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   24-JAN-2024, entry version 169.
DE   RecName: Full=Septin-11;
GN   Name=Septin11 {ECO:0000312|MGI:MGI:1277214};
GN   Synonyms=D5Ertd606e {ECO:0000312|MGI:MGI:1277214}, Sept11
GN   {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,
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   [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; 31.
DR   IntAct; Q8C1B7; 19.
DR   MINT; Q8C1B7; -.
DR   STRING; 10090.ENSMUSP00000144235; -.
DR   GlyGen; Q8C1B7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8C1B7; -.
DR   PhosphoSitePlus; Q8C1B7; -.
DR   SwissPalm; Q8C1B7; -.
DR   EPD; Q8C1B7; -.
DR   jPOST; Q8C1B7; -.
DR   MaxQB; Q8C1B7; -.
DR   PaxDb; 10090-ENSMUSP00000074293; -.
DR   PeptideAtlas; Q8C1B7; -.
DR   ProteomicsDB; 256548; -. [Q8C1B7-1]
DR   ProteomicsDB; 256549; -. [Q8C1B7-2]
DR   ProteomicsDB; 256550; -. [Q8C1B7-3]
DR   Pumba; Q8C1B7; -.
DR   Antibodypedia; 24838; 221 antibodies from 28 providers.
DR   DNASU; 52398; -.
DR   Ensembl; ENSMUST00000074733.11; ENSMUSP00000074293.8; ENSMUSG00000058013.12. [Q8C1B7-2]
DR   Ensembl; ENSMUST00000201421.4; ENSMUSP00000143928.2; ENSMUSG00000058013.12. [Q8C1B7-1]
DR   Ensembl; ENSMUST00000202308.4; ENSMUSP00000144136.2; ENSMUSG00000058013.12. [Q8C1B7-3]
DR   GeneID; 52398; -.
DR   KEGG; mmu:52398; -.
DR   UCSC; uc008ydx.1; mouse. [Q8C1B7-1]
DR   UCSC; uc008ydy.1; mouse. [Q8C1B7-2]
DR   AGR; MGI:1277214; -.
DR   CTD; 55752; -.
DR   MGI; MGI:1277214; Septin11.
DR   VEuPathDB; HostDB:ENSMUSG00000058013; -.
DR   eggNOG; KOG3859; Eukaryota.
DR   GeneTree; ENSGT00940000160196; -.
DR   InParanoid; Q8C1B7; -.
DR   OMA; INQQFEN; -.
DR   OrthoDB; 5396944at2759; -.
DR   PhylomeDB; Q8C1B7; -.
DR   TreeFam; TF101080; -.
DR   BioGRID-ORCS; 52398; 1 hit in 51 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 243 other cell types or tissues.
DR   ExpressionAtlas; Q8C1B7; baseline and differential.
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:0050807; P:regulation of synapse organization; ISO:MGI.
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   PANTHER; PTHR18884; SEPTIN; 1.
DR   PANTHER; PTHR18884:SF48; SEPTIN-11; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51719; G_SEPTIN; 1.
DR   Genevisible; Q8C1B7; MM.
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
//