Septin-5 - Mus musculus (Mouse)

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Q9Z2Q6 (SEPT5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Septin-5

Alternative name(s):
Cell division control-related protein 1
Short name=CDCrel-1
Peanut-like protein 1

Gene names

Name:	Sept5
Synonyms:	Pnutl1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Filament-forming cytoskeletal GTPase By similarity. Involved in cytokinesis Potential. May play a role in platelet secretion. Ref.7
Subunit structure	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 By similarity. Interacts with SEPT2 and SEPT5. Interaction with SEPT4 not detected. In platelets, associated with a complex containing STX4 By similarity. Interacts with PARK2. This interaction leads to SEPT5 ubiquitination and degradation. Ref.5 Ref.6
Subcellular location	Cytoplasm By similarity. Cytoplasm › cytoskeleton By similarity.
Developmental stage	Detected at 17 dpc in the brain. Expression increases during postnatal life and reaches a plateau at approximately P10 (at protein level). Ref.6
Disruption phenotype	Mice have a normal life-span and show no apparent abnormalities, including synaptic properties and hippocampal neuron growth. In platelets, hyperresponsive degranulation phenotype. Ref.6 Ref.7
Sequence similarities	Belongs to the septin family.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm Cytoskeleton
Domain	Coiled coil
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW regulation of exocytosis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cell cortex Inferred from direct assay PubMed 11064363. Source: MGI plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB septin complex Inferred from electronic annotation. Source: InterPro synaptic vesicle Inferred from sequence or structural similarity. Source: UniProtKB terminal bouton Inferred from direct assay PubMed 11064363. Source: MGI
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PARK2	O60260	2	EBI-772125,EBI-716346	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 369

369

Septin-5

PRO_0000173523

Regions

Nucleotide binding

51 – 58

GTP By similarity

Nucleotide binding

190 – 198

GTP By similarity

Coiled coil

338 – 369

Potential

Sites

Binding site

GTP By similarity

Binding site

111

GTP; via amide nitrogen By similarity

Binding site

248

GTP; via amide nitrogen and carbonyl oxygen By similarity

Binding site

263

GTP By similarity

Amino acid modifications

Modified residue

225

Phosphoserine Ref.10

Modified residue

327

Phosphoserine Ref.8 Ref.9

Modified residue

336

Phosphothreonine Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

Q9Z2Q6 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: D58468DBA9ADE626
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FASTA

369

42,748

        10         20         30         40         50         60 
MSTGLRYKSK LATPEDKQDI DKQYVGFATL PNQVHRKSVK KGFDFTLMVA GESGLGKSTL 

        70         80         90        100        110        120 
VHSLFLTDLY KDRKLLSAEE RINQTVEILK HTVDIEEKGV KLKLTIVDTP GFGDAVNNSE 

       130        140        150        160        170        180 
CWKPITDYVD QQFEQYFRDE SGLNRKNIQD NRVHCCLYFI SPFGHGLRPV DVGFMKALHE 

       190        200        210        220        230        240 
KVNIVPLIAK ADCLVPSEIR KLKDRIREEI DKFGIHVYQF PECDSDEDED FKQQDRELKE 

       250        260        270        280        290        300 
SAPFAVIGSN TVVEAKGQRV RGRLYPWGIV EVENQAHCDF VKLRNMLIRT HMHDLKDVTC 

       310        320        330        340        350        360 
DVHYENYRAH CIQQMTSKLT QDSRMESPIP ILPLPTPDAE TEKLIRMKDE ELRRMQEMLQ 


KMKQQMQDQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Medulla oblongata.
[2]	"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]. Strain: C57BL/6. Tissue: Brain.
[3]	"CDCREL-1, a septin deleted in DiGeorge Syndrome, is expressed in the developing brain and cartilage primordia in mouse embryogenesis." Botta A., Lindsay E.A., Jurecic V., Zieger B., Ware J., Baldini A. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-369. Strain: C57BL/6. Tissue: Brain, Cartilage and Skin.
[4]	Lubec G., Klug S., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 23-36; 58-71; 82-90; 182-190; 240-256; 264-282 AND 297-308, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[5]	"Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1." Zhang Y., Gao J., Chung K.K.K., Huang H., Dawson V.L., Dawson T.M. Proc. Natl. Acad. Sci. U.S.A. 97:13354-13359(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PARK2, UBIQUITIN-MEDIATED DEGRADATION.
[6]	"The septin CDCrel-1 is dispensable for normal development and neurotransmitter release." Peng X.-R., Jia Z., Zhang Y., Ware J., Trimble W.S. Mol. Cell. Biol. 22:378-387(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SEPT2 AND SEPT7, LACK OF INTERACTION WITH SEPT4, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[7]	"A prototypic platelet septin and its participation in secretion." Dent J., Kato K., Peng X.-R., Martinez C., Cattaneo M., Poujol C., Nurden P., Nurden A., Trimble W.S., Ware J. Proc. Natl. Acad. Sci. U.S.A. 99:3064-3069(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[8]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND THR-336, MASS SPECTROMETRY. Tissue: Embryonic brain.
[9]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, MASS SPECTROMETRY. Tissue: Brain cortex.
[10]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK134700 mRNA. Translation: BAE22248.1. BC059848 mRNA. Translation: AAH59848.1. BC141073 mRNA. Translation: AAI41074.1. BC145331 mRNA. Translation: AAI45332.1. AF033350 mRNA. Translation: AAC83974.1.
IPI	IPI00923056.
RefSeq	NP_998779.2. NM_213614.2.
UniGene	Mm.20365.
3D structure databases
ProteinModelPortal	Q9Z2Q6.
SMR	Q9Z2Q6. Positions 41-309.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Z2Q6. 4 interactions.
STRING	10090.ENSMUSP00000094750.
PTM databases
PhosphoSite	Q9Z2Q6.
Proteomic databases
PaxDb	Q9Z2Q6.
PRIDE	Q9Z2Q6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000096987; ENSMUSP00000094750; ENSMUSG00000072214.
GeneID	18951.
KEGG	mmu:18951.
UCSC	uc007yoj.1. mouse.
Organism-specific databases
CTD	5413.
MGI	MGI:1195461. Sept5.
Phylogenomic databases
eggNOG	COG5019.
GeneTree	ENSGT00620000087649.
HOVERGEN	HBG065093.
InParanoid	B2RUC5.
KO	K04557.
OMA	AVNNSEC.
OrthoDB	EOG447FTF.
Gene expression databases
ArrayExpress	Q9Z2Q6.
Bgee	Q9Z2Q6.
CleanEx	MM_SEPT5.
Genevestigator	Q9Z2Q6.
GermOnline	ENSMUSG00000072214. Mus musculus.
Family and domain databases
InterPro	IPR000038. Cell_div_GTP-bd. IPR016491. Septin. [Graphical view]
PANTHER	PTHR18884. PTHR18884. 1 hit.
Pfam	PF00735. Septin. 1 hit. [Graphical view]
PIRSF	PIRSF006698. Septin. 1 hit.
ProtoNet	Search...
Other
NextBio	295300.
SOURCE	Search...

Entry information

Entry name

SEPT5_MOUSE

Accession

Primary (citable) accession number: Q9Z2Q6
Secondary accession number(s): B2RUC5, Q3UYG4, Q6PB74

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 6, 2005
Last modified:	April 3, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents