ID SEPT7_MOUSE Reviewed; 436 AA. AC O55131; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 192. DE RecName: Full=Septin-7; DE AltName: Full=CDC10 protein homolog; GN Name=Septin7 {ECO:0000312|MGI:MGI:1335094}; GN Synonyms=Cdc10 {ECO:0000303|PubMed:9804986}, Sept7 GN {ECO:0000312|MGI:MGI:1335094}; 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 [GENOMIC DNA / MRNA]. RC STRAIN=BALB/cJ; RX PubMed=9804986; DOI=10.1016/s0167-4781(98)00183-3; RA Soulier S., Vilotte J.-L.; RT "Sequence of murine CDC10 cDNA, gene organization and expression RT analysis."; RL Biochim. Biophys. Acta 1442:339-346(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; 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 [3] RP PROTEIN SEQUENCE OF 25-41; 63-95; 137-146; 186-207; 221-234; 298-309; RP 333-342 AND 416-424, AND 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 [4] RP INTERACTION WITH SEPTIN2 AND SEPTIN5. RX PubMed=11739749; DOI=10.1128/mcb.22.1.378-387.2002; RA Peng X.-R., Jia Z., Zhang Y., Ware J., Trimble W.S.; RT "The septin CDCrel-1 is dispensable for normal development and RT neurotransmitter release."; RL Mol. Cell. Biol. 22:378-387(2002). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=17546647; DOI=10.1002/humu.20554; RA Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.; RT "SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are RT associated with altered interactions with SEPT4/SEPT11 and resistance to RT Rho/Rhotekin-signaling."; RL Hum. Mutat. 28:1005-1013(2007). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., RA Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in naive RT and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; THR-227; SER-333 AND RP THR-425, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, 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). RN [10] RP TISSUE SPECIFICITY. RX PubMed=20181826; DOI=10.1091/mbc.e09-10-0869; RA Shinoda T., Ito H., Sudo K., Iwamoto I., Morishita R., Nagata K.; RT "Septin 14 is involved in cortical neuronal migration via interaction with RT Septin 4."; RL Mol. Biol. Cell 21:1324-1334(2010). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-372, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal CC organization of the actin cytoskeleton. Required for normal progress CC through mitosis. Involved in cytokinesis. Required for normal CC association of CENPE with the kinetochore. Plays a role in ciliogenesis CC and collective cell movements. Forms a filamentous structure with CC SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus CC which is required for the structural integrity and motility of the CC sperm tail during postmeiotic differentiation (By similarity). CC {ECO:0000250, ECO:0000250|UniProtKB:Q16181}. CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes CC that form filaments, and associate with cellular membranes, actin CC filaments and microtubules. GTPase activity is required for filament CC formation. Filaments are assembled from asymmetrical heterotrimers, CC composed of SEPTIN2, SEPTIN6 and SEPTIN7 that associate head-to-head to CC form a hexameric unit. Within the trimer, directly interacts with CC SEPTIN6, while interaction with SEPTIN2 seems indirect. In the absence CC of SEPTIN6, forms homodimers. Interacts directly with CENPE and links CC CENPE to septin filaments composed of SEPTIN2, SEPTIN6 and SEPTIN7. CC Interacts with SEPTIN8, SEPTIN9 and SEPTIN11. Component of a septin CC core octameric complex consisting of SEPTIN12, SEPTIN7, SEPTIN6 and CC SEPTIN2 or SEPTIN4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 CC and located in the sperm annulus; the SEPTIN12:SEPTIN7 association is CC mediated by the respective GTP-binding domains (By similarity). CC Interacts with SEPTIN2 and SEPTIN5 (PubMed:11739749). {ECO:0000250, CC ECO:0000250|UniProtKB:Q16181, ECO:0000269|PubMed:11739749}. CC -!- INTERACTION: CC O55131; Q9Z2V5: Hdac6; NbExp=3; IntAct=EBI-772161, EBI-1009256; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17546647}. CC Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, CC cytoskeleton, spindle {ECO:0000250}. Cleavage furrow {ECO:0000250}. CC Midbody {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme CC {ECO:0000250}. Cell projection, cilium, flagellum CC {ECO:0000250|UniProtKB:Q16181}. Note=Distributed throughout the CC cytoplasm in prometaphase cells. Associated with the spindle during CC metaphase. Associated with the central spindle and at the cleavage CC furrow in anaphase cells. Detected at the midbody in telophase (By CC similarity). Associated with actin stress fibers. Found in the sperm CC annulus (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16181}. CC -!- TISSUE SPECIFICITY: Expressed in the cerebral cortex (at protein CC level). {ECO:0000269|PubMed:20181826}. CC -!- MISCELLANEOUS: Coordinated expression with SEPTIN2 and SEPTIN6. CC {ECO:0000250}. 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 --------------------------------------------------------------------------- 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; AJ223782; CAA11547.1; -; Genomic_DNA. DR EMBL; AJ223783; CAA11547.1; JOINED; Genomic_DNA. DR EMBL; AJ223784; CAA11547.1; JOINED; Genomic_DNA. DR EMBL; AJ223785; CAA11547.1; JOINED; Genomic_DNA. DR EMBL; AJ223786; CAA11547.1; JOINED; Genomic_DNA. DR EMBL; AJ223787; CAA11547.1; JOINED; Genomic_DNA. DR EMBL; AJ223788; CAA11547.1; JOINED; Genomic_DNA. DR EMBL; AJ223789; CAA11547.1; JOINED; Genomic_DNA. DR EMBL; AJ223790; CAA11547.1; JOINED; Genomic_DNA. DR EMBL; AJ223791; CAA11547.1; JOINED; Genomic_DNA. DR EMBL; AJ223792; CAA11547.1; JOINED; Genomic_DNA. DR EMBL; AJ223793; CAA11547.1; JOINED; Genomic_DNA. DR EMBL; AJ223794; CAA11547.1; JOINED; Genomic_DNA. DR EMBL; BC058587; AAH58587.1; -; mRNA. DR RefSeq; NP_001192296.1; NM_001205367.1. DR AlphaFoldDB; O55131; -. DR SMR; O55131; -. DR BioGRID; 231619; 37. DR IntAct; O55131; 14. DR MINT; O55131; -. DR STRING; 10090.ENSMUSP00000127641; -. DR GlyGen; O55131; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O55131; -. DR PhosphoSitePlus; O55131; -. DR SwissPalm; O55131; -. DR EPD; O55131; -. DR jPOST; O55131; -. DR MaxQB; O55131; -. DR PaxDb; 10090-ENSMUSP00000110927; -. DR PeptideAtlas; O55131; -. DR ProteomicsDB; 261159; -. DR Pumba; O55131; -. DR DNASU; 235072; -. DR GeneID; 235072; -. DR KEGG; mmu:235072; -. DR AGR; MGI:1335094; -. DR CTD; 989; -. DR MGI; MGI:1335094; Septin7. DR eggNOG; KOG2655; Eukaryota. DR InParanoid; O55131; -. DR OrthoDB; 5396944at2759; -. DR PhylomeDB; O55131; -. DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling. DR BioGRID-ORCS; 235072; 10 hits in 50 CRISPR screens. DR ChiTaRS; Sept7; mouse. DR PRO; PR:O55131; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; O55131; Protein. DR GO; GO:0043679; C:axon terminus; IDA:MGI. DR GO; GO:0005930; C:axoneme; ISS:UniProtKB. DR GO; GO:0005938; C:cell cortex; IDA:MGI. DR GO; GO:0032153; C:cell division site; IBA:GO_Central. DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW. DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central. DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell. DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB. DR GO; GO:0043005; C:neuron projection; IDA:MGI. DR GO; GO:0043025; C:neuronal cell body; IDA:MGI. DR GO; GO:0097730; C:non-motile cilium; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0150050; C:postsynaptic septin cytoskeleton; ISO:MGI. DR GO; GO:0042734; C:presynaptic membrane; IDA:SynGO. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0031105; C:septin complex; IDA:UniProtKB. DR GO; GO:0032156; C:septin cytoskeleton; IDA:MGI. DR GO; GO:0032160; C:septin filament array; IDA:MGI. DR GO; GO:0005940; C:septin ring; IDA:MGI. DR GO; GO:0097227; C:sperm annulus; ISO:MGI. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR GO; GO:0001725; C:stress fiber; ISO:MGI. DR GO; GO:0045202; C:synapse; IDA:MGI. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central. DR GO; GO:0099186; F:structural constituent of postsynapse; ISO:MGI. DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB. DR GO; GO:0048668; P:collateral sprouting; IMP:MGI. DR GO; GO:0030865; P:cortical cytoskeleton organization; IMP:MGI. DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central. DR GO; GO:0060997; P:dendritic spine morphogenesis; IMP:MGI. DR GO; GO:0000281; P:mitotic cytokinesis; IMP:MGI. DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; ISO:MGI. DR GO; GO:0099173; P:postsynapse organization; ISO:MGI. DR GO; GO:0031270; P:pseudopodium retraction; IMP:MGI. DR GO; GO:0016476; P:regulation of embryonic cell shape; ISS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW. DR CDD; cd01850; CDC_Septin; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR030379; G_SEPTIN_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR016491; Septin. DR InterPro; IPR008115; Septin7. DR PANTHER; PTHR18884; SEPTIN; 1. DR PANTHER; PTHR18884:SF129; SEPTIN-7; 1. DR Pfam; PF00735; Septin; 1. DR PIRSF; PIRSF006698; Septin; 1. DR PRINTS; PR01742; SEPTIN7. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51719; G_SEPTIN; 1. PE 1: Evidence at protein level; KW Acetylation; Cell cycle; Cell division; Cell projection; Centromere; KW Chromosome; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Differentiation; KW Direct protein sequencing; Flagellum; GTP-binding; Kinetochore; Mitosis; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Spermatogenesis. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q16181" FT CHAIN 2..436 FT /note="Septin-7" FT /id="PRO_0000173529" FT DOMAIN 46..315 FT /note="Septin-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 46..316 FT /note="Interaction with SEPTIN12" FT /evidence="ECO:0000250|UniProtKB:Q16181" FT REGION 56..63 FT /note="G1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 112..115 FT /note="G3 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 193..196 FT /note="G4 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 377..436 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 331..436 FT /evidence="ECO:0000255" FT COMPBIAS 377..412 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 56..63 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 89 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 115 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 194..202 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 249 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 264 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:Q16181" FT MOD_RES 29 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18034455" FT MOD_RES 76 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 227 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 333 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 372 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 423 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q16181" FT MOD_RES 425 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" SQ SEQUENCE 436 AA; 50550 MW; 1028CCF14023059C CRC64; MSVSARSAAA EERSVNCGTM AQPKNLEGYV GFANLPNQVY RKSVKRGFEF TLMVVGESGL GKSTLINSLF LTDLYSPEYP GPSHRIKKTV QVEQSKVLIK EGGVQLLLTI VDTPGFGDAV DNSNCWQPVI DYIDSKFEDY LNAESRVNRR QMPDNRVQCC LYFIAPSGHG LKPLDIEFMK RLHEKVNIIP LIAKADTLTP EECQQFKKQI MKEIQEHKIK IYEFPETDDE EENKLVKKIK DRLPLAVVGS NTIIEVNGKR VRGRQYPWGV AEVENGEHCD FTILRNMLIR THMQDLKDVT NNVHYENYRS RKLAAVTYNG VDNNKNKGQL TKSPLAQMEE ERREHVAKMK KMEMEMEQVF EMKVKEKVQK LKDSEAELQR RHEQMKKNLE AQHKELEEKR RQFEEEKANW EAQQRILEQQ NSSRTLEKNK KKGKIF //