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Q9QZR6 (SEPT9_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Septin-9
Alternative name(s):
Eighth septin
Eseptin
Septin-like protein
Short name=SLP
Gene names
Name:Sept9
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length564 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Filament-forming cytoskeletal GTPase By similarity. May play a role in cytokinesis Potential.

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. Interacts with SEPT2, SEPT6, SEPT7, SEPT11 and SEPT14. Interacts with RTKN and ARHGEF18 By similarity. Ref.4 Ref.7

Subcellular location

Cytoplasm › cytoskeleton. Note: In embryonic fibroblasts, associated with actin stress fibers. No apparent co-distribution with microtubules, but some colocalization with vimentin filaments in the perinuclear region. Ref.2 Ref.4

Tissue specificity

Expressed in the brain, mainly in the perikarya and processes of astrocytes in the cerebellum, dentate gyrus and corpus callosum (at protein level). In the sciatic nerve, highly expressed in Schwann cells (at protein level). Isoforms are differentially expressed in testes, kidney, liver, heart, spleen and brain. Undetectable in skeletal muscle. Ref.1 Ref.2 Ref.6

Sequence similarities

Belongs to the septin family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9QZR6-1)

Also known as: SLP-a;

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.
Isoform 2 (identifier: Q9QZR6-2)

Also known as: SLP-b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-85: Missing.
Isoform 3 (identifier: Q9QZR6-3)

Also known as: E-septin long form;

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
Isoform 4 (identifier: Q9QZR6-4)

Also known as: E-septin short form;

The sequence of this isoform differs from the canonical sequence as follows:
     1-231: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 564564Septin-9
PRO_0000173537

Regions

Nucleotide binding285 – 2928GTP By similarity
Nucleotide binding425 – 4339GTP By similarity

Sites

Binding site3191GTP By similarity
Binding site3451GTP; via amide nitrogen By similarity
Binding site4801GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding site4951GTP By similarity

Amino acid modifications

Modified residue121Phosphoserine By similarity
Modified residue241Phosphothreonine By similarity
Modified residue311Phosphothreonine Ref.5
Modified residue641Phosphoserine By similarity
Modified residue671Phosphoserine By similarity
Modified residue1251Phosphothreonine By similarity
Modified residue1431Phosphoserine By similarity
Modified residue1501Phosphothreonine Ref.5
Modified residue2581Phosphotyrosine By similarity
Modified residue3071Phosphoserine By similarity

Natural variations

Alternative sequence1 – 231231Missing in isoform 4.
VSP_012343
Alternative sequence1 – 160160Missing in isoform 3.
VSP_012344
Alternative sequence1 – 8585Missing in isoform 2.
VSP_012345

Experimental info

Mutagenesis2881G → V: Abolishes the GTP binding. Ref.1
Sequence conflict2301V → G in AAF01206. Ref.1
Sequence conflict4601E → ED in AAF01206. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SLP-a) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: B45160157F986C0C

FASTA56463,792
        10         20         30         40         50         60 
MERDRITALK RSFEVEEIEP PNSTPPRRVQ TPLLRATVAS SSQKFQDLGV KNSEPAARLV 

        70         80         90        100        110        120 
DTLSQRSPKP SLRRVDLAGA KAPEPMSRRT ELSIDISSKQ VESTASTPGP SRFGLKRAEV 

       130        140        150        160        170        180 
LGHKTPEPVP RRTEITIVKP QESGLRRVET PASKAPEGSA MPVTDAAPKR VEIQVPKPAE 

       190        200        210        220        230        240 
APNCPLPPQT LENSEAPMSQ LQSRLEPRPP VTEVPYRNQE DSEVAPSCVV DMADNPRDAM 

       250        260        270        280        290        300 
LKQAPVSRNE KAPVDFGYVG IDSILEQMRR KAMKQGFEFN IMVVGQSGLG KSTLINTLFK 

       310        320        330        340        350        360 
SKISRKSVQP ISEERIPKTI EIKSITHDIE EKGVRMKLTV IDTPGFGDHI NNENCWQPIM 

       370        380        390        400        410        420 
KFINDQYEKY LQEEVNINRK KRIPDTRVHC CLYFIPATGH SLRPLDIEFM KRLSKVVNIV 

       430        440        450        460        470        480 
PVIAKADTLT LEERVYFKQR ITSDLLSNGI DVYPQKEFDE AEDRLVNEKF REMIPFAVVG 

       490        500        510        520        530        540 
SDHEYQVNGK RILGRKTKWG TIEVENTTHC EFAYLRDLLI RTHMQNIKDI TSNIHFEAYR 

       550        560 
VKRLNEGNSA MANGIEKEPE TQEM

« Hide

Isoform 2 (SLP-b) [UniParc].

Checksum: 60936B32230625BD
Show »

FASTA47954,389
Isoform 3 (E-septin long form) [UniParc].

Checksum: 7C81BC3E3F45859F
Show »

FASTA40446,282
Isoform 4 (E-septin short form) [UniParc].

Checksum: 02941CFB5584A557
Show »

FASTA33338,524

References

« Hide 'large scale' references
[1]"Identification of a novel alternatively spliced septin."
Fung E.T., Scheller R.H.
FEBS Lett. 451:203-208(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, ALTERNATIVE SPLICING, MUTAGENESIS OF GLY-288.
Tissue: Brain.
[2]"Alternative exon usage of rat septins."
Jackisch B.O., Hausser H., Schaefer L., Kappler J., Muller H.W., Kresse H.
Biochem. Biophys. Res. Commun. 275:180-188(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
Tissue: Mesangial cell.
[3]Lubec G., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 292-300, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain.
[4]"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 SEPT7.
[5]"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND THR-150, MASS SPECTROMETRY.
Tissue: Renal collecting duct.
[6]"SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are associated with altered interactions with SEPT4/SEPT11 and resistance to Rho/Rhotekin-signaling."
Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.
Hum. Mutat. 28:1005-1013(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Characterization of a SEPT9 interacting protein, SEPT14, a novel testis-specific septin."
Peterson E.A., Kalikin L.M., Steels J.D., Estey M.P., Trimble W.S., Petty E.M.
Mamm. Genome 18:796-807(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEPT14.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF180525 mRNA. Translation: AAF01206.1.
AF180526 mRNA. Translation: AAF01207.1.
AF170253 mRNA. Translation: AAF03376.1.
AF173899 mRNA. Translation: AAF03391.1.
IPIIPI00194218.
IPI00655333.
IPI00782707.
IPI00896129.
PIRJC7365.
RefSeqNP_001106969.1. NM_001113497.1.
NP_114025.2. NM_031837.2.
NP_789826.2. NM_176856.2.
UniGeneRn.91127.

3D structure databases

ProteinModelPortalQ9QZR6.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9QZR6. 4 interactions.
STRING10116.ENSRNOP00000010365.

PTM databases

PhosphoSiteQ9QZR6.

Proteomic databases

PaxDbQ9QZR6.
PRIDEQ9QZR6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID83788.
KEGGrno:83788.

Organism-specific databases

CTD10801.
RGD708523. Sept9.

Phylogenomic databases

eggNOGCOG5019.
HOGENOMHOG000233586.
HOVERGENHBG098529.
InParanoidQ9QZR6.
OrthoDBEOG4WDDBR.

Gene expression databases

ArrayExpressQ9QZR6.
GenevestigatorQ9QZR6.
GermOnlineENSRNOG00000002807. Rattus norvegicus.

Family and domain databases

InterProIPR000038. Cell_div_GTP-bd.
[Graphical view]
PANTHERPTHR18884. PTHR18884. 1 hit.
PfamPF00735. Septin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio616359.

Entry information

Entry nameSEPT9_RAT
AccessionPrimary (citable) accession number: Q9QZR6
Secondary accession number(s): Q9QZJ7, Q9QZJ8, Q9QZP9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: May 1, 2000
Last modified: April 3, 2013
This is version 85 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

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents