SEP11_RAT
ID SEP11_RAT Reviewed; 431 AA.
AC B3GNI6; B3DMA8; B3GNI4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Septin-11;
GN Name=Septin11 {ECO:0000250|UniProtKB:Q9NVA2};
GN Synonyms=Sept11 {ECO:0000312|RGD:1307405};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=19380581; DOI=10.1074/jbc.m109.008870;
RA Li X., Serwanski D.R., Miralles C.P., Nagata K., De Blas A.L.;
RT "Septin 11 is present in GABAergic synapses and plays a functional role in
RT the cytoarchitecture of neurons and GABAergic synaptic connectivity.";
RL J. Biol. Chem. 284:17253-17265(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 PROTEIN SEQUENCE OF 2-14 AND 176-184, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fibroblast;
RA Bienvenut W.V., von Kriegsheim A., Kolch W.;
RL Submitted (JUN-2009) to UniProtKB.
RN [5]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH STRESS FIBERS.
RX PubMed=15196925; DOI=10.1016/j.febslet.2004.05.030;
RA Hanai N., Nagata K., Kawajiri A., Shiromizu T., Saitoh N., Hasegawa Y.,
RA Murakami S., Inagaki M.;
RT "Biochemical and cell biological characterization of a mammalian septin,
RT Sept11.";
RL FEBS Lett. 568:83-88(2004).
RN [6]
RP INTERACTION WITH SEPTIN7, AND SUBCELLULAR LOCATION.
RX PubMed=15485874; DOI=10.1074/jbc.m406153200;
RA Nagata K., Asano T., Nozawa Y., Inagaki M.;
RT "Biochemical and cell biological analyses of a mammalian septin complex,
RT Sept7/9b/11.";
RL J. Biol. Chem. 279:55895-55904(2004).
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. {ECO:0000269|PubMed:19380581,
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 (PubMed:15485874). Interacts with
CC SEPTIN9 and SEPTIN12 (By similarity). {ECO:0000250|UniProtKB:Q9NVA2,
CC ECO:0000269|PubMed:15485874}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Synapse. Cell
CC projection, dendritic spine. Cell projection, axon. Note=Partly
CC colocalizes with stress fibers. Association with microtubules not
CC observed in embryonic fibroblasts. In cultured hippocampal neurons,
CC localizes to 54% of GABAergic and 25% of glutamatergic synapses.
CC Frequently present at the base of dendritic protrusions and at the
CC bifurcation points of the dendritic branches. Expressed at low levels
CC in the axons of mature cultured hippocampal neurons. In embryonic
CC fibroblasts, associated with actin stress fibers.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=III;
CC IsoId=B3GNI6-1; Sequence=Displayed;
CC Name=2; Synonyms=I, II;
CC IsoId=B3GNI6-2; Sequence=VSP_038168;
CC Name=3; Synonyms=IV;
CC IsoId=B3GNI6-3; Sequence=VSP_038169;
CC -!- TISSUE SPECIFICITY: Highly expressed in cerebellum, olfactory bulb,
CC hippocampus, cerebral cortex, thalamus, and corpus striatum. In the
CC hippocampus, strong expression around the pyramidal cells of the
CC stratum pyramidale and in the stratum lucidum of the CA2-CA3 regions.
CC In the olfactory bulb, particularly strong expression in the external
CC plexiform layer. In the cerebellum, concentrates in the molecular
CC layer, particularly in Purkinje cells, where it is found at the base of
CC dendritic spines/protrusions, at the dendritic branching points and in
CC some GABAergic synapses. {ECO:0000269|PubMed:19380581}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo and in early postnatal
CC weeks. On and before P14, distributes in a homogeneous way, throughout
CC the brain. By P21, high expression observed in the molecular layer of
CC the cerebellum and in the olfactory bulb. The maximum expression and
CC the adult pattern of distribution in the brain occurs by P30. By P30,
CC P45 and P90, highest expression occurs in the molecular layer of the
CC cerebellum and in the olfactory bulb, and relatively high expression in
CC the hippocampus, cerebral cortex, thalamus and corpus striatum.
CC {ECO:0000269|PubMed:19380581}.
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; EU711414; ACE00321.1; -; mRNA.
DR EMBL; EU711415; ACE00322.1; -; mRNA.
DR EMBL; EU711416; ACE00323.1; -; mRNA.
DR EMBL; EU711417; ACE00324.1; -; mRNA.
DR EMBL; CH474060; EDL88655.1; -; Genomic_DNA.
DR EMBL; BC167769; AAI67769.1; -; mRNA.
DR RefSeq; NP_001100678.1; NM_001107208.2. [B3GNI6-2]
DR AlphaFoldDB; B3GNI6; -.
DR SMR; B3GNI6; -.
DR BioGRID; 258101; 3.
DR IntAct; B3GNI6; 2.
DR MINT; B3GNI6; -.
DR STRING; 10116.ENSRNOP00000062626; -.
DR iPTMnet; B3GNI6; -.
DR PhosphoSitePlus; B3GNI6; -.
DR jPOST; B3GNI6; -.
DR PaxDb; B3GNI6; -.
DR PeptideAtlas; B3GNI6; -.
DR PRIDE; B3GNI6; -.
DR Ensembl; ENSRNOT00000100885; ENSRNOP00000090314; ENSRNOG00000002182. [B3GNI6-2]
DR GeneID; 305227; -.
DR KEGG; rno:305227; -.
DR UCSC; RGD:1307405; rat. [B3GNI6-1]
DR CTD; 55752; -.
DR RGD; 1307405; Sept11.
DR VEuPathDB; HostDB:ENSRNOG00000002182; -.
DR eggNOG; KOG3859; Eukaryota.
DR GeneTree; ENSGT00940000160196; -.
DR InParanoid; B3GNI6; -.
DR OMA; NGFIFNI; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; B3GNI6; -.
DR TreeFam; TF101080; -.
DR PRO; PR:B3GNI6; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Proteomes; UP000234681; Chromosome 14.
DR Bgee; ENSRNOG00000002182; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; B3GNI6; baseline and differential.
DR Genevisible; B3GNI6; RN.
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; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0099629; C:postsynaptic specialization of symmetric synapse; IDA:SynGO.
DR GO; GO:0031105; C:septin complex; ISS:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; ISO:RGD.
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; IDA:SynGO.
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:0000269|Ref.4"
FT CHAIN 2..431
FT /note="Septin-11"
FT /id="PRO_0000385476"
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..408
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:0000269|Ref.4"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVA2"
FT VAR_SEQ 425
FT /note="N -> NS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19380581"
FT /id="VSP_038168"
FT VAR_SEQ 426..431
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19380581"
FT /id="VSP_038169"
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
