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Protein

Septin-2A

Gene

sept2-a

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium. Required for the progression through mitosis through regulation of chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation (By similarity). Probably plays a role in ciliogenesis and collective cell movements including convergent extension during gastrulation. In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Controls cell shape and not polarization of cells during convergent extension.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei77 – 771GTPBy similarity
Binding sitei103 – 1031GTP; via amide nitrogenBy similarity
Sitei155 – 1551Important for dimerizationBy similarity
Binding sitei240 – 2401GTP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei255 – 2551GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi43 – 508GTPBy similarity
Nucleotide bindingi182 – 1909GTPBy 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-2A
Alternative name(s):
Septin-A
Short name:
XlSeptA
Gene namesi
Name:sept2-a
Synonyms:septa
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-865354. sept2.

Subcellular locationi

GO - Cellular componenti

  • ciliary membrane Source: UniProtKB
  • cleavage furrow Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • midbody Source: UniProtKB-SubCell
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Septin-2APRO_0000363221Add
BLAST

Proteomic databases

PRIDEiQ9DE33.

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. Can form heterooligomers with other family members and form filaments. Interacts with wdpcp.2 Publications

Protein-protein interaction databases

BioGridi99538. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9DE33.
SMRiQ9DE33. Positions 35-305.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 305273Septin-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni259 – 26911Important for dimerizationBy similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG065093.
KOiK16942.

Family and domain databases

CDDicd01850. CDC_Septin. 1 hit.
Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008113. Septin2.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 1 hit.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
PIRSFiPIRSF006698. Septin. 1 hit.
PRINTSiPR01740. SEPTIN2.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DE33-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKQQAQFTN PETPGYVGFA NLPNQVHRKS VRKGFEFTLM VVGESGLGKS
60 70 80 90 100
TLINSLFLTD LYPERVVPGA ADKIERTVDI EASTVEIEER GVKLRLTVVD
110 120 130 140 150
TPGYGDAMNC VDCFKPIISY VDNQFERYLH DESGLNRRHI VDNRVHCCFY
160 170 180 190 200
FISPFGHGLK PLDVEFMKAL HNKVNIVPVI AKADTLTLRE RERLKRRVLD
210 220 230 240 250
EIEEHGIKIY QLPDAESDED EDFKEQTRLL KASIPFTVVG SNQLIEAKGK
260 270 280 290 300
KVRGRLYPWG VVEVENTEHN DFLKLRTMLI THMQDLQEVT QDLHYENFRS
310 320 330 340 350
ERLKKGVTSS KVEHVEVTKD QILQEKEAEL RRMQEMITRM QAQMQIQGQS

GDAQHL
Length:356
Mass (Da):40,928
Last modified:March 1, 2001 - v1
Checksum:i80693736E084A126
GO

Sequence cautioni

The sequence AAI26038 differs from that shown. Reason: Erroneous termination at position 25. Translated as Gln.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF212298 mRNA. Translation: AAG43543.1.
BC126037 mRNA. Translation: AAI26038.1. Different termination.
RefSeqiNP_001082061.1. NM_001088592.1.
UniGeneiXl.731.

Genome annotation databases

GeneIDi398203.
KEGGixla:398203.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF212298 mRNA. Translation: AAG43543.1.
BC126037 mRNA. Translation: AAI26038.1. Different termination.
RefSeqiNP_001082061.1. NM_001088592.1.
UniGeneiXl.731.

3D structure databases

ProteinModelPortaliQ9DE33.
SMRiQ9DE33. Positions 35-305.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi99538. 1 interaction.

Proteomic databases

PRIDEiQ9DE33.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi398203.
KEGGixla:398203.

Organism-specific databases

CTDi398203.
XenbaseiXB-GENE-865354. sept2.

Phylogenomic databases

HOVERGENiHBG065093.
KOiK16942.

Family and domain databases

CDDicd01850. CDC_Septin. 1 hit.
Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008113. Septin2.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 1 hit.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
PIRSFiPIRSF006698. Septin. 1 hit.
PRINTSiPR01740. SEPTIN2.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSEP2A_XENLA
AccessioniPrimary (citable) accession number: Q9DE33
Secondary accession number(s): A0JMX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: March 1, 2001
Last modified: September 7, 2016
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.