ID   SEPT5_RAT               Reviewed;         369 AA.
AC   Q9JJM9; Q8R2F7; Q9JJM8;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   24-JAN-2024, entry version 130.
DE   RecName: Full=Septin-5;
DE   AltName: Full=Cell division control-related protein 1;
DE            Short=CDCrel-1;
DE   AltName: Full=Peanut-like protein 1;
GN   Name=Septin5 {ECO:0000250|UniProtKB:Q99719};
GN   Synonyms=Pnutl1, Sept5 {ECO:0000312|RGD:621763};
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), AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar; TISSUE=Neonatal brain;
RX   PubMed=10873671; DOI=10.1006/bbrc.2000.3003;
RA   Tada S., Kajii Y., Sato M., Nishikawa T.;
RT   "Reciprocal expression of infant- and adult preferring transcripts of
RT   CDCrel-1 septin in the rat neocortex.";
RL   Biochem. Biophys. Res. Commun. 273:723-728(2000).
RN   [2]
RP   PROTEIN SEQUENCE OF 23-36 AND 297-308, 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   INTERACTION WITH DYRK1A.
RX   PubMed=18938227; DOI=10.1016/j.neuroscience.2008.09.034;
RA   Sitz J.H., Baumgaertel K., Haemmerle B., Papadopoulos C., Hekerman P.,
RA   Tejedor F.J., Becker W., Lutz B.;
RT   "The Down syndrome candidate dual-specificity tyrosine phosphorylation-
RT   regulated kinase 1A phosphorylates the neurodegeneration-related septin
RT   4.";
RL   Neuroscience 157:596-605(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13 AND SER-225, AND
RP   IDENTIFICATION BY 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 cytokinesis (Potential). May play a role in platelet
CC       secretion (By similarity). {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. Interacts with SEPTIN2 and SEPTIN5. In platelets, associated
CC       with a complex containing STX4. Interacts with PRKN; this interaction
CC       leads to SEPTIN5 ubiquitination and degradation (By similarity).
CC       Interacts with DYRK1A (PubMed:18938227). Interacts with STX1A; in the
CC       cerebellar cortex (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q9Z2Q6, ECO:0000269|PubMed:18938227}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=CDCrel-1F;
CC         IsoId=Q9JJM9-1; Sequence=Displayed;
CC       Name=2; Synonyms=CDCrel-1A;
CC         IsoId=Q9JJM9-2; Sequence=VSP_016539;
CC       Name=3; Synonyms=CDCrel-1AI;
CC         IsoId=Q9JJM9-3; Sequence=VSP_016540, VSP_016541;
CC   -!- TISSUE SPECIFICITY: Expressed in brain and testis and at lower level in
CC       heart, spleen, lung and kidney. {ECO:0000269|PubMed:10873671}.
CC   -!- PTM: Phosphorylated by DYRK1A. {ECO:0000250|UniProtKB:Q9Z2Q6}.
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; AB027143; BAA98051.1; -; mRNA.
DR   EMBL; AB027144; BAB87114.1; -; mRNA.
DR   EMBL; AB027145; BAA98052.1; -; mRNA.
DR   AlphaFoldDB; Q9JJM9; -.
DR   SMR; Q9JJM9; -.
DR   BioGRID; 250595; 6.
DR   IntAct; Q9JJM9; 4.
DR   MINT; Q9JJM9; -.
DR   STRING; 10116.ENSRNOP00000039995; -.
DR   GlyGen; Q9JJM9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9JJM9; -.
DR   PhosphoSitePlus; Q9JJM9; -.
DR   jPOST; Q9JJM9; -.
DR   PaxDb; 10116-ENSRNOP00000039995; -.
DR   AGR; RGD:621763; -.
DR   RGD; 621763; Septin5.
DR   eggNOG; KOG2655; Eukaryota.
DR   InParanoid; Q9JJM9; -.
DR   PRO; PR:Q9JJM9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0043679; C:axon terminus; ISO:RGD.
DR   GO; GO:0044305; C:calyx of Held; ISO:RGD.
DR   GO; GO:0005938; C:cell cortex; ISO:RGD.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0098793; C:presynapse; ISO:RGD.
DR   GO; GO:0031105; C:septin complex; IDA:UniProtKB.
DR   GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR   GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR   GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR   GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
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:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0019905; F:syntaxin binding; IDA:RGD.
DR   GO; GO:0030534; P:adult behavior; ISS:UniProtKB.
DR   GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR   GO; GO:0045921; P:positive regulation of exocytosis; IMP:RGD.
DR   GO; GO:0017157; P:regulation of exocytosis; ISS:UniProtKB.
DR   GO; GO:0099148; P:regulation of synaptic vesicle docking; ISO:RGD.
DR   GO; GO:0035176; P:social behavior; 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:SF68; SEPTIN-5; 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   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; GTP-binding; Methylation;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..369
FT                   /note="Septin-5"
FT                   /id="PRO_0000173524"
FT   DOMAIN          41..314
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          51..58
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          108..111
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   REGION          189..192
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT   COILED          338..369
FT                   /evidence="ECO:0000255"
FT   BINDING         51..58
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         190..198
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         248
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         13
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         168
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2Q6"
FT   MOD_RES         225
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         327
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99719"
FT   MOD_RES         336
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2Q6"
FT   VAR_SEQ         1..18
FT                   /note="MSTGLRYKSKLATPEDKQ -> MDSLAAPQDRLVEQLLSPRTQAQRRLK
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10873671"
FT                   /id="VSP_016539"
FT   VAR_SEQ         352..356
FT                   /note="LRRMQ -> GRAGR (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10873671"
FT                   /id="VSP_016540"
FT   VAR_SEQ         357..369
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10873671"
FT                   /id="VSP_016541"
SQ   SEQUENCE   369 AA;  42852 MW;  FBE46DDAAB7DFC77 CRC64;
     MSTGLRYKSK LATPEDKQDI DKQYVGFATL PNQVHRKSVK KGFDFTLMVA GESGLGKSTL
     VHSLFLTDLY KDRKLLSAEE RINQTVEILK HTVDIEEKGV KLKLTIVDTP GFGDAVNNFE
     CWKPITDYVD QQFEQYFRDE SGLNRKNIQD NRVHCCLYFI SPFGHGLRPV DVGFMKALHE
     KVNIVPLIAK ADCLVPSEIR KLKDRIREEI DKFGIHVYQF PECDSDEDED FKQQDRELKE
     SAPFAVIGSN TVVEAKGQRV RGRLYPWGIV EVENQAHCDF VKLRNMLIRT HMHDLKDVTC
     DVHYENYRAH CIQQMTSKLT QDSRMESPIP ILPLPTPDSE TEKLIRMKDE ELRRMQEMLQ
     KMKQRMQDQ
//