cal:CAALFM_C114120CA; -.
DR   CGD; CAL0000190649; RBE1.
DR   VEuPathDB; FungiDB:C1_14120C_A; -.
DR   eggNOG; KOG3017; Eukaryota.
DR   HOGENOM; CLU_035730_3_0_1; -.
DR   InParanoid; Q59ZX3; -.
DR   OMA; AFFRVNV; -.
DR   OrthoDB; 1528782at2759; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0009986; C:cell surface; IDA:CGD.
DR   GO; GO:0005576; C:extracellular region; IDA:CGD.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR   GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR   GO; GO:0015485; F:cholesterol binding; IDA:CGD.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.33.10; -; 1.
DR   InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR001283; CRISP-related.
DR   PANTHER; PTHR10334; PTHR10334; 1.
DR   Pfam; PF00188; CAP; 1.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; SSF55797; 1.
DR   PROSITE; PS01009; CRISP_1; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Cell wall biogenesis/degradation; Glycoprotein;
KW   Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..271
FT                   /note="Repressed by EFG1 protein 1"
FT                   /id="PRO_0000424913"
FT   DOMAIN          128..244
FT                   /note="SCP"
FT   REGION          59..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   271 AA;  29078 MW;  7A453B25C4C10D67 CRC64;
     MKITNTLLNA AALLAVTEAA TITKFFTAST QTLFVTQTSQ TVVATKSFVE TIYSAPPKQL
     TSKTQDSTSP TTSSVNSLTS SSATSYVETT TPAPSSSTLT TSTISSSTAS EDSDATPTAD
     VEFAEEILKE HNVKRALHGV PALSWSNKLA EYAQDYANTG FDCSNLNLKH SGGPYGENLA
     AGYMGGISPV DAWYDEISMV DWNNVDFTES TGHFTQLVWR STTQVGCAKM MCSTAWRQIT
     VCEYLPRGNV IGLNVTSGHS YFVDNVLPPL K
 
 
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