SEPT1_BOVIN
ID SEPT1_BOVIN Reviewed; 367 AA.
AC A5PJU9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Septin-1 {ECO:0000305};
GN Name=SEPTIN1 {ECO:0000250|UniProtKB:Q8WYJ6}; Synonyms=SEPT1;
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=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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). Interacts with AURKB (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250}. Midbody {ECO:0000250}. Note=Remains at the
CC centrosomes and the nearby microtubules throughout mitosis. Localizes
CC to the midbody during cytokinesis (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; BC142247; AAI42248.1; -; mRNA.
DR RefSeq; NP_001092417.1; NM_001098947.2.
DR AlphaFoldDB; A5PJU9; -.
DR SMR; A5PJU9; -.
DR STRING; 9913.ENSBTAP00000028271; -.
DR PaxDb; A5PJU9; -.
DR PRIDE; A5PJU9; -.
DR Ensembl; ENSBTAT00000028271; ENSBTAP00000028271; ENSBTAG00000021219.
DR GeneID; 512478; -.
DR KEGG; bta:512478; -.
DR CTD; 1731; -.
DR VEuPathDB; HostDB:ENSBTAG00000021219; -.
DR VGNC; VGNC:34449; SEPTIN1.
DR eggNOG; KOG2655; Eukaryota.
DR GeneTree; ENSGT00940000161794; -.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; A5PJU9; -.
DR OMA; EMKGSIP; -.
DR OrthoDB; 845354at2759; -.
DR TreeFam; TF101079; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000021219; Expressed in thymus and 103 other tissues.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0072687; C:meiotic spindle; IEA:Ensembl.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
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:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0051311; P:meiotic metaphase plate congression; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0007056; P:spindle assembly involved in female meiosis; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..367
FT /note="Septin-1"
FT /id="PRO_0000363218"
FT DOMAIN 22..296
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 32..39
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 89..92
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 170..173
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT BINDING 32..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 171..179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYJ6"
FT MOD_RES 248
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q8WYJ6"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P42209"
FT MOD_RES 307
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q8WYJ6"
FT MOD_RES 315
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q8WYJ6"
SQ SEQUENCE 367 AA; 41983 MW; B19C09A2CC020D54 CRC64;
MDKEYVGFAA LPNQLHRKSV KKGFDFTLMV AGESGLGKST LINSLFLTNL YEDRQIPEAS
ARLTQTLTIE RRGVEIEEGG IKVKLTVVDT PGFGDSVDCS DCWLPVVRFI EEQFEQYLRD
ESGLNRKNIQ DSRVHCCLYF ISPFGRGLRP LDVAFLRAVH EKVNIIPVIG KADALMPKET
QALKQKIREQ LKEEEINIYQ FPECDSDEDE DFKRQDAEMK ESIPFAVVGS CEVVRDGGPR
PVRGRHYSWG TVEVENPHHC DFLNLRRMLV QTHLQDLKEV THDLLYEGYR ARCLQSLARP
GARDRASRSK LSRQSATEIP LPMLPLADTE KLIREKDEEL RRMQEMLEKM QAQMQLSQAQ
GEQSDAL
