SEPT5_MACFA
ID SEPT5_MACFA Reviewed; 378 AA.
AC Q9BGQ3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Septin-5;
GN Name=SEPTIN5 {ECO:0000250|UniProtKB:Q99719}; Synonyms=SEPT5;
GN ORFNames=QflA-14636;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (FEB-2001) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB056419; BAB33077.1; -; mRNA.
DR AlphaFoldDB; Q9BGQ3; -.
DR SMR; Q9BGQ3; -.
DR STRING; 9541.XP_005568030.1; -.
DR eggNOG; KOG2655; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0031105; C:septin complex; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030534; P:adult behavior; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0017157; P:regulation of exocytosis; ISS:UniProtKB.
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..378
FT /note="Septin-5"
FT /id="PRO_0000173522"
FT DOMAIN 50..323
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 60..67
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 117..120
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 198..201
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT COILED 347..378
FT /evidence="ECO:0000255"
FT BINDING 60..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 199..207
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 177
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Q6"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99719"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99719"
FT MOD_RES 345
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Q6"
SQ SEQUENCE 378 AA; 43846 MW; 09973C9F4545BB0D CRC64;
MDSLAAPQDR LVEQLLSPRT QAQRRLKDID KQYVGFATLP NQVHRKSVKK GFDFTLMVAG
ESGLGKSTLV HSLFLTDLYK DRKLLSAEER ISQTVEILKH TVDIEEKGVK LKLTIVDTPG
FGDAVDNTEC WKPITDYVDQ QFEQYFRDES GLNRKNIQDN RVHCCLYFIS PFGHGLRPVD
VGFMKALHEK VNIVPLIAKA DCLVPSEIRK LKERIREEID KFGIHVYQFP ECDSDEDEDF
KQQDRELKES APFAVIGSNT VVEAKGQRVR GRLYPWGIVE VENQAHCDFV KLRNMLIRTH
MHDLKDVTCD VHYENYRAHC IQQMTSKLTQ DSRMESPIPI LPLPTPDAET EKLIRMKDEE
LRRMQEMLQR MKQQMQDQ
