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Protein

Cell division control protein 3

Gene

CDC3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei207GTP; via amide nitrogenBy similarity1
Binding sitei344GTP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei360GTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi126 – 133GTPBy similarity8
Nucleotide bindingi287 – 295GTPBy similarity9

GO - Molecular functioni

  • GTP binding Source: SGD
  • phosphatidylinositol-4-phosphate binding Source: SGD
  • phosphatidylinositol-5-phosphate binding Source: SGD
  • structural molecule activity Source: SGD

GO - Biological processi

  • maintenance of cell polarity Source: SGD
  • mitotic cytokinesis Source: SGD
  • septin ring assembly Source: SGD
  • septin ring disassembly Source: SGD

Keywordsi

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

Enzyme and pathway databases

BioCyciYEAST:G3O-32400-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division control protein 3
Gene namesi
Name:CDC3
Ordered Locus Names:YLR314C
ORF Names:L8543.7
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR314C.
SGDiS000004306. CDC3.

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4K → R: Abolishes sumoylation. 1 Publication1
Mutagenesisi11K → R: Abolishes sumoylation. 1 Publication1
Mutagenesisi287K → R: Abolishes sumoylation. 1 Publication1
Mutagenesisi415K → R: No effect on sumoylation. 1 Publication1
Mutagenesisi443K → R: No effect on sumoylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001734962 – 520Cell division control protein 3Add BLAST519

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Cross-linki4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei9PhosphoserineCombined sources1
Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei47PhosphothreonineCombined sources1
Modified residuei60PhosphoserineCombined sources1
Cross-linki63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)2 Publications
Modified residuei77PhosphoserineCombined sources1
Modified residuei175PhosphoserineCombined sources1
Cross-linki287Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei468PhosphothreonineCombined sources1
Modified residuei509PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by CDC28. Phosphorylation at the end of G1 may facilitate initiation of a new cell cycle by promoting disassembly of the obsolete septin ring from the previous cell cycle.1 Publication
Sumoylated during mitosis on the mother cell side of the bud neck by UBC9/SIZ1. Sumoylation probably plays a central role in regulating septin ring disassembly during the cell cycle.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei415Not sumoylated1
Sitei443Not sumoylated1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP32457.
PRIDEiP32457.

PTM databases

iPTMnetiP32457.

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 SIZ1 and SYP1.5 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi31579. 775 interactors.
DIPiDIP-3010N.
ELMiP32457.
IntActiP32457. 36 interactors.
MINTiMINT-440222.
STRINGi4932.YLR314C.

Structurei

3D structure databases

ProteinModelPortaliP32457.
SMRiP32457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini116 – 411Septin-type GAdd BLAST296

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili427 – 508Sequence analysisAdd BLAST82

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00900000140812.
HOGENOMiHOG000233586.
InParanoidiP32457.
KOiK16944.
OMAiFQFTAMV.
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. 2 hits.
PROSITEiView protein in PROSITE
PS51719. G_SEPTIN. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32457-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLKEEQVSI KQDPEQEERQ HDQFNDVQIK QESQDHDGVD SQYTNGTQND
60 70 80 90 100
DSERFEAAES DVKVEPGLGM GITSSQSEKG QVLPDQPEIK FIRRQINGYV
110 120 130 140 150
GFANLPKQWH RRSIKNGFSF NLLCVGPDGI GKTTLMKTLF NNDDIEANLV
160 170 180 190 200
KDYEEELAND QEEEEGQGEG HENQSQEQRH KVKIKSYESV IEENGVKLNL
210 220 230 240 250
NVIDTEGFGD FLNNDQKSWD PIIKEIDSRF DQYLDAENKI NRHSINDKRI
260 270 280 290 300
HACLYFIEPT GHYLKPLDLK FMQSVYEKCN LIPVIAKSDI LTDEEILSFK
310 320 330 340 350
KTIMNQLIQS NIELFKPPIY SNDDAENSHL SERLFSSLPY AVIGSNDIVE
360 370 380 390 400
NYSGNQVRGR SYPWGVIEVD NDNHSDFNLL KNLLIKQFME ELKERTSKIL
410 420 430 440 450
YENYRSSKLA KLGIKQDNSV FKEFDPISKQ QEEKTLHEAK LAKLEIEMKT
460 470 480 490 500
VFQQKVSEKE KKLQKSETEL FARHKEMKEK LTKQLKALED KKKQLELSIN
510 520
SASPNVNHSP VPTKKKGFLR
Length:520
Mass (Da):60,054
Last modified:September 21, 2011 - v3
Checksum:iDCCD4C8C16AA5E25
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti431Q → L in AAB64515 (PubMed:9169871).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L16548 Genomic DNA. Translation: AAB50034.1.
U20618 Genomic DNA. Translation: AAB64515.1.
BK006945 Genomic DNA. Translation: DAA09624.2.
PIRiS53393.
RefSeqiNP_013418.2. NM_001182203.2.

Genome annotation databases

EnsemblFungiiYLR314C; YLR314C; YLR314C.
GeneIDi851024.
KEGGisce:YLR314C.

Similar proteinsi

Entry informationi

Entry nameiCDC3_YEAST
AccessioniPrimary (citable) accession number: P32457
Secondary accession number(s): D6VYV8, Q06161
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: September 21, 2011
Last modified: October 25, 2017
This is version 170 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names