SEPT8_MOUSE
ID SEPT8_MOUSE Reviewed; 429 AA.
AC Q8CHH9; B1AQY7; Q80YC7; Q9ESF7;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Septin-8 {ECO:0000305};
GN Name=Septin8 {ECO:0000312|MGI:MGI:894310};
GN Synonyms=Kiaa0202 {ECO:0000303|PubMed:14621295},
GN Sept8 {ECO:0000312|MGI:MGI:894310};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Fetal brain, and Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-429 (ISOFORM 1).
RC STRAIN=129/Sv;
RX PubMed=10704283; DOI=10.1006/geno.1999.6100;
RA Wenderfer S.E., Slack J.P., McCluskey T.S., Monaco J.J.;
RT "Identification of 40 genes on a 1-Mb contig around the IL-4 cytokine
RT family gene cluster on mouse chromosome 11.";
RL Genomics 63:354-373(2000).
RN [5]
RP PROTEIN SEQUENCE OF 18-37; 99-113; 179-187; 283-289 AND 296-301, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP INTERACTION WITH SEPTIN5.
RX PubMed=12909369; DOI=10.1016/s0378-1119(03)00635-8;
RA Blaeser S., Jersch K., Hainmann I., Zieger W., Wunderle D., Busse A.,
RA Zieger B.;
RT "Isolation of new splice isoforms, characterization and expression analysis
RT of the human septin SEPT8 (KIAA0202).";
RL Gene 312:313-320(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-10, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP INTERACTION WITH VAMP2.
RX PubMed=19196426; DOI=10.1111/j.1471-4159.2008.05849.x;
RA Ito H., Atsuzawa K., Morishita R., Usuda N., Sudo K., Iwamoto I.,
RA Mizutani K., Katoh-Semba R., Nozawa Y., Asano T., Nagata K.;
RT "Sept8 controls the binding of vesicle-associated membrane protein 2 to
RT synaptophysin.";
RL J. Neurochem. 108:867-880(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May
CC play a role in platelet secretion (By similarity). Seems to participate
CC in the process of SNARE complex formation in synaptic vesicles (By
CC similarity). {ECO:0000250|UniProtKB:B0BNF1,
CC ECO:0000250|UniProtKB:Q92599}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and can associate with cellular membranes, actin
CC filaments and microtubules. GTPase activity is required for filament
CC formation (By similarity). Interacts with SEPTIN5 (PubMed:12909369).
CC Interacts with CDK14, SEPTIN4 and SEPTIN7 (By similarity). Interacts
CC with VAMP2; the interaction inhibits interaction of VAMP2 with SYP
CC (PubMed:19196426). Interacts with STX1A (By similarity).
CC {ECO:0000250|UniProtKB:B0BNF1, ECO:0000250|UniProtKB:Q92599,
CC ECO:0000269|PubMed:12909369, ECO:0000269|PubMed:19196426}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0BNF1}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Synapse
CC {ECO:0000250|UniProtKB:B0BNF1}. Cell projection, axon
CC {ECO:0000250|UniProtKB:B0BNF1}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000250|UniProtKB:B0BNF1}. Presynapse
CC {ECO:0000250|UniProtKB:B0BNF1}. Note=Expressed in axons of immature
CC neurons, localizes to synapses in mature neurons.
CC {ECO:0000250|UniProtKB:B0BNF1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CHH9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CHH9-2; Sequence=VSP_009645;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49819.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC41399.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB093215; BAC41399.1; ALT_SEQ; mRNA.
DR EMBL; AL596095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049819; AAH49819.1; ALT_INIT; mRNA.
DR EMBL; BC059248; AAH59248.1; -; mRNA.
DR EMBL; AF179996; AAG09408.1; -; mRNA.
DR CCDS; CCDS48794.1; -. [Q8CHH9-2]
DR CCDS; CCDS56768.1; -. [Q8CHH9-1]
DR RefSeq; NP_001239261.1; NM_001252332.1. [Q8CHH9-1]
DR RefSeq; NP_001239262.1; NM_001252333.1.
DR RefSeq; NP_149156.1; NM_033144.2. [Q8CHH9-2]
DR AlphaFoldDB; Q8CHH9; -.
DR SMR; Q8CHH9; -.
DR BioGRID; 203177; 14.
DR IntAct; Q8CHH9; 4.
DR MINT; Q8CHH9; -.
DR STRING; 10090.ENSMUSP00000112920; -.
DR iPTMnet; Q8CHH9; -.
DR PhosphoSitePlus; Q8CHH9; -.
DR SwissPalm; Q8CHH9; -.
DR UCD-2DPAGE; Q8CHH9; -.
DR EPD; Q8CHH9; -.
DR jPOST; Q8CHH9; -.
DR MaxQB; Q8CHH9; -.
DR PaxDb; Q8CHH9; -.
DR PRIDE; Q8CHH9; -.
DR ProteomicsDB; 255388; -. [Q8CHH9-1]
DR ProteomicsDB; 255389; -. [Q8CHH9-2]
DR Antibodypedia; 26134; 244 antibodies from 30 providers.
DR DNASU; 20362; -.
DR Ensembl; ENSMUST00000108987; ENSMUSP00000104615; ENSMUSG00000018398. [Q8CHH9-1]
DR Ensembl; ENSMUST00000117061; ENSMUSP00000112920; ENSMUSG00000018398. [Q8CHH9-2]
DR GeneID; 20362; -.
DR KEGG; mmu:20362; -.
DR UCSC; uc007iwh.2; mouse. [Q8CHH9-1]
DR UCSC; uc007iwj.2; mouse. [Q8CHH9-2]
DR CTD; 23176; -.
DR MGI; MGI:894310; Septin8.
DR VEuPathDB; HostDB:ENSMUSG00000018398; -.
DR eggNOG; KOG3859; Eukaryota.
DR GeneTree; ENSGT00940000156068; -.
DR HOGENOM; CLU_017718_8_1_1; -.
DR InParanoid; Q8CHH9; -.
DR OMA; MDLVCMK; -.
DR PhylomeDB; Q8CHH9; -.
DR TreeFam; TF101080; -.
DR BioGRID-ORCS; 20362; 5 hits in 48 CRISPR screens.
DR ChiTaRS; Sept8; mouse.
DR PRO; PR:Q8CHH9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8CHH9; protein.
DR Bgee; ENSMUSG00000018398; Expressed in humerus cartilage element and 251 other tissues.
DR ExpressionAtlas; Q8CHH9; baseline and differential.
DR Genevisible; Q8CHH9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0031105; C:septin complex; IDA:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0033157; P:regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0035542; P:regulation of SNARE complex assembly; ISS:UniProtKB.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030646; SEPT8.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884:SF54; PTHR18884:SF54; 1.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Direct protein sequencing; GTP-binding;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CHAIN 2..429
FT /note="Septin-8"
FT /id="PRO_0000173534"
FT DOMAIN 41..307
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..58
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 103..106
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 186..189
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 409..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 320..412
FT /evidence="ECO:0000255"
FT BINDING 51..58
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 187..195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355"
FT VAR_SEQ 429
FT /note="N -> KF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009645"
FT CONFLICT 58
FT /note="S -> A (in Ref. 1; BAC41399)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 49812 MW; 133485FF0E8D3300 CRC64;
MAATDLERVS NAEPEPRSLS LGGHVGFDSL PDQLVSKSVT QGFSFNILCV GETGIGKSTL
MNTLFNTTFE TEEASHHEEC VRLRPQTYDL QESNVHLKLT IVDAVGFGDQ INKDDSYRPI
VDYIDAQFEN YLQEELKIRR SLFDYHDTRI HVCLYFITPT GHSLKSLDLV TMKKLDSKVN
IIPIIAKADT ISKSELHKFK IKIMGELVSN GVQIYQFPTD DEAVAEINAV MNAHLPFAVV
GSTEEVKVGN KLVRARQYPW GVVQVENENH CDFVKLREML IRVNMEDLRE QTHSRHYELY
RRCKLEEMGF QDSDGDSQPF SLQETYEAKR KEFLSELQRK EEEMRQMFVN KVKETELELK
EKERELHEKF EHLKRIHQEE KRKVEEKRRE LEEETNAFNC RKAAMEALQS QALHATSQQP
LRKDKDKKN
