ID A0A2K6SNK9_SAIBB Unreviewed; 478 AA.
AC A0A2K6SNK9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN Name=SEPTIN8 {ECO:0000313|Ensembl:ENSSBOP00000008961.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000008961.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000008961.1}
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: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000256|ARBA:ARBA00004432}. Presynapse
CC {ECO:0000256|ARBA:ARBA00034106}.
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; A0A2K6SNK9; -.
DR STRING; 39432.ENSSBOP00000008961; -.
DR Ensembl; ENSSBOT00000025723.1; ENSSBOP00000008961.1; ENSSBOG00000021236.1.
DR GeneTree; ENSGT00940000156068; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0030672; C:synaptic vesicle membrane; 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:SF54; SEPTIN-8; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR006698};
KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR006698};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU004560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004560};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220}.
FT DOMAIN 36..302
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 407..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 318..403
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 414..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 55211 MW; 3E9490F6B91EBFED CRC64;
MISFLNAEAE PRSLSLGGHV GFDSLPDQLV SKSVTQGFSF NILCVGETGI GKSTLMNTLF
NTNFETEEAS HHEACVRLRP QTYDLQESNV QLKLTIVDAV GFGDQINKDE SYRPIVDYID
AQFENYLQEE LKIRRSLFDY HDTRIHVCLY FITPTGHSLK SLDLVTMKKL DSKVNIIPII
AKADTISKSE LHKFKIKIMG ELVSNGVQIY QFPTDDEAVA EINAVMNAHL PFAVVGSTEE
VKVGNKLVRA RQYPWGVVQV ENENHCDFVK LREMLIRVNM EDLREQTHSR HYELYRRCKL
EEMGFQDSDG DSQPFSLQET YEAKRKEFLS ELQRKEEEMR QMFVNKVKET ELELKEKERE
LHEKFEHLKR VHQEEKRKVE EKRHELEEET NAFNRRKAAV EALQSQALHA TSQQPLRKDK
DKKNRSDIGA HQSGMSLSNS KVMMTKASVE PLNCSSWWPA IQCCSCLVRD ATWREGFL
//
