ID A0A2K6E0R3_MACNE Unreviewed; 429 AA.
AC A0A2K6E0R3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN Name=SEPTIN8 {ECO:0000313|Ensembl:ENSMNEP00000041754.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000041754.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000041754.1}
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 RefSeq; XP_011714927.1; XM_011716625.1.
DR AlphaFoldDB; A0A2K6E0R3; -.
DR SMR; A0A2K6E0R3; -.
DR Ensembl; ENSMNET00000066253.1; ENSMNEP00000041754.1; ENSMNEG00000043687.1.
DR GeneID; 105467167; -.
DR CTD; 23176; -.
DR GeneTree; ENSGT00940000156068; -.
DR OrthoDB; 5396944at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000043687; Expressed in temporal lobe and 12 other cell types or tissues.
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 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:UP000233120}.
FT DOMAIN 41..307
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 49814 MW; B6900F134CF67474 CRC64;
MAATDLERFS NAEPEPRSLS LGGHVGFDSL PDQLVSKSVT QGFSFNILCV GETGIGKSTL
MNTLFNTTFE TEEASHHEAC VRLRPQTYDL QESNVQLKLT IVDAVGFGDQ INKDESYRPI
VDYIDAQFEN YLQEELKIRR SLFDYHDTRI HVCLYFITPT GHSLKSLDLV TMKKLDSKVN
IIPIIAKADT ISKSELHKFK IKIMGELVSN GVQIYQFPTD DEAVAEINAV MNAHLPFAVV
GSTEEVKVGN KLVRARQYPW GVVQVENENH CDFVKLREML IRVNMEDLRE QTHSRHYELY
RRCKLEEMGF QDSDGDSQPF SLQETYEAKR KEFLSELQRK EEEMRQMFVN KVKETELELK
EKERELHEKF EHLKRVHQEE KRKVEEKRRE LEEETNAFNR RKAAVEALQS QALHATSQQP
LRKDKDKKN
//
