SEPT3_RAT
ID SEPT3_RAT Reviewed; 358 AA.
AC Q9WU34; Q9R245; Q9WU35;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Neuronal-specific septin-3;
DE AltName: Full=G-septin;
DE AltName: Full=P40;
GN Name=Septin3 {ECO:0000250|UniProtKB:Q9UH03};
GN Synonyms=Sept3 {ECO:0000312|RGD:621745};
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), PROTEIN SEQUENCE OF 60-74
RP AND 314-325, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10744683; DOI=10.1074/jbc.275.14.10047;
RA Xue J., Wang X., Malladi C.S., Kinoshita M., Milburn P.J., Lengyel I.,
RA Rostas J.A., Robinson P.J.;
RT "Phosphorylation of a new brain-specific septin, G-septin, by cGMP-
RT dependent protein kinase.";
RL J. Biol. Chem. 275:10047-10056(2000).
RN [2]
RP PROTEIN SEQUENCE OF 58-74; 227-239 AND 314-325, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION AT SER-91, AND MUTAGENESIS OF SER-91 AND SER-92.
RX PubMed=15107017; DOI=10.1042/bj20040455;
RA Xue J., Milburn P.J., Hanna B.T., Graham M.E., Rostas J.A., Robinson P.J.;
RT "Phosphorylation of septin 3 on Ser-91 by cGMP-dependent protein kinase-I
RT in nerve terminals.";
RL Biochem. J. 381:753-760(2004).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15485489; DOI=10.1111/j.1471-4159.2004.02755.x;
RA Xue J., Tsang C.W., Gai W.-P., Malladi C.S., Trimble W.S., Rostas J.A.P.,
RA Robinson P.J.;
RT "Septin 3 (G-septin) is a developmentally regulated phosphoprotein enriched
RT in presynaptic nerve terminals.";
RL J. Neurochem. 91:579-590(2004).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May
CC play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}.
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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15485489}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Synapse
CC {ECO:0000269|PubMed:15485489}. Note=In cultured hippocampal neurons,
CC predominantly localized to presynaptic terminals.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=G-septin-alpha;
CC IsoId=Q9WU34-1; Sequence=Displayed;
CC Name=2; Synonyms=G-septin-beta;
CC IsoId=Q9WU34-2; Sequence=VSP_025401, VSP_025404;
CC Name=3; Synonyms=G-septin-gamma;
CC IsoId=Q9WU34-3; Sequence=VSP_025402, VSP_025403;
CC -!- TISSUE SPECIFICITY: Brain-specific, with highest expression in the
CC hippocampal CA3 region (at protein level).
CC {ECO:0000269|PubMed:10744683, ECO:0000269|PubMed:15485489}.
CC -!- DEVELOPMENTAL STAGE: First expressed in the embryonic brain from E18.
CC Levels increase during brain development until P7 and remain constant
CC until P35. Further increase in adult brain (at protein level).
CC {ECO:0000269|PubMed:15485489}.
CC -!- PTM: Phosphorylated by PKG on serine residues. Phosphorylated by PKG on
CC Ser-91. {ECO:0000269|PubMed:10744683, ECO:0000269|PubMed:15107017}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF111179; AAD21035.1; -; mRNA.
DR EMBL; AF111180; AAD21036.1; -; mRNA.
DR EMBL; AF111181; AAD21037.1; -; mRNA.
DR RefSeq; NP_062248.1; NM_019375.1.
DR AlphaFoldDB; Q9WU34; -.
DR SMR; Q9WU34; -.
DR BioGRID; 248552; 2.
DR IntAct; Q9WU34; 3.
DR MINT; Q9WU34; -.
DR STRING; 10116.ENSRNOP00000010491; -.
DR iPTMnet; Q9WU34; -.
DR PhosphoSitePlus; Q9WU34; -.
DR PaxDb; Q9WU34; -.
DR PRIDE; Q9WU34; -.
DR GeneID; 56003; -.
DR KEGG; rno:56003; -.
DR CTD; 55964; -.
DR RGD; 621745; Sept3.
DR eggNOG; KOG1547; Eukaryota.
DR InParanoid; Q9WU34; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q9WU34; -.
DR PRO; PR:Q9WU34; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0099569; C:presynaptic cytoskeleton; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
DR GO; GO:0031105; C:septin complex; ISS:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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 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; IPR016491; Septin.
DR InterPro; IPR008114; Septin3.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01741; SEPTIN3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW GTP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Synapse.
FT CHAIN 1..358
FT /note="Neuronal-specific septin-3"
FT /id="PRO_0000287229"
FT DOMAIN 58..331
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..75
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 125..128
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 207..210
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT BINDING 68..75
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 102
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 208..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 280
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15107017"
FT VAR_SEQ 1..67
FT /note="MSKGLPEARTDTAMSELVPEPRPKPAVPMKPVSINSNLLGCIGIDTIIEQMR
FT KKTMKTGFDFNIMVV -> MESNCHFPRPLSYLPKRHQFLPDAHSSSSNKAWPGPQLWS
FT SISSQEGSAAQEADVGLSPFLCLPFCAA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10744683"
FT /id="VSP_025401"
FT VAR_SEQ 299..301
FT /note="LLR -> PRA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10744683"
FT /id="VSP_025402"
FT VAR_SEQ 302..358
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10744683"
FT /id="VSP_025403"
FT VAR_SEQ 338..358
FT /note="GEGLLGTVLPPVPATPCPTAE -> VSVDTEESH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10744683"
FT /id="VSP_025404"
FT MUTAGEN 91
FT /note="S->A: Abolishes phosphorylation by PKG."
FT /evidence="ECO:0000269|PubMed:15107017"
FT MUTAGEN 92
FT /note="S->A: Increases phosphorylation by PKG."
FT /evidence="ECO:0000269|PubMed:15107017"
FT CONFLICT 41
FT /note="C -> Y (in Ref. 1; AAD21037)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="V -> I (in Ref. 1; AAD21035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 40598 MW; 96F05B2CFD195599 CRC64;
MSKGLPEART DTAMSELVPE PRPKPAVPMK PVSINSNLLG CIGIDTIIEQ MRKKTMKTGF
DFNIMVVGQS GLGKSTLVNT LFKSQVSRKA SSWNREEKIP KTVEIKAIGH VIEEGGVKMK
LTVIDTPGFG DQINNENCWE PIEKYINEQY EKFLKEEVNI ARKKRIPDTR VHCCLYFISP
TGHSLRPLDL EFMKHLSKVV NVIPVIAKAD TMTLEEKSEF KQRVRKELEV NGIEFYPQKE
FDEDLEDKTE NDKIRQESMP FAVVGSDKEY QVNGKRVLGR KTPWGIIEVE NLNHCEFALL
RDFVIRTHLQ DLKEVTHNIH YETYRAKRLN DNGGLPPGEG LLGTVLPPVP ATPCPTAE
