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Q9WVC0 (SEPT7_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.3

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. According to Ref.3, also found in the nucleus. Ref.3

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 436435Septin-7
PRO_0000173532

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 By similarity
Modified residue3331Phosphoserine By similarity
Modified residue3721N6-acetyllysine By similarity
Modified residue4231Phosphoserine By similarity
Modified residue4251Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9WVC0 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 666DC3C1F0880404

FASTA43650,508
        10         20         30         40         50         60 
MSVSARSAAA EERSVNCSTM 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 MKEIQGHKIK 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

[1]"Identification of postsynaptic density proteins by MALDI-TOF mass spectrometry (Abstract #713.1)."
Walikonis R.S., Jensen O., Mann M., Kennedy M.B.
Abstr. - Soc. Neurosci. 24:1801-1801(1998)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
[2]Lubec G., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 137-146 AND 186-194, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain.
[3]"Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11."
Nagata K., Asano T., Nozawa Y., Inagaki M.
J. Biol. Chem. 279:55895-55904(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SEPT2; SEPT7; SEPT8; SEPT9 AND SEPT11.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF142759 mRNA. Translation: AAD37861.1.
RefSeqNP_072138.2. NM_022616.2.
UniGeneRn.48701.

3D structure databases

ProteinModelPortalQ9WVC0.
SMRQ9WVC0. Positions 33-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249132. 3 interactions.
IntActQ9WVC0. 3 interactions.
MINTMINT-4569549.

PTM databases

PhosphoSiteQ9WVC0.

Proteomic databases

PaxDbQ9WVC0.
PRIDEQ9WVC0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID64551.
KEGGrno:64551.
UCSCRGD:620469. rat.

Organism-specific databases

CTD989.
RGD620469. Sept7.

Phylogenomic databases

eggNOGCOG5019.
HOVERGENHBG065093.
InParanoidQ9WVC0.
KOK16944.
PhylomeDBQ9WVC0.

Gene expression databases

GenevestigatorQ9WVC0.

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

NextBio613444.
PROQ9WVC0.

Entry information

Entry nameSEPT7_RAT
AccessionPrimary (citable) accession number: Q9WVC0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 107 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