ID SEPT8_BOVIN Reviewed; 442 AA.
AC Q0VCP4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 3.
DT 24-JAN-2024, entry version 106.
DE RecName: Full=Septin-8;
GN Name=SEPTIN8 {ECO:0000250|UniProtKB:Q92599}; Synonyms=SEPT8;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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; BC120074; AAI20075.1; -; mRNA.
DR RefSeq; NP_001069698.1; NM_001076230.2.
DR AlphaFoldDB; Q0VCP4; -.
DR SMR; Q0VCP4; -.
DR STRING; 9913.ENSBTAP00000058319; -.
DR PaxDb; 9913-ENSBTAP00000011359; -.
DR Ensembl; ENSBTAT00000011359.4; ENSBTAP00000011359.3; ENSBTAG00000008609.6.
DR GeneID; 540614; -.
DR KEGG; bta:540614; -.
DR CTD; 23176; -.
DR VEuPathDB; HostDB:ENSBTAG00000008609; -.
DR VGNC; VGNC:34458; SEPTIN8.
DR eggNOG; KOG3859; Eukaryota.
DR GeneTree; ENSGT00940000156068; -.
DR HOGENOM; CLU_017718_8_1_1; -.
DR InParanoid; Q0VCP4; -.
DR TreeFam; TF101080; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000008609; Expressed in hypothalamus and 103 other cell types or tissues.
DR ExpressionAtlas; Q0VCP4; baseline.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
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; 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 2: Evidence at transcript level;
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_0000270223"
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 379..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 320..413
FT /evidence="ECO:0000255"
FT COMPBIAS 379..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; 51250 MW; 409516F64066A37E CRC64;
MAATDLERFS NAEPEPRSLS LGGHVGFDSL PDQLVSKSVT QGFSFNILCV GETGIGKSTL
MNTLFNTTFE TEEASHHEEC 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 EHLKRLHQEE KRKVEEKRRE LEEETNAFNR RKAAVEALQS QALHATSQQP
LRKDKDKKKA SGWSSIYSVT IP
//
