SEPT3_MOUSE
ID SEPT3_MOUSE Reviewed; 350 AA.
AC Q9Z1S5; Q3TNZ2; Q7TNT7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Neuronal-specific septin-3;
GN Name=Septin3 {ECO:0000303|PubMed:10446280};
GN Synonyms=Sep3 {ECO:0000303|PubMed:10446280},
GN Sept3 {ECO:0000312|MGI:MGI:1345148};
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 [MRNA] (ISOFORM 2).
RX PubMed=10446280; DOI=10.1016/s0925-4773(99)00113-6;
RA Xiong J.-W., Leahy A., Stuhlmann H.;
RT "Retroviral promoter-trap insertion into a novel mammalian septin gene
RT expressed during mouse neuronal development.";
RL Mech. Dev. 86:183-191(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Spinal ganglion;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP PROTEIN SEQUENCE OF 132-139; 186-204 AND 314-325, AND IDENTIFICATION BY
RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20181826; DOI=10.1091/mbc.e09-10-0869;
RA Shinoda T., Ito H., Sudo K., Iwamoto I., Morishita R., Nagata K.;
RT "Septin 14 is involved in cortical neuronal migration via interaction with
RT Septin 4.";
RL Mol. Biol. Cell 21:1324-1334(2010).
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. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Synapse {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z1S5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z1S5-2; Sequence=VSP_025400;
CC -!- TISSUE SPECIFICITY: Expressed in the brain including the cerebrum,
CC hippocampus and cerebellum (at protein level).
CC {ECO:0000269|PubMed:20181826}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the cerebral cortex from 13.5 dpc to
CC P30, expression peaks at P15. {ECO:0000269|PubMed:20181826}.
CC -!- PTM: Phosphorylated by PKG on serine residues. Phosphorylated by PKG on
CC Ser-91 (By similarity). {ECO:0000250}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAD02884.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF104411; AAD02884.1; ALT_FRAME; mRNA.
DR EMBL; AK164861; BAE37945.1; -; mRNA.
DR EMBL; AK169916; BAE41456.1; -; mRNA.
DR EMBL; AK141915; BAE24884.1; -; mRNA.
DR EMBL; BC055738; AAH55738.1; -; mRNA.
DR CCDS; CCDS37157.1; -. [Q9Z1S5-2]
DR RefSeq; NP_036019.2; NM_011889.2. [Q9Z1S5-2]
DR AlphaFoldDB; Q9Z1S5; -.
DR SMR; Q9Z1S5; -.
DR BioGRID; 204863; 13.
DR IntAct; Q9Z1S5; 4.
DR STRING; 10090.ENSMUSP00000023095; -.
DR iPTMnet; Q9Z1S5; -.
DR PhosphoSitePlus; Q9Z1S5; -.
DR UCD-2DPAGE; Q9Z1S5; -.
DR MaxQB; Q9Z1S5; -.
DR PaxDb; Q9Z1S5; -.
DR PeptideAtlas; Q9Z1S5; -.
DR PRIDE; Q9Z1S5; -.
DR ProteomicsDB; 255380; -. [Q9Z1S5-1]
DR ProteomicsDB; 255381; -. [Q9Z1S5-2]
DR Antibodypedia; 290; 266 antibodies from 33 providers.
DR DNASU; 24050; -.
DR Ensembl; ENSMUST00000023095; ENSMUSP00000023095; ENSMUSG00000022456. [Q9Z1S5-2]
DR Ensembl; ENSMUST00000116423; ENSMUSP00000112124; ENSMUSG00000022456. [Q9Z1S5-2]
DR GeneID; 24050; -.
DR KEGG; mmu:24050; -.
DR UCSC; uc007wyq.1; mouse. [Q9Z1S5-1]
DR CTD; 55964; -.
DR MGI; MGI:1345148; Septin3.
DR VEuPathDB; HostDB:ENSMUSG00000022456; -.
DR eggNOG; KOG1547; Eukaryota.
DR GeneTree; ENSGT00940000158004; -.
DR HOGENOM; CLU_017718_7_1_1; -.
DR InParanoid; Q9Z1S5; -.
DR OMA; QCEFVYL; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q9Z1S5; -.
DR TreeFam; TF101078; -.
DR BioGRID-ORCS; 24050; 5 hits in 51 CRISPR screens.
DR ChiTaRS; Sept3; mouse.
DR PRO; PR:Q9Z1S5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9Z1S5; protein.
DR Bgee; ENSMUSG00000022456; Expressed in cortical plate and 204 other tissues.
DR ExpressionAtlas; Q9Z1S5; baseline and differential.
DR Genevisible; Q9Z1S5; MM.
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; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0098793; C:presynapse; IDA:UniProtKB.
DR GO; GO:0099569; C:presynaptic cytoskeleton; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0031105; C:septin complex; IDA:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
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: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; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Synapse.
FT CHAIN 1..350
FT /note="Neuronal-specific septin-3"
FT /id="PRO_0000173518"
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 REGION 328..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:Q9WU34"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10446280,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025400"
FT CONFLICT 221..235
FT /note="KQRVRKELEVNGIEF -> LPSEGI (in Ref. 1; AAD02884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 40038 MW; AEF37C023AB21C0D CRC64;
MSKGLPEART DAAMSELVPE PRPKPAVPMK PVSINSNLLG YIGIDTIIEQ MRKKTMKTGF
DFNIMVVGQS GLGKSTLVNT LFKSQVSRKA SSWNREEKIP KTVEIKAIGH VIEEGGVKMK
LTVIDTPGFG DQINNENCWE PIEKYINEQY EKFLKEEVNI ARKKRIPDTR VHCCLYFISP
TGHSLRPLDL EFMKHLSKVV NIIPVIAKAD TMTLEEKSEF KQRVRKELEV NGIEFYPQKE
FDEDLEDKTE NDKIRQESMP FAVVGSDKEY QVNGKRVLGR KTPWGIIEVE NLNHCEFALL
RDFVIRTHLQ DLKEVTHNIH YETYRAKRLN DNGGLPPVSV DTEESHDSNP
