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   24-JAN-2024, entry version 165.
DE   RecName: Full=Neuronal-specific septin-3;
GN   Name=Septin3 {ECO:0000303|PubMed:10446280};
GN   Synonyms=Sep3 {ECO:0000303|PubMed:10446280}, Sept3
GN   {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; 17.
DR   IntAct; Q9Z1S5; 5.
DR   STRING; 10090.ENSMUSP00000023095; -.
DR   GlyGen; Q9Z1S5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Z1S5; -.
DR   PhosphoSitePlus; Q9Z1S5; -.
DR   SwissPalm; Q9Z1S5; -.
DR   MaxQB; Q9Z1S5; -.
DR   PaxDb; 10090-ENSMUSP00000023095; -.
DR   PeptideAtlas; Q9Z1S5; -.
DR   ProteomicsDB; 255380; -. [Q9Z1S5-1]
DR   ProteomicsDB; 255381; -. [Q9Z1S5-2]
DR   Antibodypedia; 290; 308 antibodies from 33 providers.
DR   DNASU; 24050; -.
DR   Ensembl; ENSMUST00000023095.14; ENSMUSP00000023095.7; ENSMUSG00000022456.19. [Q9Z1S5-2]
DR   Ensembl; ENSMUST00000116423.3; ENSMUSP00000112124.2; ENSMUSG00000022456.19. [Q9Z1S5-2]
DR   GeneID; 24050; -.
DR   KEGG; mmu:24050; -.
DR   UCSC; uc007wyq.1; mouse. [Q9Z1S5-1]
DR   AGR; MGI:1345148; -.
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; 5396944at2759; -.
DR   PhylomeDB; Q9Z1S5; -.
DR   TreeFam; TF101078; -.
DR   BioGRID-ORCS; 24050; 5 hits in 53 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 207 other cell types or tissues.
DR   ExpressionAtlas; Q9Z1S5; baseline and differential.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
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   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   InterPro; IPR008114; Septin3.
DR   PANTHER; PTHR18884:SF62; NEURONAL-SPECIFIC SEPTIN-3; 1.
DR   PANTHER; PTHR18884; SEPTIN; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
DR   PRINTS; PR01741; SEPTIN3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51719; G_SEPTIN; 1.
DR   UCD-2DPAGE; Q9Z1S5; -.
DR   Genevisible; Q9Z1S5; MM.
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
//