Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Septin-7

Gene

Sept7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891GTPBy similarity
Binding sitei115 – 1151GTP; via amide nitrogenBy similarity
Binding sitei249 – 2491GTP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei264 – 2641GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi56 – 638GTPBy similarity
Nucleotide bindingi194 – 2029GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-7
Alternative name(s):
CDC10 protein homolog
Gene namesi
Name:Sept7
Synonyms:Cdc10
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620469. Sept7.

Subcellular locationi

GO - Cellular componenti

  • axoneme Source: UniProtKB
  • cleavage furrow Source: UniProtKB-SubCell
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • membrane Source: RGD
  • midbody Source: UniProtKB-SubCell
  • septin complex Source: InterPro
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Centromere, Chromosome, Cilium, Cytoplasm, Cytoskeleton, Kinetochore

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 436435Septin-7PRO_0000173532Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei29 – 291PhosphotyrosineBy similarity
Modified residuei333 – 3331PhosphoserineBy similarity
Modified residuei372 – 3721N6-acetyllysineBy similarity
Modified residuei423 – 4231PhosphoserineBy similarity
Modified residuei425 – 4251PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9WVC0.
PRIDEiQ9WVC0.

PTM databases

PhosphoSiteiQ9WVC0.

Expressioni

Gene expression databases

GenevisibleiQ9WVC0. RN.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi249132. 3 interactions.
IntActiQ9WVC0. 3 interactions.
MINTiMINT-4569549.
STRINGi10116.ENSRNOP00000008839.

Structurei

3D structure databases

ProteinModelPortaliQ9WVC0.
SMRiQ9WVC0. Positions 33-314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 315270Septin-type GAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili331 – 436106Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5019.
HOVERGENiHBG065093.
InParanoidiQ9WVC0.
PhylomeDBiQ9WVC0.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008115. Septin7.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 1 hit.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
PIRSFiPIRSF006698. Septin. 1 hit.
PRINTSiPR01742. SEPTIN7.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WVC0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVSARSAAA EERSVNCSTM AQPKNLEGYV GFANLPNQVY RKSVKRGFEF
60 70 80 90 100
TLMVVGESGL GKSTLINSLF LTDLYSPEYP GPSHRIKKTV QVEQSKVLIK
110 120 130 140 150
EGGVQLLLTI VDTPGFGDAV DNSNCWQPVI DYIDSKFEDY LNAESRVNRR
160 170 180 190 200
QMPDNRVQCC LYFIAPSGHG LKPLDIEFMK RLHEKVNIIP LIAKADTLTP
210 220 230 240 250
EECQQFKKQI MKEIQGHKIK IYEFPETDDE EENKLVKKIK DRLPLAVVGS
260 270 280 290 300
NTIIEVNGKR VRGRQYPWGV AEVENGEHCD FTILRNMLIR THMQDLKDVT
310 320 330 340 350
NNVHYENYRS RKLAAVTYNG VDNNKNKGQL TKSPLAQMEE ERREHVAKMK
360 370 380 390 400
KMEMEMEQVF EMKVKEKVQK LKDSEAELQR RHEQMKKNLE AQHKELEEKR
410 420 430
RQFEEEKANW EAQQRILEQQ NSSRTLEKNK KKGKIF
Length:436
Mass (Da):50,508
Last modified:November 1, 1999 - v1
Checksum:i666DC3C1F0880404
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF142759 mRNA. Translation: AAD37861.1.
RefSeqiNP_072138.2. NM_022616.2.
UniGeneiRn.48701.

Genome annotation databases

GeneIDi64551.
UCSCiRGD:620469. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF142759 mRNA. Translation: AAD37861.1.
RefSeqiNP_072138.2. NM_022616.2.
UniGeneiRn.48701.

3D structure databases

ProteinModelPortaliQ9WVC0.
SMRiQ9WVC0. Positions 33-314.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249132. 3 interactions.
IntActiQ9WVC0. 3 interactions.
MINTiMINT-4569549.
STRINGi10116.ENSRNOP00000008839.

PTM databases

PhosphoSiteiQ9WVC0.

Proteomic databases

PaxDbiQ9WVC0.
PRIDEiQ9WVC0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64551.
UCSCiRGD:620469. rat.

Organism-specific databases

CTDi989.
RGDi620469. Sept7.

Phylogenomic databases

eggNOGiCOG5019.
HOVERGENiHBG065093.
InParanoidiQ9WVC0.
PhylomeDBiQ9WVC0.

Miscellaneous databases

NextBioi613444.
PROiQ9WVC0.

Gene expression databases

GenevisibleiQ9WVC0. RN.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008115. Septin7.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 1 hit.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
PIRSFiPIRSF006698. Septin. 1 hit.
PRINTSiPR01742. SEPTIN7.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiSEPT7_RAT
AccessioniPrimary (citable) accession number: Q9WVC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: July 22, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Coordinated expression with SEPT2 and SEPT6.By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.