SEP11_MOUSE
ID SEP11_MOUSE Reviewed; 431 AA.
AC Q8C1B7; Q3TBA0; Q3TC24; Q5D0F0; Q6P2K5; Q6P6I0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Septin-11;
GN Name=Septin11 {ECO:0000312|MGI:MGI:1277214};
GN Synonyms=D5Ertd606e {ECO:0000312|MGI:MGI:1277214},
GN Sept11 {ECO:0000312|MGI:MGI:1277214};
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] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Mammary gland, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 15-79; 84-93; 96-110; 138-146; 163-170; 176-184;
RP 280-286; 293-298; 309-336; 387-397 AND 399-418, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
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 [5]
RP 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 [6]
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).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase. May play a role in
CC cytokinesis (Potential). May play a role in the cytoarchitecture of
CC neurons, including dendritic arborization and dendritic spines, and in
CC GABAergic synaptic connectivity (By similarity). {ECO:0000250,
CC ECO:0000305}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and can associate with cellular membranes, actin
CC filaments and microtubules (By similarity). Forms homooligomers (By
CC similarity). GTPase activity is required for filament formation (By
CC similarity). Interacts with SEPTIN7, SEPTIN9 and SEPTIN12 (By
CC similarity). {ECO:0000250|UniProtKB:Q9NVA2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17546647}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17546647}. Synapse
CC {ECO:0000269|PubMed:17546647}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:17546647}. Cell projection, axon {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8C1B7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C1B7-2; Sequence=VSP_011041;
CC Name=3;
CC IsoId=Q8C1B7-3; Sequence=VSP_011042;
CC -!- TISSUE SPECIFICITY: Expressed in the cerebral cortex (at protein
CC level). {ECO:0000269|PubMed:20181826}.
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; AK028475; BAC25969.1; -; mRNA.
DR EMBL; AK166517; BAE38822.1; -; mRNA.
DR EMBL; AK170945; BAE42133.1; -; mRNA.
DR EMBL; AK171368; BAE42414.1; -; mRNA.
DR EMBL; BC031456; AAH31456.1; -; mRNA.
DR EMBL; BC062206; AAH62206.1; -; mRNA.
DR EMBL; BC064466; AAH64466.1; -; mRNA.
DR CCDS; CCDS51549.1; -. [Q8C1B7-2]
DR CCDS; CCDS80331.1; -. [Q8C1B7-1]
DR CCDS; CCDS80332.1; -. [Q8C1B7-3]
DR RefSeq; NP_001009818.1; NM_001009818.2. [Q8C1B7-2]
DR RefSeq; NP_001297598.1; NM_001310669.1. [Q8C1B7-1]
DR RefSeq; NP_001297600.1; NM_001310671.1. [Q8C1B7-3]
DR AlphaFoldDB; Q8C1B7; -.
DR SMR; Q8C1B7; -.
DR BioGRID; 206563; 27.
DR IntAct; Q8C1B7; 19.
DR MINT; Q8C1B7; -.
DR STRING; 10090.ENSMUSP00000074293; -.
DR iPTMnet; Q8C1B7; -.
DR PhosphoSitePlus; Q8C1B7; -.
DR SwissPalm; Q8C1B7; -.
DR EPD; Q8C1B7; -.
DR jPOST; Q8C1B7; -.
DR MaxQB; Q8C1B7; -.
DR PaxDb; Q8C1B7; -.
DR PeptideAtlas; Q8C1B7; -.
DR PRIDE; Q8C1B7; -.
DR ProteomicsDB; 256548; -. [Q8C1B7-1]
DR ProteomicsDB; 256549; -. [Q8C1B7-2]
DR ProteomicsDB; 256550; -. [Q8C1B7-3]
DR Antibodypedia; 24838; 203 antibodies from 28 providers.
DR DNASU; 52398; -.
DR Ensembl; ENSMUST00000074733; ENSMUSP00000074293; ENSMUSG00000058013. [Q8C1B7-2]
DR Ensembl; ENSMUST00000201421; ENSMUSP00000143928; ENSMUSG00000058013. [Q8C1B7-1]
DR Ensembl; ENSMUST00000202308; ENSMUSP00000144136; ENSMUSG00000058013. [Q8C1B7-3]
DR GeneID; 52398; -.
DR KEGG; mmu:52398; -.
DR UCSC; uc008ydx.1; mouse. [Q8C1B7-1]
DR UCSC; uc008ydy.1; mouse. [Q8C1B7-2]
DR CTD; 55752; -.
DR MGI; MGI:1277214; Septin11.
DR VEuPathDB; HostDB:ENSMUSG00000058013; -.
DR eggNOG; KOG3859; Eukaryota.
DR GeneTree; ENSGT00940000160196; -.
DR InParanoid; Q8C1B7; -.
DR OMA; NGFIFNI; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q8C1B7; -.
DR TreeFam; TF101080; -.
DR BioGRID-ORCS; 52398; 1 hit in 49 CRISPR screens.
DR ChiTaRS; Sept11; mouse.
DR PRO; PR:Q8C1B7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8C1B7; protein.
DR Bgee; ENSMUSG00000058013; Expressed in gonadal ridge and 240 other tissues.
DR ExpressionAtlas; Q8C1B7; baseline and differential.
DR Genevisible; Q8C1B7; 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:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0099629; C:postsynaptic specialization of symmetric synapse; ISO:MGI.
DR GO; GO:0031105; C:septin complex; IDA:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
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:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
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 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 cycle; Cell division;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NVA2"
FT CHAIN 2..431
FT /note="Septin-11"
FT /id="PRO_0000173543"
FT DOMAIN 38..304
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 48..55
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 100..103
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 183..186
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 400..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 320..413
FT /evidence="ECO:0000255"
FT COMPBIAS 400..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48..55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 184..192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVA2"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVA2"
FT VAR_SEQ 426..431
FT /note="PWLCTE -> ASFA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011041"
FT VAR_SEQ 426..431
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011042"
FT CONFLICT 171
FT /note="K -> N (in Ref. 1; BAC25969)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="K -> T (in Ref. 1; BAE42414)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="N -> K (in Ref. 1; BAE42414)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 49695 MW; CC838B791729B511 CRC64;
MAVAVGRPSN EELRNLSLSG HVGFDSLPDQ LVNKSTSQGF CFNILCVGET GIGKSTLMDT
LFNTKFESDP ATHNEPGVRL KARSYELQES NVRLKLTIVD TVGFGDQINK DDSYKPIVEY
IDAQFEAYLQ EELKIKRSLF NYHDTRIHAC LYFIAPTGHS LKSLDLVTMK KLDSKVNIIP
IIAKADTIAK NELHKFKSKI MSELVSNGVQ IYQFPTDEET VAEINATMSV HLPFAVVGST
EEVKIGNKMA KARQYPWGVV QVENENHCDF VKLREMLIRV NMEDLREQTH TRHYELYRRC
KLEEMGFKDT DPDSKPFSLQ ETYEAKRNEF LGELQKKEEE MRQMFVMRVK EKEAELKEAE
KELHEKFDLL KRTHQEEKKK VEDKKKELEE EVSNFQKKKA AAQLLQSQAQ QSGAQQTKKD
KDKKNPWLCT E
