SEPT7_MOUSE
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 03-AUG-2022, entry version 184.
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},
GN Sept7 {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, Pancreas,
RC 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 octomeric 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}.
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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; 32.
DR IntAct; O55131; 13.
DR MINT; O55131; -.
DR STRING; 10090.ENSMUSP00000110927; -.
DR iPTMnet; O55131; -.
DR PhosphoSitePlus; O55131; -.
DR SwissPalm; O55131; -.
DR EPD; O55131; -.
DR jPOST; O55131; -.
DR MaxQB; O55131; -.
DR PaxDb; O55131; -.
DR PeptideAtlas; O55131; -.
DR PRIDE; O55131; -.
DR ProteomicsDB; 261159; -.
DR DNASU; 235072; -.
DR GeneID; 235072; -.
DR KEGG; mmu:235072; -.
DR CTD; 989; -.
DR MGI; MGI:1335094; Septin7.
DR eggNOG; KOG2655; Eukaryota.
DR InParanoid; O55131; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; O55131; -.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR BioGRID-ORCS; 235072; 10 hits in 48 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:0016020; C:membrane; ISO:MGI.
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: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: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:0008104; P:protein localization; IBA:GO_Central.
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; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR InterPro; IPR008115; Septin7.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01742; SEPTIN7.
DR SUPFAM; SSF52540; SSF52540; 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
