O55131 (SEPT7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Septin-7

Alternative name(s):
CDC10 protein homolog

Gene names

Name:	Sept7
Synonyms:	Cdc10

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements By similarity.
Subunit structure	Septins polymerize into heterooligomeric protein complexes that form filaments, and associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation. Filaments are assembled from asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7 that associate head-to-head to form a hexameric unit. Within the trimer, directly interacts with SEPT6, while interaction with SEPT2 seems indirect. In the absence of SEPT6, forms homodimers. Interacts directly with CENPE and links CENPE to septin filaments composed of SEPT2, SEPT6 and SEPT7. Interacts with SEPT5, SEPT8, SEPT9 and SEPT11 By similarity. Ref.4
Subcellular location	Cytoplasm. Chromosome › centromere › kinetochore By similarity. Cytoplasm › cytoskeleton › spindle By similarity. Cleavage furrow By similarity. Midbody By similarity. Cytoplasm › cytoskeleton › cilium axoneme By similarity. Note: Distributed throughout the cytoplasm in prometaphase cells. Associated with the spindle during metaphase. Associated with the central spindle and at the cleavage furrow in anaphase cells. Detected at the midbody in telophase By similarity. Associated with actin stress fibers By similarity. Ref.5
Miscellaneous	Coordinated expression with SEPT2 and SEPT6 By similarity.
Sequence similarities	Belongs to the septin family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cell projection Centromere Chromosome Cilium Cytoplasm Cytoskeleton Kinetochore
Domain	Coiled coil
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW cilium morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW protein heterooligomerization Inferred from electronic annotation. Source: Compara regulation of embryonic cell shape Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	axon terminus Inferred from direct assay PubMed 11064363. Source: MGI cell cortex Inferred from direct assay PubMed 11064363. Source: MGI cilium axoneme Inferred from sequence or structural similarity. Source: UniProtKB cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara septin complex Inferred from electronic annotation. Source: InterPro spindle Inferred from electronic annotation. Source: UniProtKB-SubCell stress fiber Inferred from electronic annotation. Source: Compara synapse Inferred from direct assay Ref.4. Source: MGI
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 436	436	Septin-7		PRO_0000173529
Regions
	Nucleotide binding	56 – 63	8	GTP By similarity
	Nucleotide binding	194 – 202	9	GTP By similarity
	Coiled coil	331 – 436	106	Potential
Sites
	Binding site	89	1	GTP By similarity
	Binding site	115	1	GTP; via amide nitrogen By similarity
	Binding site	249	1	GTP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	264	1	GTP By similarity
Amino acid modifications
	Modified residue	29	1	Phosphotyrosine Ref.6
	Modified residue	227	1	Phosphothreonine Ref.7
	Modified residue	333	1	Phosphoserine Ref.8
	Modified residue	423	1	Phosphoserine By similarity
	Modified residue	425	1	Phosphothreonine Ref.8 Ref.9

Sequences

	Sequence		Length	Mass (Da)
	O55131 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 1028CCF14023059C	FASTA	436	50,550
	10 20 30 40 50 60 MSVSARSAAA EERSVNCGTM AQPKNLEGYV GFANLPNQVY RKSVKRGFEF TLMVVGESGL 70 80 90 100 110 120 GKSTLINSLF LTDLYSPEYP GPSHRIKKTV QVEQSKVLIK EGGVQLLLTI VDTPGFGDAV 130 140 150 160 170 180 DNSNCWQPVI DYIDSKFEDY LNAESRVNRR QMPDNRVQCC LYFIAPSGHG LKPLDIEFMK 190 200 210 220 230 240 RLHEKVNIIP LIAKADTLTP EECQQFKKQI MKEIQEHKIK IYEFPETDDE EENKLVKKIK 250 260 270 280 290 300 DRLPLAVVGS NTIIEVNGKR VRGRQYPWGV AEVENGEHCD FTILRNMLIR THMQDLKDVT 310 320 330 340 350 360 NNVHYENYRS RKLAAVTYNG VDNNKNKGQL TKSPLAQMEE ERREHVAKMK KMEMEMEQVF 370 380 390 400 410 420 EMKVKEKVQK LKDSEAELQR RHEQMKKNLE AQHKELEEKR RQFEEEKANW EAQQRILEQQ 430 NSSRTLEKNK KKGKIF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of murine CDC10 cDNA, gene organization and expression analysis." Soulier S., Vilotte J.-L. Biochim. Biophys. Acta 1442:339-346(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: BALB/c.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Colon.
[3]	Lubec G., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 25-41; 63-95; 137-146; 186-207; 221-234; 298-309; 333-342 AND 416-424, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[4]	"The septin CDCrel-1 is dispensable for normal development and neurotransmitter release." Peng X.-R., Jia Z., Zhang Y., Ware J., Trimble W.S. Mol. Cell. Biol. 22:378-387(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SEPT2 AND SEPT5.
[5]	"SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are associated with altered interactions with SEPT4/SEPT11 and resistance to Rho/Rhotekin-signaling." Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K. Hum. Mutat. 28:1005-1013(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[6]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, MASS SPECTROMETRY. Tissue: Brain.
[7]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND THR-425, MASS SPECTROMETRY. Tissue: Brain cortex.
[9]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-425, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ223782 , AJ223783, AJ223784, AJ223785, AJ223786, AJ223787, AJ223788, AJ223789, AJ223790, AJ223791, AJ223792, AJ223793, AJ223794 Genomic DNA. Translation: CAA11547.1. BC058587 mRNA. Translation: AAH58587.1.
IPI	IPI00874440.
RefSeq	NP_001192296.1. NM_001205367.1.
UniGene	Mm.270259.
3D structure databases
ProteinModelPortal	O55131.
SMR	O55131. Positions 48-315.
ModBase	Search...
Protein-protein interaction databases
IntAct	O55131. 2 interactions.
PTM databases
PhosphoSite	O55131.
Proteomic databases
PaxDb	O55131.
PRIDE	O55131.
Protocols and materials databases
DNASU	235072.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	235072.
KEGG	mmu:235072.
Organism-specific databases
CTD	989.
MGI	MGI:1335094. Sept7.
Phylogenomic databases
eggNOG	COG5019.
HOGENOM	HOG000233586.
HOVERGEN	HBG065093.
OrthoDB	EOG4894MJ.
Gene expression databases
ArrayExpress	O55131.
Bgee	O55131.
CleanEx	MM_SEPT7.
Genevestigator	O55131.
GermOnline	ENSMUSG00000001833. Mus musculus.
Family and domain databases
InterPro	IPR000038. Cell_div_GTP-bd. IPR016491. Septin. IPR008115. Septin7. [Graphical view]
PANTHER	PTHR18884. PTHR18884. 1 hit.
Pfam	PF00735. Septin. 1 hit. [Graphical view]
PIRSF	PIRSF006698. Septin. 1 hit.
PRINTS	PR01742. SEPTIN7.
ProtoNet	Search...
Other
ChiTaRS	SEPT7. mouse.
NextBio	382505.
SOURCE	Search...

Entry information

Entry name

SEPT7_MOUSE

Accession

Primary (citable) accession number: O55131

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program