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Septin CDC11 (Cell division control protein 11)

 CDC11_CANAL             Reviewed;         402 AA.
G1UB61; A0A1D8PMT9;
13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
19-OCT-2011, sequence version 1.
25-OCT-2017, entry version 35.
RecName: Full=Septin CDC11;
AltName: Full=Cell division control protein 11;
Name=CDC11; OrderedLocusNames=CAALFM_C500070WA; ORFNames=CaO19.5691;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[2]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[4]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=11454197; DOI=10.1046/j.1365-2958.2001.02459.x;
Sudbery P.E.;
"The germ tubes of Candida albicans hyphae and pseudohyphae show
different patterns of septin ring localization.";
Mol. Microbiol. 41:19-31(2001).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12181342; DOI=10.1091/mbc.E02-01-0013;
Warenda A.J., Konopka J.B.;
"Septin function in Candida albicans morphogenesis.";
Mol. Biol. Cell 13:2732-2746(2002).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12819094; DOI=10.1128/IAI.71.7.4045-4051.2003;
Warenda A.J., Kauffman S., Sherrill T.P., Becker J.M., Konopka J.B.;
"Candida albicans septin mutants are defective for invasive growth and
virulence.";
Infect. Immun. 71:4045-4051(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SEPTIN
COMPLEX.
PubMed=15449307; DOI=10.1002/yea.1147;
Kaneko A., Umeyama T., Hanaoka N., Monk B.C., Uehara Y., Niimi M.;
"Tandem affinity purification of the Candida albicans septin protein
complex.";
Yeast 21:1025-1033(2004).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16002645; DOI=10.1128/EC.4.7.1191-1202.2005;
Martin S.W., Douglas L.M., Konopka J.B.;
"Cell cycle dynamics and quorum sensing in Candida albicans
chlamydospores are distinct from budding and hyphal growth.";
Eukaryot. Cell 4:1191-1202(2005).
[9]
INTERACTION WITH HSL1.
PubMed=15659158; DOI=10.1111/j.1365-2958.2004.04405.x;
Umeyama T., Kaneko A., Nagai Y., Hanaoka N., Tanabe K., Takano Y.,
Niimi M., Uehara Y.;
"Candida albicans protein kinase CaHsl1p regulates cell elongation and
virulence.";
Mol. Microbiol. 55:381-395(2005).
[10]
PHOSPHORYLATION AT SER-4; SER-394 AND SER-395, MUTAGENESIS OF SER-394
AND SER-395, ACETYLATION AT MET-1, AND FUNCTION.
PubMed=17765684; DOI=10.1016/j.devcel.2007.06.011;
Sinha I., Wang Y.M., Philp R., Li C.R., Yap W.H., Wang Y.;
"Cyclin-dependent kinases control septin phosphorylation in Candida
albicans hyphal development.";
Dev. Cell 13:421-432(2007).
[11]
FUNCTION.
PubMed=17504812; DOI=10.1242/jcs.002931;
Li C.R., Lee R.T., Wang Y.M., Zheng X.D., Wang Y.;
"Candida albicans hyphal morphogenesis occurs in Sec3p-independent and
Sec3p-dependent phases separated by septin ring formation.";
J. Cell Sci. 120:1898-1907(2007).
[12]
SUBCELLULAR LOCATION.
PubMed=19915075; DOI=10.1128/EC.00327-09;
Zhang C., Konopka J.B.;
"A photostable green fluorescent protein variant for analysis of
protein localization in Candida albicans.";
Eukaryot. Cell 9:224-226(2010).
[13]
DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
PubMed=22687514; DOI=10.1128/AAC.00112-12;
Badrane H., Nguyen M.H., Blankenship J.R., Cheng S., Hao B.,
Mitchell A.P., Clancy C.J.;
"Rapid redistribution of phosphatidylinositol-(4,5)-bisphosphate and
septins during the Candida albicans response to caspofungin.";
Antimicrob. Agents Chemother. 56:4614-4624(2012).
-!- FUNCTION: Septins are GTPases involved in cytokinesis that
assemble early in the cell cycle as a patch at the incipient bud
site and form a ring before bud emergence, which transforms into
an hour-glass shaped collar of cortical filaments that spans both
sides of the mother-bud neck. This collar persists until just
before cytokinesis, when it splits into two rings that occupy
opposite sides of the neck. The septins at the bud neck serve as a
structural scaffold that recruits different components involved in
diverse processes at specific stages during the cell cycle. Many
proteins bind asymmetrically to the septin collar. The septin
assembly is regulated by protein kinase GIN4. Septins are also
involved in cell morphogenesis, chlamydospores morphogenesis, bud
site selection, chitin deposition, cell cycle regulation, cell
compartmentalization, and spore wall formation. CDC11 is required
for the correct localization of SEC3 at bud tips and bud necks.
Plays a key role in invasive growth and virulence.
{ECO:0000269|PubMed:11454197, ECO:0000269|PubMed:12181342,
ECO:0000269|PubMed:12819094, ECO:0000269|PubMed:16002645,
ECO:0000269|PubMed:17504812, ECO:0000269|PubMed:17765684}.
-!- SUBUNIT: Component of the septin complex which consists of CDC3,
CDC10, CDC11, CDC12 and probably SEP7. The purified septin complex
appeared to have a stoichiometry of 2 CDC3, 1 to 2 CDC10, 1 CDC11,
2 CDC12, and 1 or none SEP7 subunit. Interacts with HSL1.
{ECO:0000269|PubMed:15449307, ECO:0000269|PubMed:15659158}.
-!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:11454197,
ECO:0000269|PubMed:12181342, ECO:0000269|PubMed:19915075,
ECO:0000269|PubMed:22687514}. Note=Localizes to a tight ring at
the bud and pseudohyphae necks and as a more diffuse array in
emerging germ tubes of hyphae.
-!- PTM: Hyphal induction causes immediate phosphorylation at Ser-395
by GIN4 and at Ser-394 by CDC28-CCN1. GIN4 phosphorylation at Ser-
395 primes CDC11 for further phosphorylation by CDC28-CCN1. CDC28-
HGC1 then maintains CDC11 phosphorylation throughout hyphal
growth. Ser-4 is also phosphorylated in yeast cells but not hyphal
cells. {ECO:0000269|PubMed:17765684}.
-!- PTM: Met-1 is acetylated. {ECO:0000269|PubMed:17765684}.
-!- DISRUPTION PHENOTYPE: Causes greater curvature of cells growing in
a filamentous manner and morphological defects in suspensor cells
and chlamydospores. Leads to reduced tissue penetration and non-
invasive fungal masses in mice infected kidneys. Leads also to
hypersusceptibility to caspofungin. {ECO:0000269|PubMed:12819094,
ECO:0000269|PubMed:16002645, ECO:0000269|PubMed:22687514}.
-!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-
like GTPase superfamily. Septin GTPase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; CP017627; AOW29453.1; -; Genomic_DNA.
RefSeq; XP_710520.1; XM_705428.1.
ProteinModelPortal; G1UB61; -.
SMR; G1UB61; -.
BioGrid; 1230981; 3.
iPTMnet; G1UB61; -.
PRIDE; G1UB61; -.
GeneID; 3647888; -.
KEGG; cal:CAALFM_C500070WA; -.
CGD; CAL0000177264; CDC11.
EuPathDB; FungiDB:C5_00070W_A; -.
InParanoid; G1UB61; -.
KO; K16945; -.
OrthoDB; EOG092C3HL6; -.
Proteomes; UP000000559; Chromosome 5.
GO; GO:0005935; C:cellular bud neck; IDA:CGD.
GO; GO:0000144; C:cellular bud neck septin ring; IDA:CGD.
GO; GO:0000399; C:cellular bud neck septin structure; IDA:CGD.
GO; GO:0032168; C:hyphal septin ring; IDA:CGD.
GO; GO:0001411; C:hyphal tip; IDA:CGD.
GO; GO:0005940; C:septin ring; IDA:CGD.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0008105; P:asymmetric protein localization; IMP:CGD.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006033; P:chitin localization; IMP:CGD.
GO; GO:0001410; P:chlamydospore formation; IMP:CGD.
GO; GO:0070783; P:growth of unicellular organism as a thread of attached cells; IMP:CGD.
GO; GO:0030448; P:hyphal growth; IMP:CGD.
GO; GO:0030011; P:maintenance of cell polarity; IMP:CGD.
GO; GO:0007097; P:nuclear migration; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IMP:CGD.
GO; GO:0000921; P:septin ring assembly; IMP:CGD.
CDD; cd01850; CDC_Septin; 1.
InterPro; IPR030379; G_SEPTIN_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR016491; Septin.
Pfam; PF00735; Septin; 1.
PIRSF; PIRSF006698; Septin; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51719; G_SEPTIN; 1.
1: Evidence at protein level;
Acetylation; Cell cycle; Cell division; Coiled coil;
Complete proteome; GTP-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; Virulence.
CHAIN 1 402 Septin CDC11.
/FTId=PRO_0000424349.
DOMAIN 21 307 Septin-type G.
NP_BIND 31 38 GTP. {ECO:0000250}.
NP_BIND 172 180 GTP. {ECO:0000250}.
COILED 318 376 {ECO:0000255}.
MOTIF 14 21 Basic motif. {ECO:0000250}.
BINDING 233 233 GTP; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:17765684}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000269|PubMed:17765684}.
MOD_RES 394 394 Phosphoserine; by CDC28.
{ECO:0000269|PubMed:17765684}.
MOD_RES 395 395 Phosphoserine; by GIN4.
{ECO:0000269|PubMed:17765684}.
MUTAGEN 394 394 S->A: Blocks phosphorylation of Ser-394
and impairs hyphal morphogenesis.
{ECO:0000269|PubMed:17765684}.
MUTAGEN 395 395 S->A: Blocks phosphorylation of Ser-394
and Ser-395 and impairs hyphal
morphogenesis.
{ECO:0000269|PubMed:17765684}.
SEQUENCE 402 AA; 46712 MW; 9D09A5D55B3BC87E CRC64;
MNYSTENVSS AALRKRKTLK KSINFSIMII GESGSGRSTL INTLCGGNSI VPTSSTATQD
PFTKKLTLRH ENVELEDNEG HKISLNIIDT PNFANSINCD DDFKIIVDFI RHQFDEVLLE
ESRVKRNPRF KDGRIHVLIY MINPTGHGLS DIDVKFLQHV NNLVNIIPII SKADSLTPKE
LKLNKELILE DLNNYGINFY KFNEYDYEQD YIDEEIIEYN KYLNSLIPFA IIGANEYRSN
PNGSEDEDDI LKLRILNKDF KPIDIDNAEI NDFTILKNVL LVTHLNEFKD ITHDSIYENY
RTEALSGKQF QYVNKDSAKQ EISESDYLMK EEQIKLEEER LRKFEERVHQ DLINKRKELL
ERENELKEIE KRLLAEGLKF DENGDVVKVH EEESSENEVK VI


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