ID SEP11_BOVIN Reviewed; 425 AA.
AC A2VE99;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 101.
DE RecName: Full=Septin-11;
GN Name=SEPTIN11 {ECO:0000250|UniProtKB:Q9NVA2}; Synonyms=SEPT11;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal spinal cord;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May
CC play a role in cytokinesis (Potential). May play a role in the
CC cytoarchitecture of neurons, including dendritic arborization and
CC dendritic spines, and in GABAergic synaptic connectivity (By
CC similarity). {ECO:0000250, 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, cytoskeleton. Synapse. Cell
CC projection, dendritic spine. Cell projection, axon {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; BC133640; AAI33641.1; -; mRNA.
DR RefSeq; NP_001075916.1; NM_001082447.2.
DR AlphaFoldDB; A2VE99; -.
DR SMR; A2VE99; -.
DR STRING; 9913.ENSBTAP00000066044; -.
DR PaxDb; 9913-ENSBTAP00000005626; -.
DR Ensembl; ENSBTAT00000075617.1; ENSBTAP00000063083.1; ENSBTAG00000021372.6.
DR GeneID; 535746; -.
DR KEGG; bta:535746; -.
DR CTD; 55752; -.
DR VEuPathDB; HostDB:ENSBTAG00000021372; -.
DR VGNC; VGNC:34451; SEPTIN11.
DR eggNOG; KOG3859; Eukaryota.
DR GeneTree; ENSGT00940000160196; -.
DR HOGENOM; CLU_017718_8_1_1; -.
DR InParanoid; A2VE99; -.
DR OMA; INQQFEN; -.
DR TreeFam; TF101080; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000021372; Expressed in conceptus and 111 other cell types or tissues.
DR ExpressionAtlas; A2VE99; baseline.
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:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0031105; C:septin complex; ISS:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
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 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.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; 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..425
FT /note="Septin-11"
FT /id="PRO_0000312862"
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 399..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 320..410
FT /evidence="ECO:0000255"
FT COMPBIAS 399..415
FT /note="Polar 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"
SQ SEQUENCE 425 AA; 48992 MW; B5FFD028DD2E0767 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 EVNNFQKKKA AAQLLQSQAQ QSGAQQTKKD
KDKKN
//
