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SUN41_CANAL
ID   SUN41_CANAL             Reviewed;         418 AA.
AC   Q59NP5; A0A1D8PPG8;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Secreted beta-glucosidase SUN41;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   Name=SUN41 {ECO:0000303|PubMed:12492856}; Synonyms=SUN4;
GN   OrderedLocusNames=CAALFM_C600820WA; ORFNames=CaO19.11124, CaO19.3642;
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   PREDICTION AS A SUBSTRATE FOR KEX2 CLEAVAGE.
RX   PubMed=12419804; DOI=10.1074/jbc.m209713200;
RA   Newport G., Kuo A., Flattery A., Gill C., Blake J.J., Kurtz M.B.,
RA   Abruzzo G.K., Agabian N.;
RT   "Inactivation of Kex2p diminishes the virulence of Candida albicans.";
RL   J. Biol. Chem. 278:1713-1720(2003).
RN   [5]
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   [6]
RP   INDUCTION.
RX   PubMed=15917516; DOI=10.1128/aac.49.6.2226-2236.2005;
RA   Liu T.T., Lee R.E., Barker K.S., Lee R.E., Wei L., Homayouni R.,
RA   Rogers P.D.;
RT   "Genome-wide expression profiling of the response to azole, polyene,
RT   echinocandin, and pyrimidine antifungal agents in Candida albicans.";
RL   Antimicrob. Agents Chemother. 49:2226-2236(2005).
RN   [7]
RP   INDUCTION.
RX   PubMed=16854431; DOI=10.1016/j.jmb.2006.06.040;
RA   Setiadi E.R., Doedt T., Cottier F., Noffz C., Ernst J.F.;
RT   "Transcriptional response of Candida albicans to hypoxia: linkage of oxygen
RT   sensing and Efg1p-regulatory networks.";
RL   J. Mol. Biol. 361:399-411(2006).
RN   [8]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17873081; DOI=10.1128/ec.00314-07;
RA   Norice C.T., Smith F.J. Jr., Solis N., Filler S.G., Mitchell A.P.;
RT   "Requirement for Candida albicans Sun41 in biofilm formation and
RT   virulence.";
RL   Eukaryot. Cell 6:2046-2055(2007).
RN   [9]
RP   DISRUPTION PHENOTYPE, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=17905924; DOI=10.1128/ec.00285-07;
RA   Hiller E., Heine S., Brunner H., Rupp S.;
RT   "Candida albicans Sun41p, a putative glycosidase, is involved in
RT   morphogenesis, cell wall biogenesis, and biofilm formation.";
RL   Eukaryot. Cell 6:2056-2065(2007).
RN   [10]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=18001349; DOI=10.1111/j.1365-2958.2007.06011.x;
RA   Firon A., Aubert S., Iraqui I., Guadagnini S., Goyard S., Prevost M.C.,
RA   Janbon G., d'Enfert C.;
RT   "The SUN41 and SUN42 genes are essential for cell separation in Candida
RT   albicans.";
RL   Mol. Microbiol. 66:1256-1275(2007).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=19819358; DOI=10.1016/j.jprot.2009.10.003;
RA   Thomas D.P., Lopez-Ribot J.L., Lee S.A.;
RT   "A proteomic analysis of secretory proteins of a pre-vacuolar mutant of
RT   Candida albicans.";
RL   J. Proteomics 73:342-351(2009).
RN   [12]
RP   INDUCTION.
RX   PubMed=19798425; DOI=10.1371/journal.ppat.1000601;
RA   Sahni N., Yi S., Daniels K.J., Srikantha T., Pujol C., Soll D.R.;
RT   "Genes selectively up-regulated by pheromone in white cells are involved in
RT   biofilm formation in Candida albicans.";
RL   PLoS Pathog. 5:E1000601-E1000601(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
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   [14]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=23508952; DOI=10.1074/jbc.m112.440172;
RA   Gastebois A., Aimanianda V., Bachellier-Bassi S., Nesseir A., Firon A.,
RA   Beauvais A., Schmitt C., England P., Beau R., Prevost M.C., d'Enfert C.,
RA   Latge J.P., Mouyna I.;
RT   "SUN proteins belong to a novel family of beta-(1,3)-glucan-modifying
RT   enzymes involved in fungal morphogenesis.";
RL   J. Biol. Chem. 288:13387-13396(2013).
CC   -!- FUNCTION: Cell surface beta-glucosidase involved in cytokinesis, cell
CC       wall biogenesis, adhesion to host tissue, and biofilm formation; thus
CC       playing an important role in the host-pathogen interaction. Has
CC       hydrolytic activity on linear (1->3)-beta-D-glucans such as
CC       laminaribiose and other laminarioligosaccharides.
CC       {ECO:0000269|PubMed:17873081, ECO:0000269|PubMed:17905924,
CC       ECO:0000269|PubMed:18001349, ECO:0000269|PubMed:23508952}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5. {ECO:0000269|PubMed:23508952};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:21622905}. Secreted {ECO:0000269|PubMed:17905924,
CC       ECO:0000269|PubMed:19819358}. Note=Secreted into the medium of cells
CC       growing as blastospores as well as those forming hyphae
CC       (PubMed:17905924). Secretion is decreased in cells lacking VPS4
CC       (PubMed:19819358). {ECO:0000269|PubMed:17905924,
CC       ECO:0000269|PubMed:19819358}.
CC   -!- INDUCTION: Strongly up-regulated under hypoxic conditions and in white
CC       but not opaque cells (PubMed:16854431, PubMed:19798425). Repressed by
CC       exposure to caspofungin (PubMed:15917516). Expression is probably
CC       regulated by EFG1 since SUN41 has 9 E-boxes in its promoter
CC       (PubMed:12492856). {ECO:0000269|PubMed:12492856,
CC       ECO:0000269|PubMed:15917516, ECO:0000269|PubMed:16854431,
CC       ECO:0000269|PubMed:19798425}.
CC   -!- PTM: Predicted to be a substrate for cleavage by KEX2.
CC       {ECO:0000305|PubMed:12419804}.
CC   -!- DISRUPTION PHENOTYPE: Leads to increased cell size, cytokinesis
CC       defects, altered sensitivity to the cell wall-modifying substance Congo
CC       red, defects in adhesion, and reduced biofilm formation.
CC       {ECO:0000269|PubMed:17873081, ECO:0000269|PubMed:17905924,
CC       ECO:0000269|PubMed:18001349}.
CC   -!- SIMILARITY: Belongs to the SUN family. {ECO:0000305}.
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DR   EMBL; CP017628; AOW30028.1; -; Genomic_DNA.
DR   RefSeq; XP_711315.2; XM_706223.2.
DR   AlphaFoldDB; Q59NP5; -.
DR   BioGRID; 1230112; 3.
DR   STRING; 237561.Q59NP5; -.
DR   CAZy; GH132; Glycoside Hydrolase Family 132.
DR   GeneID; 3647067; -.
DR   KEGG; cal:CAALFM_C600820WA; -.
DR   CGD; CAL0000175157; SUN41.
DR   VEuPathDB; FungiDB:C6_00820W_A; -.
DR   HOGENOM; CLU_033459_2_0_1; -.
DR   InParanoid; Q59NP5; -.
DR   OMA; CSYACQS; -.
DR   OrthoDB; 1130819at2759; -.
DR   PRO; PR:Q59NP5; -.
DR   Proteomes; UP000000559; Chromosome 6.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005556; SUN.
DR   Pfam; PF03856; SUN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell wall; Cell wall biogenesis/degradation;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..418
FT                   /note="Secreted beta-glucosidase SUN41"
FT                   /id="PRO_0000425079"
FT   REGION          81..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   418 AA;  43693 MW;  50A64905AD1E7B5A CRC64;
     MRFSQATVLA FAALSLAAPA FEADNKNIKR EDCDKTSFHG HHKHKRAVAY DYAYVTVTVD
     GNGNPITTVS PVLSIETIAK SEETSSTSTS ISSTTTIVQN DSLTSDEPKT LSLPSGTIKP
     SSFATESQSQ SQSSSTGGSG SGSTNGIEGD LAAFEDPTEE FEDGVLSCSD FPSGQGVIPL
     DHLGFGGWSG IENSDGSTGG NCKEGSYCSY ACQSGMSKTQ WPEDQPSNGV SIGGLLCKNG
     KLYKSSTRSN YLCEWGVKKA NVVNKLSETV AICRTDYPGT ENMVIPTVVG GGSTSVITVV
     DQSTYYTWRG GATSAQYYVN NAGVSWEDGC VWGTPGSGVG NWAPLNFGAG YANGIAYLSL
     IPNPNNRDSL NFKVKIVGES GSTVSGSCSY ANGKFNGNSD DGCTVGVTSG EADFVLYN
 
 
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