ID   SEPT8_CALJA             Reviewed;         442 AA.
AC   B0KWP7;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Septin-8;
GN   Name=SEPTIN8 {ECO:0000250|UniProtKB:Q92599}; Synonyms=SEPT8;
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA   Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA   Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA   Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA   Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA   Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA   Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA   Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA   Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA   Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT   "NISC comparative sequencing initiative.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May
CC       play a role in platelet secretion (By similarity). Seems to participate
CC       in the process of SNARE complex formation in synaptic vesicles (By
CC       similarity). {ECO:0000250|UniProtKB:B0BNF1,
CC       ECO:0000250|UniProtKB:Q92599}.
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 (By similarity). Interacts with CDK14, SEPTIN4, SEPTIN5 and
CC       SEPTIN7 (By similarity). Interacts with VAMP2; the interaction inhibits
CC       interaction of VAMP2 with SYP (By similarity). Interacts with STX1A (By
CC       similarity). {ECO:0000250|UniProtKB:B0BNF1,
CC       ECO:0000250|UniProtKB:Q8CHH9, ECO:0000250|UniProtKB:Q92599}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0BNF1}.
CC       Cytoplasm, cytoskeleton {ECO:0000250}. Synapse
CC       {ECO:0000250|UniProtKB:B0BNF1}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:B0BNF1}. Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane {ECO:0000250|UniProtKB:B0BNF1}. Presynapse
CC       {ECO:0000250|UniProtKB:B0BNF1}. Note=Expressed in axons of immature
CC       neurons, localizes to synapses in mature neurons.
CC       {ECO:0000250|UniProtKB:B0BNF1}.
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}.
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DR   EMBL; DP000584; ABZ10527.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0KWP7; -.
DR   SMR; B0KWP7; -.
DR   STRING; 9483.ENSCJAP00000027173; -.
DR   eggNOG; KOG3859; Eukaryota.
DR   InParanoid; B0KWP7; -.
DR   Proteomes; UP000008225; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0033157; P:regulation of intracellular protein transport; ISS:UniProtKB.
DR   GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR   GO; GO:0035542; P:regulation of SNARE complex assembly; 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; IPR030646; SEPT8.
DR   InterPro; IPR016491; Septin.
DR   PANTHER; PTHR18884:SF54; PTHR18884:SF54; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51719; G_SEPTIN; 1.
PE   3: Inferred from homology;
KW   Acetylation; Cell projection; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW   Cytoskeleton; GTP-binding; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Synapse.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q92599"
FT   CHAIN           2..442
FT                   /note="Septin-8"
FT                   /id="PRO_0000363225"
FT   DOMAIN          41..307
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          51..58
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          103..106
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          186..189
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          377..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          322..410
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        377..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         51..58
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         187..195
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92599"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92599"
SQ   SEQUENCE   442 AA;  51152 MW;  BB23DEA3FE1019F7 CRC64;
     MAATDLERFS NAEAEPRSLS 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
     LRKDKDKKKA SGWSSIYSVT IP