ID   SEPT8_RAT               Reviewed;         442 AA.
AC   B0BNF1;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Septin-8 {ECO:0000305};
GN   Name=Septin8 {ECO:0000250|UniProtKB:Q92599};
GN   Synonyms=Sept8 {ECO:0000312|RGD:1308449};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAI58797.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:AAI58797.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   INTERACTION WITH SEPTIN7.
RX   PubMed=15485874; DOI=10.1074/jbc.m406153200;
RA   Nagata K., Asano T., Nozawa Y., Inagaki M.;
RT   "Biochemical and cell biological analyses of a mammalian septin complex,
RT   Sept7/9b/11.";
RL   J. Biol. Chem. 279:55895-55904(2004).
RN   [3] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RA   Maurya D.K., Bhargava P.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP   AND INTERACTION WITH STX1A AND VAMP2.
RX   PubMed=19196426; DOI=10.1111/j.1471-4159.2008.05849.x;
RA   Ito H., Atsuzawa K., Morishita R., Usuda N., Sudo K., Iwamoto I.,
RA   Mizutani K., Katoh-Semba R., Nozawa Y., Asano T., Nagata K.;
RT   "Sept8 controls the binding of vesicle-associated membrane protein 2 to
RT   synaptophysin.";
RL   J. Neurochem. 108:867-880(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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
CC       (PubMed:19196426). {ECO:0000250|UniProtKB:Q92599,
CC       ECO:0000269|PubMed:19196426}.
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 SEPTIN7 (PubMed:15485874).
CC       Interacts with CDK14, SEPTIN4 and SEPTIN5 (By similarity). Interacts
CC       with VAMP2; the interaction inhibits interaction of VAMP2 with SYP
CC       (PubMed:19196426). Interacts with STX1A (PubMed:19196426).
CC       {ECO:0000250|UniProtKB:Q8CHH9, ECO:0000250|UniProtKB:Q92599,
CC       ECO:0000269|PubMed:15485874, ECO:0000269|PubMed:19196426}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19196426}.
CC       Cytoplasm, cytoskeleton {ECO:0000250}. Synapse
CC       {ECO:0000269|PubMed:19196426}. Cell projection, axon
CC       {ECO:0000269|PubMed:19196426}. Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane {ECO:0000305|PubMed:19196426}. Presynapse
CC       {ECO:0000269|PubMed:19196426}. Note=Expressed in axons of immature
CC       neurons, localizes to synapses in mature neurons.
CC       {ECO:0000269|PubMed:19196426}.
CC   -!- TISSUE SPECIFICITY: Expressed in cerebrum, hippocampus and cerebellum
CC       (at protein level). Expressed in heart (at protein level).
CC       {ECO:0000269|PubMed:19196426}.
CC   -!- DEVELOPMENTAL STAGE: In brain, expression increases from E12.5 to
CC       adulthood. {ECO:0000269|PubMed:19196426}.
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; BC158796; AAI58797.1; -; mRNA.
DR   AlphaFoldDB; B0BNF1; -.
DR   SMR; B0BNF1; -.
DR   STRING; 10116.ENSRNOP00000063893; -.
DR   iPTMnet; B0BNF1; -.
DR   PhosphoSitePlus; B0BNF1; -.
DR   jPOST; B0BNF1; -.
DR   PaxDb; B0BNF1; -.
DR   PeptideAtlas; B0BNF1; -.
DR   PRIDE; B0BNF1; -.
DR   UCSC; RGD:1308449; rat.
DR   RGD; 1308449; Sept8.
DR   eggNOG; KOG3859; Eukaryota.
DR   InParanoid; B0BNF1; -.
DR   PhylomeDB; B0BNF1; -.
DR   PRO; PR:B0BNF1; -.
DR   Proteomes; UP000002494; Unplaced.
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:0043209; C:myelin sheath; IDA:UniProtKB.
DR   GO; GO:0098793; C:presynapse; IDA:SynGO.
DR   GO; GO:0031105; C:septin complex; ISO:RGD.
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:0000149; F:SNARE binding; IPI:UniProtKB.
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; IDA: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   1: Evidence at protein 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                   /evidence="ECO:0000250|UniProtKB:Q15019"
FT                   /id="PRO_0000365102"
FT   DOMAIN          41..307
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          1..21
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          411..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          322..407
FT                   /evidence="ECO:0000255"
FT   BINDING         51..58
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q15019"
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|UniProtKB:Q15019"
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:0007744|PubMed:22673903"
SQ   SEQUENCE   442 AA;  51252 MW;  2DD4E3F4BC33FDC2 CRC64;
     MAATDLERIS NAEPEPRSLS LGGHVGFDSL PDQLVSKSVT QGFSFNILCV GETGIGKSTL
     MNTFFNTTFE TEEASHHEEC VRLRPQTYDL QESNVHLKLT IVDAVGFGDQ INKDDSYRPI
     VDYIDTQFEN YLQEELKIRR SLFDYHDTRI HVCLYFITPT GHSLKSLDLV TMKKLDSKVN
     IIPIIAKADT ISKSELHKFK IKIMGELVSN GVQIYQFPTD DEAVAEINAV MNAHLPFAVV
     GSTEEVKVGN KLVRARQYPW GVVQVENENH CDFVKLREML IRVNMEDLRE QTHSRHYELY
     RRCKLEEMGF QDSDGDSQPF SLQETYEAKR KEFLSELQRK EEEMRQMFVN KVKETELELK
     EKERELHEKF EHLKRIHQEE KRKVEEKRRE LEEETNAFNC RKAAMEALQS QALHATSQQP
     LRKDKDKKKV GGWSSIYSVT IP