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Protein

Septin-2

Gene

Sept2

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

Functioni

Filament-forming cytoskeletal GTPase. Forms a filamentous structure with SEPT12, SEPT6, SEPT2 and probably SEPT4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (By similarity). Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements. 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: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein (By similarity).By similarity

Miscellaneous

Coordinated expression with SEPT2 and SEPT7.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei78GTPBy similarity1
Binding sitei104GTP; via amide nitrogenBy similarity1
Sitei156Important for dimerizationBy similarity1
Binding sitei241GTP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei256GTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi44 – 51GTPBy similarity8
Nucleotide bindingi183 – 191GTPBy similarity9

GO - Molecular functioni

  • cadherin binding Source: Ensembl
  • GTPase activity Source: RGD
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cilium assembly Source: UniProtKB
  • neuron projection development Source: RGD
  • smoothened signaling pathway Source: UniProtKB
  • spermatogenesis Source: UniProtKB-KW

Keywordsi

Biological processCell cycle, Cell division, Differentiation, Mitosis, Spermatogenesis
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-5620912. Anchoring of the basal body to the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-2
Alternative name(s):
Vascular endothelial cell specific protein 11
Gene namesi
Name:Sept2
Synonyms:Vesp11
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi620056. Sept2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002702081 – 361Septin-2Add BLAST361

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17PhosphotyrosineBy similarity1
Modified residuei190N6-acetyllysineBy similarity1
Modified residuei211PhosphotyrosineBy similarity1
Modified residuei218PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ91Y81.
PRIDEiQ91Y81.

2D gel databases

World-2DPAGEi0004:Q91Y81.

PTM databases

iPTMnetiQ91Y81.
PhosphoSitePlusiQ91Y81.

Expressioni

Gene expression databases

BgeeiENSRNOG00000017952.
GenevisibleiQ91Y81. RN.

Interactioni

Subunit structurei

Septins polymerize into heterooligomeric protein complexes that form filaments, and associate with cellular membranes, actin filaments and microtubules (By similarity). GTPase activity is required for filament formation (By similarity). Septin filaments are assembled from asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7 that associate head-to-head to form a hexameric unit (By similarity). Interaction between SEPT2 and SEPT7 seems indirect (PubMed:15485874). Interacts also with SEPT9 and SEPT5 (By similarity). Interaction with SEPT4 not detected (By similarity). Component of a septin core octomeric complex consisting of SEPT12, SEPT7, SEPT6 and SEPT2 or SEPT4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm annulus (By similarity). Interacts with MAP4 (By similarity). Interacts with DZIP1L (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi250737. 2 interactors.
IntActiQ91Y81. 3 interactors.
MINTiMINT-3381912.
STRINGi10116.ENSRNOP00000024261.

Structurei

3D structure databases

ProteinModelPortaliQ91Y81.
SMRiQ91Y81.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 306Septin-type GAdd BLAST273

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni260 – 270Important for dimerizationBy similarityAdd BLAST11

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00900000140812.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiQ91Y81.
KOiK16942.
OMAiQWEQHLI.
OrthoDBiEOG091G07TS.
PhylomeDBiQ91Y81.
TreeFamiTF101079.

Family and domain databases

CDDicd01850. CDC_Septin. 1 hit.
InterProiView protein in InterPro
IPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008113. Septin2.
PfamiView protein in Pfam
PF00735. Septin. 1 hit.
PIRSFiPIRSF006698. Septin. 1 hit.
PRINTSiPR01740. SEPTIN2.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiView protein in PROSITE
PS51719. G_SEPTIN. 1 hit.

Sequencei

Sequence statusi: Complete.

Q91Y81-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK
60 70 80 90 100
STLINSLFLT DLYPERIIPG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV
110 120 130 140 150
DTPGYGDAIN SRDCFKTIIS YIDEQFERYL HDESGLNRRH IIDNRVHCCF
160 170 180 190 200
YFISPFGHGL KPLDVAFMKA IHNKVNIVPV IAKADTLTLK ERERLKKRIL
210 220 230 240 250
DEIEEHSIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV GSNQLIEAKG
260 270 280 290 300
KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR
310 320 330 340 350
SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG
360
DTDSSTLGHH V
Length:361
Mass (Da):41,593
Last modified:December 1, 2001 - v1
Checksum:iC4B9335F18098641
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027561 mRNA. Translation: BAB47151.1.
BC081745 mRNA. Translation: AAH81745.1.
RefSeqiNP_476489.1. NM_057148.2.
XP_006245574.1. XM_006245512.3.
XP_006245576.1. XM_006245514.1.
UniGeneiRn.98570.

Genome annotation databases

EnsembliENSRNOT00000024261; ENSRNOP00000024261; ENSRNOG00000017952.
GeneIDi117515.
KEGGirno:117515.
UCSCiRGD:620056. rat.

Similar proteinsi

Entry informationi

Entry nameiSEPT2_RAT
AccessioniPrimary (citable) accession number: Q91Y81
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: December 1, 2001
Last modified: October 25, 2017
This is version 115 of the entry and version 1 of the sequence. See 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