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}.
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; 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
//
