ID A0A2K5WKW7_MACFA Unreviewed; 367 AA.
AC A0A2K5WKW7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN Name=SEPTIN5 {ECO:0000313|Ensembl:ENSMFAP00000037787.2};
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 {ECO:0000313|Ensembl:ENSMFAP00000037787.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000037787.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000037787.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase.
CC {ECO:0000256|PIRNR:PIRNR006698}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments. {ECO:0000256|PIRNR:PIRNR006698}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|PIRNR:PIRNR006698, ECO:0000256|RuleBase:RU004560}.
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DR AlphaFoldDB; A0A2K5WKW7; -.
DR Ensembl; ENSMFAT00000012039.2; ENSMFAP00000037787.2; ENSMFAG00000038117.2.
DR VEuPathDB; HostDB:ENSMFAG00000038117; -.
DR GeneTree; ENSGT00940000159913; -.
DR OrthoDB; 5396944at2759; -.
DR Proteomes; UP000233100; Chromosome 10.
DR Bgee; ENSMFAG00000038117; Expressed in temporal lobe and 12 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
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:SF68; SEPTIN-5; 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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR006698};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR006698-
KW 2}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR006698-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100}.
FT DOMAIN 41..312
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT SITE 161
FT /note="Important for dimerization"
FT /evidence="ECO:0000256|PIRSR:PIRSR006698-2"
SQ SEQUENCE 367 AA; 42503 MW; B15ED0475E75FD49 CRC64;
MSTGLRYKSK LATPEDKQDI DKQYVGFATL PNQVHRKSVK KGFDFTLMVA GESGLGKSTL
VHSLFLTDLY KDRKLLSAEE RISQTVEILK HTVDIEEKGV KLKLTIVDTP GFGDAVNNTE
CWKPITDYVD QQFEQYFRGG LNRKNIQDNR VHCCLYFISP FGHGLRPVDV GFMKALHEKV
NIVPLIAKAD CLVPSEIRKL KERIREEIDK FGIHVYQFPE CDSDEDEDFK QQDRELKESA
PFAVIGSNTV VEAKGQRVRG RLYPWGIVEV ENQAHCDFVK LRNMLIRTHM HDLKDVTCDV
HYENYRAHCI QQMTSKLTQD SRMESPIPIL PLPTPDAETE KLIRMKDEEL RRMQEMLQRM
KQQMQDQ
//
