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-11

Gene

Sept11

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

Functioni

Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity.Curated1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031GTP; via amide nitrogenBy similarity
Binding sitei238 – 2381GTP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei253 – 2531GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 558GTPBy similarity
Nucleotide bindingi184 – 1929GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-11
Gene namesi
Name:Sept11
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi1307405. Sept11.

Subcellular locationi

  • Cytoplasmcytoskeleton
  • Cell junctionsynapse
  • Cell projectiondendritic spine
  • Cell projectionaxon

  • Note: Partly colocalizes with stress fibers. Association with microtubules not observed in embryonic fibroblasts. In cultured hippocampal neurons, localizes to 54% of GABAergic and 25% of glutamatergic synapses. Frequently present at the base of dendritic protrusions and at the bifurcation points of the dendritic branches. Expressed at low levels in the axons of mature cultured hippocampal neurons. In embryonic fibroblasts, associated with actin stress fibers.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 431430Septin-11PRO_0000385476Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiB3GNI6.
PRIDEiB3GNI6.

PTM databases

iPTMnetiB3GNI6.

Expressioni

Tissue specificityi

Highly expressed in cerebellum, olfactory bulb, hippocampus, cerebral cortex, thalamus, and corpus striatum. In the hippocampus, strong expression around the pyramidal cells of the stratum pyramidale and in the stratum lucidum of the CA2-CA3 regions. In the olfactory bulb, particularly strong expression in the external plexiform layer. In the cerebellum, concentrates in the molecular layer, particularly in Purkinje cells, where it is found at the base of dendritic spines/protrusions, at the dendritic branching points and in some GABAergic synapses.1 Publication

Developmental stagei

Expressed in the embryo and in early postnatal weeks. On and before P14, distributes in a homogeneous way, throughout the brain. By P21, high expression observed in the molecular layer of the cerebellum and in the olfactory bulb. The maximum expression and the adult pattern of distribution in the brain occurs by P30. By P30, P45 and P90, highest expression occurs in the molecular layer of the cerebellum and in the olfactory bulb, and relatively high expression in the hippocampus, cerebral cortex, thalamus and corpus striatum.1 Publication

Gene expression databases

ExpressionAtlasiB3GNI6. baseline and differential.
GenevisibleiB3GNI6. RN.

Interactioni

Subunit structurei

Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation. Interacts with SEPT7, SEPT9 and SEPT12. Forms homooligomers (By similarity).By similarity

Protein-protein interaction databases

BioGridi258101. 2 interactions.
IntActiB3GNI6. 1 interaction.
STRINGi10116.ENSRNOP00000062626.

Structurei

3D structure databases

ProteinModelPortaliB3GNI6.
SMRiB3GNI6. Positions 18-306.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 304267Septin-type GAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili320 – 40889Sequence analysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00760000118899.
HOGENOMiHOG000233586.
InParanoidiB3GNI6.
KOiK16939.
OMAiDKKNSPW.
OrthoDBiEOG7J9VQK.
PhylomeDBiB3GNI6.
TreeFamiTF101080.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: B3GNI6-1) [UniParc]FASTAAdd to basket

Also known as: III

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAVAVGRPSN EELRNLSLSG HVGFDSLPDQ LVNKSTSQGF CFNILCVGET
60 70 80 90 100
GIGKSTLMDT LFNTKFESDP ATHNEPGVRL KARSYELQES NVRLKLTIVD
110 120 130 140 150
TVGFGDQINK DDSYKPIVEY IDAQFEAYLQ EELKIKRSLF NYHDTRIHAC
160 170 180 190 200
LYFIAPTGHS LKSLDLVTMK KLDSKVNIIP IIAKADTIAK NELHKFKSKI
210 220 230 240 250
MSELVSNGVQ IYQFPTDEET VAEINATMSV HLPFAVVGST EEVKIGNKMA
260 270 280 290 300
KARQYPWGVV QVENENHCDF VKLREMLIRV NMEDLREQTH TRHYELYRRC
310 320 330 340 350
KLEEMGFKDT DPDSKPFSLQ ETYEAKRNEF LGELQKKEEE MRQMFVMRVK
360 370 380 390 400
EKEAELKEAE KELHEKFDLL KRTHQEEKKK VEDKKKELEE EVSNFQKKKA
410 420 430
AAQLLQSQAQ QSGAQQTKKD KDKKNPWLCT E
Length:431
Mass (Da):49,695
Last modified:July 22, 2008 - v1
Checksum:iCC838B791729B511
GO
Isoform 2 (identifier: B3GNI6-2) [UniParc]FASTAAdd to basket

Also known as: I, II

The sequence of this isoform differs from the canonical sequence as follows:
     425-425: N → NS

Show »
Length:432
Mass (Da):49,782
Checksum:i71162C92FD433B65
GO
Isoform 3 (identifier: B3GNI6-3) [UniParc]FASTAAdd to basket

Also known as: IV

The sequence of this isoform differs from the canonical sequence as follows:
     426-431: Missing.

Show »
Length:425
Mass (Da):48,965
Checksum:iA511DED8DD2E0767
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei425 – 4251N → NS in isoform 2. 1 PublicationVSP_038168
Alternative sequencei426 – 4316Missing in isoform 3. 1 PublicationVSP_038169

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU711414 mRNA. Translation: ACE00321.1.
EU711415 mRNA. Translation: ACE00322.1.
EU711416 mRNA. Translation: ACE00323.1.
EU711417 mRNA. Translation: ACE00324.1.
CH474060 Genomic DNA. Translation: EDL88655.1.
BC167769 mRNA. Translation: AAI67769.1.
RefSeqiNP_001100678.1. NM_001107208.2. [B3GNI6-2]
UniGeneiRn.27798.

Genome annotation databases

EnsembliENSRNOT00000067222; ENSRNOP00000062626; ENSRNOG00000002182. [B3GNI6-2]
GeneIDi305227.
KEGGirno:305227.
UCSCiRGD:1307405. rat. [B3GNI6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU711414 mRNA. Translation: ACE00321.1.
EU711415 mRNA. Translation: ACE00322.1.
EU711416 mRNA. Translation: ACE00323.1.
EU711417 mRNA. Translation: ACE00324.1.
CH474060 Genomic DNA. Translation: EDL88655.1.
BC167769 mRNA. Translation: AAI67769.1.
RefSeqiNP_001100678.1. NM_001107208.2. [B3GNI6-2]
UniGeneiRn.27798.

3D structure databases

ProteinModelPortaliB3GNI6.
SMRiB3GNI6. Positions 18-306.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi258101. 2 interactions.
IntActiB3GNI6. 1 interaction.
STRINGi10116.ENSRNOP00000062626.

PTM databases

iPTMnetiB3GNI6.

Proteomic databases

PaxDbiB3GNI6.
PRIDEiB3GNI6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000067222; ENSRNOP00000062626; ENSRNOG00000002182. [B3GNI6-2]
GeneIDi305227.
KEGGirno:305227.
UCSCiRGD:1307405. rat. [B3GNI6-1]

Organism-specific databases

CTDi55752.
RGDi1307405. Sept11.

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00760000118899.
HOGENOMiHOG000233586.
InParanoidiB3GNI6.
KOiK16939.
OMAiDKKNSPW.
OrthoDBiEOG7J9VQK.
PhylomeDBiB3GNI6.
TreeFamiTF101080.

Miscellaneous databases

PROiB3GNI6.

Gene expression databases

ExpressionAtlasiB3GNI6. baseline and differential.
GenevisibleiB3GNI6. RN.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Septin 11 is present in GABAergic synapses and plays a functional role in the cytoarchitecture of neurons and GABAergic synaptic connectivity."
    Li X., Serwanski D.R., Miralles C.P., Nagata K., De Blas A.L.
    J. Biol. Chem. 284:17253-17265(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Testis.
  4. Bienvenut W.V., von Kriegsheim A., Kolch W.
    Submitted (JUN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-14 AND 176-184, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fibroblast.
  5. "Biochemical and cell biological characterization of a mammalian septin, Sept11."
    Hanai N., Nagata K., Kawajiri A., Shiromizu T., Saitoh N., Hasegawa Y., Murakami S., Inagaki M.
    FEBS Lett. 568:83-88(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH STRESS FIBERS.
  6. "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: INTERACTION WITH SEPT7, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSEP11_RAT
AccessioniPrimary (citable) accession number: B3GNI6
Secondary accession number(s): B3DMA8, B3GNI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 22, 2008
Last modified: June 8, 2016
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.