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   03-AUG-2022, entry version 100.
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.ENSBTAP00000011359; -.
DR   PaxDb; Q0VCP4; -.
DR   PRIDE; Q0VCP4; -.
DR   Ensembl; ENSBTAT00000011359; ENSBTAP00000011359; ENSBTAG00000008609.
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   OrthoDB; 845354at2759; -.
DR   TreeFam; TF101080; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000008609; Expressed in hypothalamus and 103 other tissues.
DR   ExpressionAtlas; Q0VCP4; baseline and differential.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0008104; P:protein localization; 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; -; 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   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