Q9R1T4 (SEPT6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Septin-6

Gene names

Name:	Sept6
Synonyms:	Kiaa0128

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis.
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. Filaments are assembled from asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7 that associate head-to-head to form a hexameric unit. Within the trimer, directly interacts with SEPT2 and SEPT7. Also interacts with SEPT9 and SEPT12. Interaction with SEPT12 alters filament structure. Interacts with SOCS7. Interacts with HNRNPA1 By similarity.
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton › spindle. Chromosome › centromere › kinetochore By similarity. Cleavage furrow By similarity. Midbody By similarity. Note: In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition to the kinetochores of the congressed chromosomes. In cells undergoing cytokinesis, localized to the midbody, the ingressing cleavage furrow, and the central spindle By similarity.
Tissue specificity	Associated with synaptic vesicles in various brain regions, including glomeruli of the olfactory bulb. Ref.7
Miscellaneous	Coordinated expression with SEPT2 and SEPT7 By similarity.
Sequence similarities	Belongs to the septin family.
Sequence caution	The sequence BAD32172.1 differs from that shown. Reason: Erroneous initiation. The sequence CAM19782.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation 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
Cellular_component	axon terminus Inferred from direct assay Ref.7. Source: MGI cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from electronic annotation. Source: UniProtKB-SubCell septin complex Inferred from electronic annotation. Source: InterPro spindle Inferred from electronic annotation. Source: UniProtKB-SubCell synaptic vesicle Inferred from direct assay Ref.7. Source: MGI
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform II (identifier: Q9R1T4-1)

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 I (identifier: Q9R1T4-2)

Also known as: III;

The sequence of this isoform differs from the canonical sequence as follows:
     428-434: Missing.

Isoform V (identifier: Q9R1T4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     428-434: NPWLCIE → FF

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 434	433	Septin-6		PRO_0000173526
Regions
	Nucleotide binding	49 – 56	8	GTP By similarity
	Nucleotide binding	185 – 193	9	GTP By similarity
	Coiled coil	321 – 407	87	Potential
Sites
	Binding site	104	1	GTP; via amide nitrogen By similarity
	Binding site	239	1	GTP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	254	1	GTP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	367	1	N6-acetyllysine By similarity
	Modified residue	416	1	Phosphoserine Ref.8
Natural variations
	Alternative sequence	428 – 434	7	Missing in isoform I.		VSP_006055
	Alternative sequence	428 – 434	7	NPWLCIE → FF in isoform V.		VSP_006056
Experimental info
	Sequence conflict	10	1	V → L in BAB28516. Ref.2
	Sequence conflict	10	1	Missing in BAC33342. Ref.2
	Sequence conflict	62	1	L → P in BAC40335. Ref.2
	Sequence conflict	141	1	H → Y in BAA82838. Ref.1
	Sequence conflict	170	1	M → I in BAE36069. Ref.2
	Sequence conflict	238 – 239	2	VG → C in BAB28516. Ref.2
	Sequence conflict	350	1	V → A in BAC40335. Ref.2
	Sequence conflict	403	1	A → R in BAA82838. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform II [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 33DCD4F44607168A	FASTA	434	49,620
	10 20 30 40 50 60 MAAADIARQV GEDCRTVPLA GHVGFDSLPD QLVNKSVSQG FCFNILCVGE TGLGKSTLMD 70 80 90 100 110 120 TLFNTKFEGE PATHTQPGVQ LQSNTYDLQE SNVGLKLTIV STVGFGDQIN KEDSYKPIVE 130 140 150 160 170 180 FIDAQFEAYL QEELKIRRVL HSYHDSRIHV CLYFIAPTGH SLKSLDLVTM KKLDSKVNII 190 200 210 220 230 240 PVIAKSDAIS KSELAKFKIK ITSELVSNGV QIYQFPTDDE SVSEINGTMN AHLPFAVVGS 250 260 270 280 290 300 TEEVKIGNKM MRARQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HARHYELYRR 310 320 330 340 350 360 CKLEEMGFKD TDPDSKPFSL QETYEAKRNE FLGELQKKEE EMRQMFVQRV KEKEAELKEA 370 380 390 400 410 420 EKELHEKFDR LKKLHQEEKK KLEDKKKCLD EEMNAFKQRK AAAELLQSQG SQAGGSQTLK 430 RDKEKKNNPW LCIE
	Isoform I (III) [UniParc]. Checksum: 6A6315BB1E6B24C4	FASTA	427	48,764
	10 20 30 40 50 60 MAAADIARQV GEDCRTVPLA GHVGFDSLPD QLVNKSVSQG FCFNILCVGE TGLGKSTLMD 70 80 90 100 110 120 TLFNTKFEGE PATHTQPGVQ LQSNTYDLQE SNVGLKLTIV STVGFGDQIN KEDSYKPIVE 130 140 150 160 170 180 FIDAQFEAYL QEELKIRRVL HSYHDSRIHV CLYFIAPTGH SLKSLDLVTM KKLDSKVNII 190 200 210 220 230 240 PVIAKSDAIS KSELAKFKIK ITSELVSNGV QIYQFPTDDE SVSEINGTMN AHLPFAVVGS 250 260 270 280 290 300 TEEVKIGNKM MRARQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HARHYELYRR 310 320 330 340 350 360 CKLEEMGFKD TDPDSKPFSL QETYEAKRNE FLGELQKKEE EMRQMFVQRV KEKEAELKEA 370 380 390 400 410 420 EKELHEKFDR LKKLHQEEKK KLEDKKKCLD EEMNAFKQRK AAAELLQSQG SQAGGSQTLK RDKEKKN
	Isoform V [UniParc]. Checksum: 59BB0A6315BB1E6B	FASTA	429	49,058
	10 20 30 40 50 60 MAAADIARQV GEDCRTVPLA GHVGFDSLPD QLVNKSVSQG FCFNILCVGE TGLGKSTLMD 70 80 90 100 110 120 TLFNTKFEGE PATHTQPGVQ LQSNTYDLQE SNVGLKLTIV STVGFGDQIN KEDSYKPIVE 130 140 150 160 170 180 FIDAQFEAYL QEELKIRRVL HSYHDSRIHV CLYFIAPTGH SLKSLDLVTM KKLDSKVNII 190 200 210 220 230 240 PVIAKSDAIS KSELAKFKIK ITSELVSNGV QIYQFPTDDE SVSEINGTMN AHLPFAVVGS 250 260 270 280 290 300 TEEVKIGNKM MRARQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HARHYELYRR 310 320 330 340 350 360 CKLEEMGFKD TDPDSKPFSL QETYEAKRNE FLGELQKKEE EMRQMFVQRV KEKEAELKEA 370 380 390 400 410 420 EKELHEKFDR LKKLHQEEKK KLEDKKKCLD EEMNAFKQRK AAAELLQSQG SQAGGSQTLK RDKEKKNFF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of mouse Septin6 gene and its product." Kinoshita M. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V). Strain: NIH Swiss. Tissue: Heart.
[2]	"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. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS II AND V). Strain: C57BL/6J and NOD. Tissue: Embryo, Head and Thymus.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"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] (ISOFORM I). Tissue: Salivary gland.
[5]	"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H. DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-427. Tissue: Fetal brain.
[6]	Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 16-111; 164-171; 177-185; 255-273; 281-287; 294-299; 310-337; 388-397 AND 400-420, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[7]	"Differential localization of septins in the mouse brain." Kinoshita A., Noda M., Kinoshita M. J. Comp. Neurol. 428:223-239(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"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-416, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB023622 mRNA. Translation: BAA82838.1. AK012858 mRNA. Translation: BAB28516.1. AK048455 mRNA. Translation: BAC33342.1. AK088406 mRNA. Translation: BAC40335.1. AK088614 mRNA. Translation: BAC40453.1. AK160884 mRNA. Translation: BAE36069.1. AK162755 mRNA. Translation: BAE37050.1. AL450399 Genomic DNA. Translation: CAM19780.1. AL450399 Genomic DNA. Translation: CAM19781.1. AL450399 Genomic DNA. Translation: CAM19782.1. Sequence problems. BC010489 mRNA. Translation: AAH10489.1. AK172894 mRNA. Translation: BAD32172.1. Different initiation.
IPI	IPI00226602. IPI00462803. IPI00473707.
RefSeq	NP_001170794.1. NM_001177323.2. NP_001170795.1. NM_001177324.1. NP_001240635.1. NM_001253706.1. NP_064326.2. NM_019942.5.
UniGene	Mm.260036. Mm.470184.
3D structure databases
ProteinModelPortal	Q9R1T4.
SMR	Q9R1T4. Positions 25-303.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9R1T4. 2 interactions.
MINT	MINT-4134187.
PTM databases
PhosphoSite	Q9R1T4.
Proteomic databases
PaxDb	Q9R1T4.
PRIDE	Q9R1T4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000053456; ENSMUSP00000054034; ENSMUSG00000050379. ENSMUST00000060474; ENSMUSP00000062014; ENSMUSG00000050379. ENSMUST00000115239; ENSMUSP00000110894; ENSMUSG00000050379.
GeneID	56526.
KEGG	mmu:56526.
UCSC	uc009sxx.2. mouse. uc009sxz.2. mouse.
Organism-specific databases
CTD	23157.
MGI	MGI:1888939. Sept6.
Rouge	Search...
Phylogenomic databases
eggNOG	COG5019.
GeneTree	ENSGT00640000091237.
HOVERGEN	HBG065093.
InParanoid	Q9R1T4.
OrthoDB	EOG4320Z8.
Gene expression databases
ArrayExpress	Q9R1T4.
Bgee	Q9R1T4.
CleanEx	MM_SEPT6.
Genevestigator	Q9R1T4.
GermOnline	ENSMUSG00000050379. Mus musculus.
Family and domain databases
InterPro	IPR000038. Cell_div_GTP-bd. IPR027417. P-loop_NTPase. IPR016491. Septin. [Graphical view]
PANTHER	PTHR18884. PTHR18884. 1 hit.
Pfam	PF00735. Septin. 1 hit. [Graphical view]
PIRSF	PIRSF006698. Septin. 1 hit.
SUPFAM	SSF52540. SSF52540. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	SEPT6. mouse.
NextBio	312866.
SOURCE	Search...

Entry information

Entry name

SEPT6_MOUSE

Accession

Primary (citable) accession number: Q9R1T4
Secondary accession number(s): A2A3V9 , A2A3W0, Q3TRH9, Q3TUA2, Q542H3, Q6A0C4, Q8C2L2, Q8C848, Q91XH2, Q9CZ94

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 115 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program