CDC11_CANAL
ID CDC11_CANAL Reviewed; 402 AA.
AC G1UB61; A0A1D8PMT9;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Septin CDC11;
DE AltName: Full=Cell division control protein 11;
GN Name=CDC11; OrderedLocusNames=CAALFM_C500070WA; ORFNames=CaO19.5691;
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 SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11454197; DOI=10.1046/j.1365-2958.2001.02459.x;
RA Sudbery P.E.;
RT "The germ tubes of Candida albicans hyphae and pseudohyphae show different
RT patterns of septin ring localization.";
RL Mol. Microbiol. 41:19-31(2001).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12181342; DOI=10.1091/mbc.e02-01-0013;
RA Warenda A.J., Konopka J.B.;
RT "Septin function in Candida albicans morphogenesis.";
RL Mol. Biol. Cell 13:2732-2746(2002).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12819094; DOI=10.1128/iai.71.7.4045-4051.2003;
RA Warenda A.J., Kauffman S., Sherrill T.P., Becker J.M., Konopka J.B.;
RT "Candida albicans septin mutants are defective for invasive growth and
RT virulence.";
RL Infect. Immun. 71:4045-4051(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SEPTIN
RP COMPLEX.
RX PubMed=15449307; DOI=10.1002/yea.1147;
RA Kaneko A., Umeyama T., Hanaoka N., Monk B.C., Uehara Y., Niimi M.;
RT "Tandem affinity purification of the Candida albicans septin protein
RT complex.";
RL Yeast 21:1025-1033(2004).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16002645; DOI=10.1128/ec.4.7.1191-1202.2005;
RA Martin S.W., Douglas L.M., Konopka J.B.;
RT "Cell cycle dynamics and quorum sensing in Candida albicans chlamydospores
RT are distinct from budding and hyphal growth.";
RL Eukaryot. Cell 4:1191-1202(2005).
RN [9]
RP INTERACTION WITH HSL1.
RX PubMed=15659158; DOI=10.1111/j.1365-2958.2004.04405.x;
RA Umeyama T., Kaneko A., Nagai Y., Hanaoka N., Tanabe K., Takano Y.,
RA Niimi M., Uehara Y.;
RT "Candida albicans protein kinase CaHsl1p regulates cell elongation and
RT virulence.";
RL Mol. Microbiol. 55:381-395(2005).
RN [10]
RP PHOSPHORYLATION AT SER-4; SER-394 AND SER-395, MUTAGENESIS OF SER-394 AND
RP SER-395, ACETYLATION AT MET-1, AND FUNCTION.
RX PubMed=17765684; DOI=10.1016/j.devcel.2007.06.011;
RA Sinha I., Wang Y.M., Philp R., Li C.R., Yap W.H., Wang Y.;
RT "Cyclin-dependent kinases control septin phosphorylation in Candida
RT albicans hyphal development.";
RL Dev. Cell 13:421-432(2007).
RN [11]
RP FUNCTION.
RX PubMed=17504812; DOI=10.1242/jcs.002931;
RA Li C.R., Lee R.T., Wang Y.M., Zheng X.D., Wang Y.;
RT "Candida albicans hyphal morphogenesis occurs in Sec3p-independent and
RT Sec3p-dependent phases separated by septin ring formation.";
RL J. Cell Sci. 120:1898-1907(2007).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=19915075; DOI=10.1128/ec.00327-09;
RA Zhang C., Konopka J.B.;
RT "A photostable green fluorescent protein variant for analysis of protein
RT localization in Candida albicans.";
RL Eukaryot. Cell 9:224-226(2010).
RN [13]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=22687514; DOI=10.1128/aac.00112-12;
RA Badrane H., Nguyen M.H., Blankenship J.R., Cheng S., Hao B., Mitchell A.P.,
RA Clancy C.J.;
RT "Rapid redistribution of phosphatidylinositol-(4,5)-bisphosphate and
RT septins during the Candida albicans response to caspofungin.";
RL Antimicrob. Agents Chemother. 56:4614-4624(2012).
CC -!- FUNCTION: Septins are GTPases involved in cytokinesis that assemble
CC early in the cell cycle as a patch at the incipient bud site and form a
CC ring before bud emergence, which transforms into an hour-glass shaped
CC collar of cortical filaments that spans both sides of the mother-bud
CC neck. This collar persists until just before cytokinesis, when it
CC splits into two rings that occupy opposite sides of the neck. The
CC septins at the bud neck serve as a structural scaffold that recruits
CC different components involved in diverse processes at specific stages
CC during the cell cycle. Many proteins bind asymmetrically to the septin
CC collar. The septin assembly is regulated by protein kinase GIN4.
CC Septins are also involved in cell morphogenesis, chlamydospores
CC morphogenesis, bud site selection, chitin deposition, cell cycle
CC regulation, cell compartmentalization, and spore wall formation. CDC11
CC is required for the correct localization of SEC3 at bud tips and bud
CC necks. Plays a key role in invasive growth and virulence.
CC {ECO:0000269|PubMed:11454197, ECO:0000269|PubMed:12181342,
CC ECO:0000269|PubMed:12819094, ECO:0000269|PubMed:16002645,
CC ECO:0000269|PubMed:17504812, ECO:0000269|PubMed:17765684}.
CC -!- SUBUNIT: Component of the septin complex which consists of CDC3, CDC10,
CC CDC11, CDC12 and probably SEP7. The purified septin complex appeared to
CC have a stoichiometry of 2 CDC3, 1 to 2 CDC10, 1 CDC11, 2 CDC12, and 1
CC or none SEP7 subunit. Interacts with HSL1.
CC {ECO:0000269|PubMed:15449307, ECO:0000269|PubMed:15659158}.
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:11454197,
CC ECO:0000269|PubMed:12181342, ECO:0000269|PubMed:19915075,
CC ECO:0000269|PubMed:22687514}. Note=Localizes to a tight ring at the bud
CC and pseudohyphae necks and as a more diffuse array in emerging germ
CC tubes of hyphae.
CC -!- PTM: Hyphal induction causes immediate phosphorylation at Ser-395 by
CC GIN4 and at Ser-394 by CDC28-CCN1. GIN4 phosphorylation at Ser-395
CC primes CDC11 for further phosphorylation by CDC28-CCN1. CDC28-HGC1 then
CC maintains CDC11 phosphorylation throughout hyphal growth. Ser-4 is also
CC phosphorylated in yeast cells but not hyphal cells.
CC {ECO:0000269|PubMed:17765684}.
CC -!- PTM: Met-1 is acetylated. {ECO:0000269|PubMed:17765684}.
CC -!- DISRUPTION PHENOTYPE: Causes greater curvature of cells growing in a
CC filamentous manner and morphological defects in suspensor cells and
CC chlamydospores. Leads to reduced tissue penetration and non-invasive
CC fungal masses in mice infected kidneys. Leads also to
CC hypersusceptibility to caspofungin. {ECO:0000269|PubMed:12819094,
CC ECO:0000269|PubMed:16002645, ECO:0000269|PubMed:22687514}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
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DR EMBL; CP017627; AOW29453.1; -; Genomic_DNA.
DR RefSeq; XP_710520.1; XM_705428.1.
DR AlphaFoldDB; G1UB61; -.
DR SMR; G1UB61; -.
DR BioGRID; 1230981; 9.
DR STRING; 237561.G1UB61; -.
DR iPTMnet; G1UB61; -.
DR PRIDE; G1UB61; -.
DR GeneID; 3647888; -.
DR KEGG; cal:CAALFM_C500070WA; -.
DR CGD; CAL0000177264; CDC11.
DR VEuPathDB; FungiDB:C5_00070W_A; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_7_4_1; -.
DR InParanoid; G1UB61; -.
DR OMA; VENIMHD; -.
DR OrthoDB; 845354at2759; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0005619; C:ascospore wall; IEA:EnsemblFungi.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IDA:CGD.
DR GO; GO:0000144; C:cellular bud neck septin ring; IDA:CGD.
DR GO; GO:0000399; C:cellular bud neck septin structure; IDA:CGD.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:EnsemblFungi.
DR GO; GO:1990317; C:Gin4 complex; IEA:EnsemblFungi.
DR GO; GO:0032168; C:hyphal septin ring; IDA:CGD.
DR GO; GO:0001411; C:hyphal tip; IDA:CGD.
DR GO; GO:0001400; C:mating projection base; IEA:EnsemblFungi.
DR GO; GO:0072687; C:meiotic spindle; IEA:EnsemblFungi.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; IEA:EnsemblFungi.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0032160; C:septin filament array; IEA:EnsemblFungi.
DR GO; GO:0005940; C:septin ring; IDA:CGD.
DR GO; GO:0005876; C:spindle microtubule; IEA:EnsemblFungi.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:EnsemblFungi.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IBA:GO_Central.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IBA:GO_Central.
DR GO; GO:0006033; P:chitin localization; IMP:CGD.
DR GO; GO:0001410; P:chlamydospore formation; IMP:CGD.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IBA:GO_Central.
DR GO; GO:0070783; P:growth of unicellular organism as a thread of attached cells; IMP:CGD.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR GO; GO:0030011; P:maintenance of cell polarity; IMP:CGD.
DR GO; GO:0007097; P:nuclear migration; IMP:CGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:EnsemblFungi.
DR GO; GO:0008104; P:protein localization; IMP:CGD.
DR GO; GO:0097271; P:protein localization to bud neck; IBA:GO_Central.
DR GO; GO:0000921; P:septin ring assembly; IMP:CGD.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Coiled coil; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Virulence.
FT CHAIN 1..402
FT /note="Septin CDC11"
FT /id="PRO_0000424349"
FT DOMAIN 21..307
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 31..38
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 89..92
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 171..174
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT COILED 318..376
FT /evidence="ECO:0000255"
FT MOTIF 14..21
FT /note="Basic motif"
FT /evidence="ECO:0000250"
FT BINDING 31..38
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 172..180
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:17765684"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17765684"
FT MOD_RES 394
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:17765684"
FT MOD_RES 395
FT /note="Phosphoserine; by GIN4"
FT /evidence="ECO:0000269|PubMed:17765684"
FT MUTAGEN 394
FT /note="S->A: Blocks phosphorylation of Ser-394 and impairs
FT hyphal morphogenesis."
FT /evidence="ECO:0000269|PubMed:17765684"
FT MUTAGEN 395
FT /note="S->A: Blocks phosphorylation of Ser-394 and Ser-395
FT and impairs hyphal morphogenesis."
FT /evidence="ECO:0000269|PubMed:17765684"
SQ 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
