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O55131 (SEPT7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Septin-7
Alternative name(s):
CDC10 protein homolog
Gene names
Name:Sept7
Synonyms:Cdc10
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Chromosomecentromerekinetochore By similarity. Cytoplasmcytoskeletonspindle By similarity. Cleavage furrow By similarity. Midbody By similarity. Cytoplasmcytoskeletoncilium 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.6

Miscellaneous

Coordinated expression with SEPT2 and SEPT6 By similarity.

Sequence similarities

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

Contains 1 septin-type G (guanine nucleotide-binding) domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCell projection
Centromere
Chromosome
Cilium
Cytoplasm
Cytoskeleton
Kinetochore
   DomainCoiled coil
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcilium morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of embryonic cell shape

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon terminus

Inferred from direct assay PubMed 11064363. Source: MGI

axoneme

Inferred from sequence or structural similarity. Source: UniProtKB

cell cortex

Inferred from direct assay PubMed 11064363. Source: MGI

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: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

septin complex

Inferred from electronic annotation. Source: InterPro

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

stress fiber

Inferred from electronic annotation. Source: Ensembl

synapse

Inferred from direct assay Ref.4. Source: MGI

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.4. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 436435Septin-7
PRO_0000173529

Regions

Domain46 – 315270Septin-type G
Nucleotide binding56 – 638GTP By similarity
Nucleotide binding194 – 2029GTP By similarity
Coiled coil331 – 436106 Potential

Sites

Binding site891GTP By similarity
Binding site1151GTP; via amide nitrogen By similarity
Binding site2491GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding site2641GTP By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue291Phosphotyrosine Ref.8
Modified residue3331Phosphoserine By similarity
Modified residue3721N6-acetyllysine Ref.9
Modified residue4231Phosphoserine By similarity
Modified residue4251Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
O55131 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 1028CCF14023059C

FASTA43650,550
        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 

« Hide

References

« Hide '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, IDENTIFICATION BY 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]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"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.
[7]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[8]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[9]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ223782 expand/collapse EMBL AC list , AJ223783, AJ223784, AJ223785, AJ223786, AJ223787, AJ223788, AJ223789, AJ223790, AJ223791, AJ223792, AJ223793, AJ223794 Genomic DNA. Translation: CAA11547.1.
BC058587 mRNA. Translation: AAH58587.1.
RefSeqNP_001192296.1. NM_001205367.1.
UniGeneMm.270259.

3D structure databases

ProteinModelPortalO55131.
SMRO55131. Positions 48-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231619. 4 interactions.
IntActO55131. 5 interactions.
MINTMINT-1865824.

PTM databases

PhosphoSiteO55131.

Proteomic databases

MaxQBO55131.
PaxDbO55131.
PRIDEO55131.

Protocols and materials databases

DNASU235072.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID235072.
KEGGmmu:235072.

Organism-specific databases

CTD989.
MGIMGI:1335094. Sept7.

Phylogenomic databases

eggNOGCOG5019.
HOGENOMHOG000233586.
HOVERGENHBG065093.
KOK16944.
PhylomeDBO55131.

Gene expression databases

ArrayExpressO55131.
BgeeO55131.
CleanExMM_SEPT7.
GenevestigatorO55131.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008115. Septin7.
[Graphical view]
PANTHERPTHR18884. PTHR18884. 1 hit.
PfamPF00735. Septin. 1 hit.
[Graphical view]
PIRSFPIRSF006698. Septin. 1 hit.
PRINTSPR01742. SEPTIN7.
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS51719. G_SEPTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSEPT7. mouse.
NextBio382505.
PROO55131.
SOURCESearch...

Entry information

Entry nameSEPT7_MOUSE
AccessionPrimary (citable) accession number: O55131
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot