SEPT3_BOVIN
ID SEPT3_BOVIN Reviewed; 357 AA.
AC Q08DM7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Neuronal-specific septin-3;
GN Name=SEPTIN3 {ECO:0000250|UniProtKB:Q9UH03}; Synonyms=SEPT3;
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=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May
CC play a role in cytokinesis (Potential). {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. GTPase activity is required for filament
CC formation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Synapse {ECO:0000250}.
CC -!- PTM: Phosphorylated by PKG on serine residues. Phosphorylated by PKG on
CC Ser-91 (By similarity). {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; BC123664; AAI23665.1; -; mRNA.
DR RefSeq; NP_001070417.1; NM_001076949.1.
DR AlphaFoldDB; Q08DM7; -.
DR SMR; Q08DM7; -.
DR STRING; 9913.ENSBTAP00000017531; -.
DR PaxDb; Q08DM7; -.
DR PRIDE; Q08DM7; -.
DR Ensembl; ENSBTAT00000017531; ENSBTAP00000017531; ENSBTAG00000013173.
DR GeneID; 618235; -.
DR KEGG; bta:618235; -.
DR CTD; 55964; -.
DR VEuPathDB; HostDB:ENSBTAG00000013173; -.
DR VGNC; VGNC:34455; SEPTIN3.
DR eggNOG; KOG1547; Eukaryota.
DR GeneTree; ENSGT00940000158004; -.
DR HOGENOM; CLU_017718_7_1_1; -.
DR InParanoid; Q08DM7; -.
DR OMA; QCEFVYL; -.
DR OrthoDB; 845354at2759; -.
DR TreeFam; TF101078; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000013173; Expressed in Ammon's horn and 78 other tissues.
DR ExpressionAtlas; Q08DM7; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0099569; C:presynaptic 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 GO; GO:0008104; P:protein localization; IBA:GO_Central.
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; IPR008114; Septin3.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01741; SEPTIN3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..357
FT /note="Neuronal-specific septin-3"
FT /id="PRO_0000270221"
FT DOMAIN 58..330
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..75
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 125..128
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 207..210
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT BINDING 68..75
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 102
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 208..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 264
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 279
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU34"
SQ SEQUENCE 357 AA; 40538 MW; 664DD1E4A0C988B1 CRC64;
MSKGLPETRT DAAMSELVPE PRPKPAVPMK PIGINPNLLG YIGIDTIIEQ MRKKTMKTGF
DFNIMVVGQS GLGKSTLVNT LFKSQVSRKA SSWNREEKIP KTVEIKAIGH VIEEGGVKMK
LTVIDTPGFG DQINNENCWE PIEKYINEQY EKFLKEEVNI ARKKRIPDTR VHCCLYFISP
TGHSLRPLDL EFMKHLSKVV NIIPVIAKAD TMTLEEKSEF KQRVRKELEV NGIEFYPQKE
FDEDLEDKTE NDKIRESMPF AVVGSDKEYQ VNGKRVLGRK TPWGIIEVEN LNHCEFALLR
DFVIRTHLQD LKEVTHNIHY ETYRAKRLND NGGLPPGEGL LGTVLPPVPA TPCPTAE
