SEPT5_BOVIN
ID SEPT5_BOVIN Reviewed; 369 AA.
AC Q0VC68;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Septin-5;
GN Name=SEPTIN5 {ECO:0000250|UniProtKB:Q99719}; Synonyms=SEPT5;
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 (AUG-2006) 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 platelet
CC secretion (By 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. GTPase activity is required for filament
CC formation. Interacts with SEPTIN2 and SEPTIN5. In platelets, associated
CC with a complex containing STX4. Interacts with PRKN; this interaction
CC leads to SEPTIN5 ubiquitination and degradation (By similarity).
CC Interacts with DYRK1A (By similarity). Interacts with STX1A; in the
CC cerebellar cortex (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9Z2Q6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by DYRK1A. {ECO:0000250|UniProtKB:Q9Z2Q6}.
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; BC120325; AAI20326.1; -; mRNA.
DR RefSeq; NP_001069839.1; NM_001076371.1.
DR AlphaFoldDB; Q0VC68; -.
DR SMR; Q0VC68; -.
DR STRING; 9913.ENSBTAP00000010956; -.
DR PaxDb; Q0VC68; -.
DR PRIDE; Q0VC68; -.
DR GeneID; 615408; -.
DR KEGG; bta:615408; -.
DR CTD; 5413; -.
DR eggNOG; KOG2655; Eukaryota.
DR InParanoid; Q0VC68; -.
DR OrthoDB; 845354at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0031105; C:septin complex; ISS:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; 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:0030534; P:adult behavior; ISS:UniProtKB.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0035176; P:social behavior; ISS:UniProtKB.
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; IPR030647; SEPT5.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884:SF68; PTHR18884:SF68; 1.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW GTP-binding; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..369
FT /note="Septin-5"
FT /id="PRO_0000270222"
FT DOMAIN 41..314
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 51..58
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 108..111
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 189..192
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT COILED 338..369
FT /evidence="ECO:0000255"
FT BINDING 51..58
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 190..198
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Q6"
FT MOD_RES 168
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Q6"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99719"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99719"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Q6"
SQ SEQUENCE 369 AA; 42705 MW; 6BB362E36BBF0090 CRC64;
MSTGLRYKSK LATPEDKQDV DKQYVGFATL PNQVHRKSVK KGFDFTLMVA GESGLGKSTL
VHSLFLTDLY KERKLLSAEE RISQTVEILK HTVDIEEKGV KLKLTIVDTP GFGDAVNNSE
CWKPITDYVD QQFEQYFRDE SGLNRKNIQD NRVHCCLYFI SPFGHGLRPV DVGFMKALHE
KVNIVPLIAK ADCLVPGEIR KLKERIREEI DKFGIHVYQF PECDSDEDED FKQQDRELKE
SAPFAVIGSN TVVEAKGQRV RGRLYPWGIV EVENQAHCDF VKLRNMLIRT HMHDLKDVTC
DVHYENYRAH CIQQMTSKLT QDSRMESPIP ILPLPTPDAE TEKLIRMKDE ELRRMQEMLQ
KMKQQMQDQ
