SEPT5_MOUSE
ID SEPT5_MOUSE Reviewed; 369 AA.
AC Q9Z2Q6; B2RUC5; Q3UYG4; Q6PB74;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 166.
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:0000312|MGI:MGI:1195461};
GN Synonyms=Pnutl1 {ECO:0000312|MGI:MGI:1195461},
GN Sept5 {ECO:0000312|MGI:MGI:1195461};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-369.
RC STRAIN=C57BL/6J; TISSUE=Brain, Cartilage, and Skin;
RA Botta A., Lindsay E.A., Jurecic V., Zieger B., Ware J., Baldini A.;
RT "CDCREL-1, a septin deleted in DiGeorge Syndrome, is expressed in the
RT developing brain and cartilage primordia in mouse embryogenesis.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 23-36; 58-71; 82-90; 182-190; 240-256; 264-282 AND
RP 297-308, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH PRKN, AND UBIQUITIN-MEDIATED DEGRADATION.
RX PubMed=11078524; DOI=10.1073/pnas.240347797;
RA Zhang Y., Gao J., Chung K.K.K., Huang H., Dawson V.L., Dawson T.M.;
RT "Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes
RT the degradation of the synaptic vesicle-associated protein, CDCrel-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13354-13359(2000).
RN [6]
RP INTERACTION WITH SEPTIN2 AND SEPTIN7, LACK OF INTERACTION WITH SEPTIN4,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11739749; DOI=10.1128/mcb.22.1.378-387.2002;
RA Peng X.-R., Jia Z., Zhang Y., Ware J., Trimble W.S.;
RT "The septin CDCrel-1 is dispensable for normal development and
RT neurotransmitter release.";
RL Mol. Cell. Biol. 22:378-387(2002).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11880646; DOI=10.1073/pnas.052715199;
RA Dent J., Kato K., Peng X.-R., Martinez C., Cattaneo M., Poujol C.,
RA Nurden P., Nurden A., Trimble W.S., Ware J.;
RT "A prototypic platelet septin and its participation in secretion.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:3064-3069(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND THR-336, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [10]
RP INTERACTION WITH STX1A.
RX PubMed=17296554; DOI=10.1016/j.neuron.2007.01.019;
RA Ihara M., Yamasaki N., Hagiwara A., Tanigaki A., Kitano A., Hikawa R.,
RA Tomimoto H., Noda M., Takanashi M., Mori H., Hattori N., Miyakawa T.,
RA Kinoshita M.;
RT "Sept4, a component of presynaptic scaffold and Lewy bodies, is required
RT for the suppression of alpha-synuclein neurotoxicity.";
RL Neuron 53:519-533(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [12]
RP INTERACTION WITH DYRK1A, AND PHOSPHORYLATION.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-225; SER-327 AND
RP THR-336, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-168, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity).
CC Involved in cytokinesis (Potential). May play a role in platelet
CC secretion. {ECO:0000250, ECO:0000269|PubMed:11880646, 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). Interacts with SEPTIN2 and SEPTIN5.
CC Interaction with SEPTIN4 not detected. In platelets, associated with a
CC complex containing STX4 (By similarity). Interacts with PRKN; this
CC interaction leads to SEPTIN5 ubiquitination and degradation
CC (PubMed:11078524). Interacts with DYRK1A (PubMed:18938227). Interacts
CC with STX1A; in the cerebellar cortex (PubMed:17296554). {ECO:0000250,
CC ECO:0000269|PubMed:11078524, ECO:0000269|PubMed:11739749,
CC ECO:0000269|PubMed:17296554, ECO:0000269|PubMed:18938227}.
CC -!- INTERACTION:
CC Q9Z2Q6; O60260: PRKN; Xeno; NbExp=2; IntAct=EBI-772125, EBI-716346;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Detected at 17 dpc in the brain. Expression
CC increases during postnatal life and reaches a plateau at approximately
CC P10 (at protein level). {ECO:0000269|PubMed:11739749}.
CC -!- PTM: Phosphorylated by DYRK1A. {ECO:0000269|PubMed:18938227}.
CC -!- DISRUPTION PHENOTYPE: Mice have a normal life-span and show no apparent
CC abnormalities, including synaptic properties and hippocampal neuron
CC growth. In platelets, hyperresponsive degranulation phenotype.
CC {ECO:0000269|PubMed:11739749, ECO:0000269|PubMed:11880646}.
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; AK134700; BAE22248.1; -; mRNA.
DR EMBL; BC059848; AAH59848.1; -; mRNA.
DR EMBL; BC141073; AAI41074.1; -; mRNA.
DR EMBL; BC145331; AAI45332.1; -; mRNA.
DR EMBL; AF033350; AAC83974.1; -; mRNA.
DR CCDS; CCDS57021.1; -.
DR RefSeq; NP_998779.2; NM_213614.2.
DR AlphaFoldDB; Q9Z2Q6; -.
DR SMR; Q9Z2Q6; -.
DR BioGRID; 202285; 16.
DR IntAct; Q9Z2Q6; 7.
DR MINT; Q9Z2Q6; -.
DR STRING; 10090.ENSMUSP00000094750; -.
DR iPTMnet; Q9Z2Q6; -.
DR PhosphoSitePlus; Q9Z2Q6; -.
DR SwissPalm; Q9Z2Q6; -.
DR EPD; Q9Z2Q6; -.
DR jPOST; Q9Z2Q6; -.
DR MaxQB; Q9Z2Q6; -.
DR PaxDb; Q9Z2Q6; -.
DR PeptideAtlas; Q9Z2Q6; -.
DR PRIDE; Q9Z2Q6; -.
DR ProteomicsDB; 261155; -.
DR DNASU; 18951; -.
DR Ensembl; ENSMUST00000096987; ENSMUSP00000094750; ENSMUSG00000072214.
DR GeneID; 18951; -.
DR KEGG; mmu:18951; -.
DR UCSC; uc007yoj.1; mouse.
DR CTD; 5413; -.
DR MGI; MGI:1195461; Septin5.
DR VEuPathDB; HostDB:ENSMUSG00000072214; -.
DR eggNOG; KOG2655; Eukaryota.
DR GeneTree; ENSGT00940000159913; -.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; Q9Z2Q6; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q9Z2Q6; -.
DR TreeFam; TF101079; -.
DR BioGRID-ORCS; 18951; 0 hits in 49 CRISPR screens.
DR PRO; PR:Q9Z2Q6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9Z2Q6; protein.
DR Bgee; ENSMUSG00000072214; Expressed in superior frontal gyrus and 122 other tissues.
DR ExpressionAtlas; Q9Z2Q6; baseline and differential.
DR Genevisible; Q9Z2Q6; MM.
DR GO; GO:0043679; C:axon terminus; IDA:MGI.
DR GO; GO:0044305; C:calyx of Held; IDA:SynGO.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; ISO:MGI.
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; IDA:UniProtKB.
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; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; IDA:MGI.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0030534; P:adult behavior; IMP:UniProtKB.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; ISS:UniProtKB.
DR GO; GO:0099148; P:regulation of synaptic vesicle docking; IDA:SynGO.
DR GO; GO:0035176; P:social behavior; IMP: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; IPR030647; SEPT5.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884:SF68; PTHR18884:SF68; 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 Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; GTP-binding; Methylation; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..369
FT /note="Septin-5"
FT /id="PRO_0000173523"
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:21183079"
FT MOD_RES 168
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 369 AA; 42748 MW; D58468DBA9ADE626 CRC64;
MSTGLRYKSK LATPEDKQDI DKQYVGFATL PNQVHRKSVK KGFDFTLMVA GESGLGKSTL
VHSLFLTDLY KDRKLLSAEE RINQTVEILK HTVDIEEKGV KLKLTIVDTP GFGDAVNNSE
CWKPITDYVD QQFEQYFRDE SGLNRKNIQD NRVHCCLYFI SPFGHGLRPV DVGFMKALHE
KVNIVPLIAK ADCLVPSEIR KLKDRIREEI DKFGIHVYQF PECDSDEDED FKQQDRELKE
SAPFAVIGSN TVVEAKGQRV RGRLYPWGIV EVENQAHCDF VKLRNMLIRT HMHDLKDVTC
DVHYENYRAH CIQQMTSKLT QDSRMESPIP ILPLPTPDAE TEKLIRMKDE ELRRMQEMLQ
KMKQQMQDQ
