Cell division control protein 3 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P32457 (CDC3_YEAST)

Last modified November 24, 2009. Version 93. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Cell division control protein 3

Gene names

Name:	CDC3
Ordered Locus Names:	YLR314C
ORF Names:	L8543.7

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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 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 assymetrically 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.
Subunit structure	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. Ref.5 Ref.8
Subcellular location	Membrane; Peripheral membrane protein. Bud neck. Note: Present at the bud neck during cell division. Probably interacts with phosphoinosides such as phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate.
Post-translational modification	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. Ref.6 Ref.12 Ref.13 Ref.14 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. Ref.5 Ref.4 Ref.10 Ref.11
Sequence similarities	Belongs to the septin family.

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Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Membrane
Domain	Coiled coil
Ligand	GTP-binding Nucleotide-binding
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	axial cellular bud site selection Traceable author statement. Source: SGD cell wall organization Traceable author statement. Source: SGD
Cellular component	ascospore wall Traceable author statement. Source: SGD cellular bud neck septin ring Traceable author statement. Source: SGD extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mating projection base Inferred from direct assay. Source: SGD prospore membrane Traceable author statement. Source: SGD septin complex Ref.3 Inferred from direct assay. Source: SGD
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol binding Ref.8 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct structural constituent of cytoskeleton Traceable author statement. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
GIC1	P38785	2	EBI-4429,EBI-7575
GIC2	Q06648	2	EBI-4429,EBI-7585

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 520

520

Cell division control protein 3

PRO_0000173496

Regions

Nucleotide binding

126 – 133

GTP By similarity

Nucleotide binding

289 – 295

GTP By similarity

Coiled coil

427 – 508

Potential

Sites

Binding site

344

GTP; via amide nitrogen and carbonyl oxygen By similarity

Binding site

362

GTP By similarity

Site

415

Not sumoylated

Site

443

Not sumoylated

Amino acid modifications

Modified residue

Phosphoserine Ref.12 Ref.13 Ref.14

Modified residue

Phosphothreonine Ref.13

Modified residue

Phosphoserine Ref.14

Modified residue

Phosphoserine Ref.14

Modified residue

175

Phosphoserine Ref.13 Ref.14

Modified residue

468

Phosphothreonine Ref.14

Modified residue

509

Phosphoserine Ref.14

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.4

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.4

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.4

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.4 Ref.10 Ref.11

Cross-link

287

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.4

Experimental info

Mutagenesis

K → R: Abolishes sumoylation. Ref.4

Mutagenesis

K → R: Abolishes sumoylation. Ref.4

Mutagenesis

287

K → R: Abolishes sumoylation. Ref.4

Mutagenesis

415

K → R: No effect on sumoylation. Ref.4

Mutagenesis

443

K → R: No effect on sumoylation. Ref.4

Sequence conflict

431

L → Q in AAB50034. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P32457-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: DCD18190C76742E8
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FASTA

520

60,039

        10         20         30         40         50         60 
MSLKEEQVSI KQDPEQEERQ HDQFNDVQIK QESQDHDGVD SQYTNGTQND DSERFEAAES 

        70         80         90        100        110        120 
DVKVEPGLGM GITSSQSEKG QVLPDQPEIK FIRRQINGYV GFANLPKQWH RRSIKNGFSF 

       130        140        150        160        170        180 
NLLCVGPDGI GKTTLMKTLF NNDDIEANLV KDYEEELAND QEEEEGQGEG HENQSQEQRH 

       190        200        210        220        230        240 
KVKIKSYESV IEENGVKLNL NVIDTEGFGD FLNNDQKSWD PIIKEIDSRF DQYLDAENKI 

       250        260        270        280        290        300 
NRHSINDKRI HACLYFIEPT GHYLKPLDLK FMQSVYEKCN LIPVIAKSDI LTDEEILSFK 

       310        320        330        340        350        360 
KTIMNQLIQS NIELFKPPIY SNDDAENSHL SERLFSSLPY AVIGSNDIVE NYSGNQVRGR 

       370        380        390        400        410        420 
SYPWGVIEVD NDNHSDFNLL KNLLIKQFME ELKERTSKIL YENYRSSKLA KLGIKQDNSV 

       430        440        450        460        470        480 
FKEFDPISKQ LEEKTLHEAK LAKLEIEMKT VFQQKVSEKE KKLQKSETEL FARHKEMKEK 

       490        500        510        520 
LTKQLKALED KKKQLELSIN SASPNVNHSP VPTKKKGFLR

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Haarer B.K., Ketcham S., Ford S., Ashcroft D., Pringle J.R. Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204510 / AB320.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function." Frazier J.A., Wong M.L., Longtine M.S., Pringle J.R., Mann M., Mitchison T.J., Field C. J. Cell Biol. 143:737-749(1998) [PubMed: 9813094] [Abstract] Cited for: IDENTIFICATION IN THE SEPTIN COMPLEX.
[4]	"Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins." Johnson E.S., Blobel G. J. Cell Biol. 147:981-994(1999) [PubMed: 10579719] [Abstract] Cited for: SUMOYLATION AT LYS-4; LYS-11; LYS-30; LYS-63 AND LYS-287, MUTAGENESIS OF LYS-4; LYS-11; LYS-287; LYS-415 AND LYS-443, MASS SPECTROMETRY.
[5]	"A novel factor required for the SUMO1/Smt3 conjugation of yeast septins." Takahashi Y., Toh-e A., Kikuchi Y. Gene 275:223-231(2001) [PubMed: 11587849] [Abstract] Cited for: SUMOYLATION, INTERACTION WITH SIZ1.
[6]	"Phosphorylation of the septin cdc3 in G1 by the cdc28 kinase is essential for efficient septin ring disassembly." Tang C.S., Reed S.I. Cell Cycle 1:42-49(2002) [PubMed: 12429908] [Abstract] Cited for: PHOSPHORYLATION BY CDC28.
[7]	"Cell cycle-dependent assembly of a Gin4-septin complex." Mortensen E.M., McDonald H., Yates J. III, Kellogg D.R. Mol. Biol. Cell 13:2091-2105(2002) [PubMed: 12058072] [Abstract] Cited for: MASS SPECTROMETRY, IDENTIFICATION IN THE GIN4 COMPLEX.
[8]	"Molecular dissection of a yeast septin: distinct domains are required for septin interaction, localization, and function." Casamayor A., Snyder M. Mol. Cell. Biol. 23:2762-2777(2003) [PubMed: 12665577] [Abstract] Cited for: ASSOCIATION WITH PHOSPHOINOSIDES LIPIDS, INTERACTION WITH CDC11.
[9]	"Protein-protein interactions governing septin heteropentamer assembly and septin filament organization in Saccharomyces cerevisiae." Versele M., Gullbrand B., Shulewitz M.J., Cid V.J., Bahmanyar S., Chen R.E., Barth P., Alber T., Thorner J. Mol. Biol. Cell 15:4568-4583(2004) [PubMed: 15282341] [Abstract] Cited for: SELF-ASSOCIATION, ASSEMBLY OF THE SEPTIN FILAMENTS.
[10]	"Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses." Zhou W., Ryan J.J., Zhou H. J. Biol. Chem. 279:32262-32268(2004) [PubMed: 15166219] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-63, MASS SPECTROMETRY.
[11]	"A proteomic strategy for gaining insights into protein sumoylation in yeast." Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D., Gygi S.P. Mol. Cell. Proteomics 4:246-254(2005) [PubMed: 15542864] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-63, MASS SPECTROMETRY.
[12]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY.
[13]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; THR-73 AND SER-175, MASS SPECTROMETRY.
[14]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-75; SER-77; SER-175; THR-468 AND SER-509, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	L16548 Genomic DNA. Translation: AAB50034.1. U20618 Genomic DNA. Translation: AAB64515.1.
PIR	S53393.
RefSeq	NP_013418.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:3010N.
IntAct	P32457. 19 interactions.
STRING	P32457.
Proteomic databases
PeptideAtlas	P32457.
PRIDE	P32457.
Genome annotation databases
Ensembl	YLR314C; YLR314C; YLR314C; Saccharomyces cerevisiae. [Genome view]
GeneID	851024.
KEGG	sce:YLR314C.
NMPDR	fig\|4932.3.peg.4438.
Organism-specific databases
CYGD	YLR314c.
SGD	S000004306. CDC3.
Phylogenomic databases
HOGENOM	P32457.
OMA	INSMFLS
OrthoDB	EOG9F7Q2J
Gene expression databases
ArrayExpress	P32457.
Genevestigator	P32457.
GermOnline	YLR314C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000038. Cell_Div_GTP_bd. IPR016491. Septin. [Graphical view]
PANTHER	PTHR18884. Cell_Div_GTP_bd. 1 hit.
Pfam	PF00735. Septin. 1 hit. [Graphical view]
PIRSF	PIRSF006698. Septin. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	967601.

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Entry information

Entry name

CDC3_YEAST

Accession

Primary (citable) accession number: P32457
Secondary accession number(s): Q06161

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	November 1, 1997
Last modified:	November 24, 2009
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents