LIPID MAPS

LMPD ID

LMP007085

Gene ID

850358

Species

Saccharomyces cerevisiae S288c (Yeast (S288c))

Gene Name

septin CDC10

Gene Symbol

CDC10

Synonyms

-

Chromosome

III

septin CDC10
Refseq ID	NP_009928
Protein GI	6319847
UniProt ID	P25342
mRNA ID	NM_001178715
Length	322
MDPLSSVQPASYVGFDTITNQIEHRLLKKGFQFNIMVVGQSGLGKSTLINTLFASHLIDSATGDDISALPVTKTTEMKISTHTLVEDRVRLNINVIDTPGFGDFIDNSKAWEPIVKYIKEQHSQYLRKELTAQRERFITDTRVHAILYFLQPNGKELSRLDVEALKRLTEIANVIPVIGKSDTLTLDERTEFRELIQNEFEKYNFKIYPYDSEELTDEELELNRSVRSIIPFAVVGSENEIEINGETFRGRKTRWSAINVEDINQCDFVYLREFLIRTHLQDLIETTSYIHYEGFRARQLIALKENANSRSSAHMSSNAIQR

Entrez Gene ID

850358

Gene Name

septin CDC10

Gene Symbol

CDC10

Species

Saccharomyces cerevisiae S288c

Gene Ontology (GO Annotations)

GO ID	Source	Type	Description
GO:0042764	IDA:SGD	C	ascospore-type prospore
GO:0000144	IDA:SGD	C	cellular bud neck septin ring
GO:0001400	IDA:SGD	C	mating projection base
GO:0072687	IDA:SGD	C	meiotic spindle
GO:0005628	IDA:SGD	C	prospore membrane
GO:0031105	IDA:SGD	C	septin complex
GO:0032160	IDA:SGD	C	septin filament array
GO:0005876	IDA:SGD	C	spindle microtubule
GO:0005545	IDA:SGD	F	1-phosphatidylinositol binding
GO:0005525	IEA:UniProtKB-KW	F	GTP binding
GO:0003924	IDA:SGD	F	GTPase activity
GO:0032947	IDA:SGD	F	protein complex scaffold
GO:0005198	IDA:SGD	F	structural molecule activity
GO:0006184	IDA:GOC	P	GTP catabolic process
GO:0010458	IMP:SGD	P	exit from mitosis
GO:0030011	IC:SGD	P	maintenance of cell polarity
GO:0000921	IMP:SGD	P	septin ring assembly
GO:0043934	IDA:SGD	P	sporulation

InterPro Annotations

Accession	Description
IPR000038	Cell_div_GTP-bd
IPR027417	P-loop containing nucleoside triphosphate hydrolase
IPR016491	Septin

Entry Information

Gene Name

septin CDC10

Protein Entry

CDC10_YEAST

UniProt ID

P25342

Species

Yeast (S288c)

Comments

Comment Type	Description
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 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.
Interaction	P47136:BUD4; NbExp=2; IntAct=EBI-4174, EBI-3848;
Miscellaneous	Present with 14100 molecules/cell in log phase SD medium
Miscellaneous	Present with 14100 molecules/cell in log phase SD medium. {ECO:0000269\|PubMed:14562106}.
Similarity	Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- like GTPase superfamily. Septin GTPase family
Similarity	Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- like GTPase superfamily. Septin GTPase family. {ECO:0000305}.
Similarity	Contains 1 septin-type G (guanine nucleotide-binding) domain
Similarity	Contains 1 septin-type G (guanine nucleotide-binding) domain. {ECO:0000305}.
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.
Subcellular Location	Membrane {ECO:0000269\|PubMed:14562095}; Peripheral membrane protein {ECO:0000269\|PubMed:14562095}. Bud neck {ECO:0000269\|PubMed:14562095}. Note=Present at the bud neck during cell division. Probably interacts with phosphoinosides such as phosphatidylinositol 4-phosphate or phosphatidylinositol 5- phosphate.
Subunit	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. {ECO:0000269\|PubMed:12058072, ECO:0000269\|PubMed:12665577, ECO:0000269\|PubMed:18791237, ECO:0000269\|PubMed:9813094}.