SEPT8_RHIFE
ID SEPT8_RHIFE Reviewed; 429 AA.
AC B2KIE9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Septin-8;
GN Name=SEPTIN8 {ECO:0000250|UniProtKB:Q92599}; Synonyms=SEPT8;
OS Rhinolophus ferrumequinum (Greater horseshoe bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC Rhinolophinae; Rhinolophus.
OX NCBI_TaxID=59479;
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 (APR-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; DP000722; ACC68857.1; -; Genomic_DNA.
DR AlphaFoldDB; B2KIE9; -.
DR SMR; B2KIE9; -.
DR Proteomes; UP000472240; 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..429
FT /note="Septin-8"
FT /id="PRO_0000363228"
FT DOMAIN 41..307
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 376..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 322..410
FT /evidence="ECO:0000255"
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 429 AA; 49872 MW; EF243CAF6BF1FFF0 CRC64;
MAATDLERFS NAEPEPRSLS LGGHVGFDSL PDQLVSKSVT QGFSFNILCV GETGIGKSTL
MNTLFNTTFE TEEASHHEEC VRLRPQTYDL QESNVQLKLT IVDAVGFGDQ INKDESYRPI
VDYIDAQFES YLQEELKIRR SLFDYHDTRV 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 QALHATLQQP
LRKDKDKKK
