ID A0A2I3G9P0_NOMLE Unreviewed; 441 AA.
AC A0A2I3G9P0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN Name=SEPTIN8 {ECO:0000313|Ensembl:ENSNLEP00000028008.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000028008.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000028008.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000028008.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; ADFV01188462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01188463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3G9P0; -.
DR Ensembl; ENSNLET00000043128.1; ENSNLEP00000028008.1; ENSNLEG00000008147.3.
DR GeneTree; ENSGT00940000156068; -.
DR Proteomes; UP000001073; Chromosome 2.
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:UP000001073}.
FT DOMAIN 40..306
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 376..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 51088 MW; 072922805C00585B CRC64;
EFKTDLANIN AEPEPRSLSL GGHVGFDSLP DQLVSKSVTQ GFSFNILCVG ETGIGKSTLM
NTLFNTTFET EEASHHEACV RLRPQTYDLQ ESNVQLKLTI VDAVGFGDQI NKDESYRPIV
DYIDAQFENY LQEELKIRRS LFDYHDTRIH VCLYFITPTG HSLKSLDLVT MKKLDSKVNI
IPIIAKADTI SKSELHKFKI KIMGELVSNG VQIYQFPTDD EAVAEINAVM NAHLPFAVVG
STEEVKVGNK LVRARQYPWG VVQVENENHC DFVKLREMLI RVNMEDLREQ THSRHYELYR
RCKLEEMGFQ DSDGDSQPFS LQETYEAKRK EFLSELQRKE EEMRQMFVNK VKETELELKE
KERELHEKFE HLKRVHQEEK RKVEEKRREL EEETNAFNRR KAAVEALQSQ ALHATSQQPL
RKDKDKKKAS GWSSIYSVTI P
//
