Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cell division control protein 10

Gene

CDC10

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 approximate 15 minutes 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 kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation.

Miscellaneous

Present with 14100 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei74GTPBy similarity1
Binding sitei100GTP; via amide nitrogenBy similarity1
Binding sitei236GTP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei251GTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi39 – 46GTPBy similarity8
Nucleotide bindingi180 – 188GTPBy similarity9

GO - Molecular functioni

  • 1-phosphatidylinositol binding Source: SGD
  • GTPase activity Source: SGD
  • GTP binding Source: UniProtKB-KW
  • phosphatidylinositol-4-phosphate binding Source: SGD
  • phosphatidylinositol-5-phosphate binding Source: SGD
  • protein-containing complex scaffold activity Source: SGD
  • structural molecule activity Source: SGD

GO - Biological processi

  • exit from mitosis Source: SGD
  • maintenance of cell polarity Source: SGD
  • mitotic cytokinesis Source: SGD
  • septin ring assembly Source: SGD
  • sporulation Source: SGD

Keywordsi

Biological processCell cycle, Cell division
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29321-MONOMER
ReactomeiR-SCE-5687128 MAPK6/MAPK4 signaling

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division control protein 10
Gene namesi
Name:CDC10
Ordered Locus Names:YCR002C
ORF Names:YCR022, YCR2C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCR002C
SGDiS000000595 CDC10

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001734981 – 322Cell division control protein 10Add BLAST322

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei216PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP25342
PaxDbiP25342
PRIDEiP25342

PTM databases

iPTMnetiP25342

Interactioni

Subunit structurei

Component of the septin complex which consists of CDC3, CDC10, CDC11, CDC12 and probably SHS1 and rearranges to a cortical collar of highly ordered filaments at the mother-bud-neck. A complex formed by CDC3, CDC10, CDC11 and CDC12 is capable of forming long filaments in vitro and the components seem to be present in a 2:2:2:2 arrangement in vivo. The filaments are proposed to be formed by the end-to-end polymerization of CDC3-CDC12-CDC11 complexes with CDC10 serving as a bridge to bundle the polymers into paired filaments. Component of the GIN4 complex composed of at least BNI5, CDC3, CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1. Self-associates. Interacts with SYP1.4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein-containing complex scaffold activity Source: SGD

Protein-protein interaction databases

BioGridi30980, 564 interactors
ComplexPortaliCPX-1675 Septin complex
CPX-1712 Gin4 complex
DIPiDIP-673N
IntActiP25342, 46 interactors
MINTiP25342
STRINGi4932.YCR002C

Structurei

3D structure databases

ProteinModelPortaliP25342
SMRiP25342
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 302Septin-type GPROSITE-ProRule annotationAdd BLAST274

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni39 – 46G1 motifPROSITE-ProRule annotation8
Regioni97 – 100G3 motifPROSITE-ProRule annotation4
Regioni179 – 182G4 motifPROSITE-ProRule annotation4

Sequence similaritiesi

Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00910000144020
HOGENOMiHOG000233586
InParanoidiP25342
KOiK16938
OMAiENHCEFV
OrthoDBiEOG092C3HL6

Family and domain databases

CDDicd01850 CDC_Septin, 1 hit
InterProiView protein in InterPro
IPR030379 G_SEPTIN_dom
IPR027417 P-loop_NTPase
IPR016491 Septin
PfamiView protein in Pfam
PF00735 Septin, 1 hit
PIRSFiPIRSF006698 Septin, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51719 G_SEPTIN, 1 hit

Sequencei

Sequence statusi: Complete.

P25342-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPLSSVQPA SYVGFDTITN QIEHRLLKKG FQFNIMVVGQ SGLGKSTLIN
60 70 80 90 100
TLFASHLIDS ATGDDISALP VTKTTEMKIS THTLVEDRVR LNINVIDTPG
110 120 130 140 150
FGDFIDNSKA WEPIVKYIKE QHSQYLRKEL TAQRERFITD TRVHAILYFL
160 170 180 190 200
QPNGKELSRL DVEALKRLTE IANVIPVIGK SDTLTLDERT EFRELIQNEF
210 220 230 240 250
EKYNFKIYPY DSEELTDEEL ELNRSVRSII PFAVVGSENE IEINGETFRG
260 270 280 290 300
RKTRWSAINV EDINQCDFVY LREFLIRTHL QDLIETTSYI HYEGFRARQL
310 320
IALKENANSR SSAHMSSNAI QR
Length:322
Mass (Da):37,025
Last modified:May 1, 1992 - v1
Checksum:i672467301D4D2697
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L16549 Genomic DNA Translation: AAB49377.1
S48552 Genomic DNA Translation: AAD13856.1
X59720 Genomic DNA Translation: CAA42339.1
BK006937 Genomic DNA Translation: DAA07481.1
PIRiS19441
RefSeqiNP_009928.1, NM_001178715.1

Genome annotation databases

EnsemblFungiiCAA42339; CAA42339; CAA42339
YCR002C; YCR002C; YCR002C
GeneIDi850358
KEGGisce:YCR002C

Similar proteinsi

Entry informationi

Entry nameiCDC10_YEAST
AccessioniPrimary (citable) accession number: P25342
Secondary accession number(s): D6VR12
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 20, 2018
This is version 186 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health