SEPT2_MOUSE
ID SEPT2_MOUSE Reviewed; 361 AA.
AC P42208; B2RRZ2; Q3U9Y5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Septin-2;
DE AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 5;
DE Short=NEDD-5;
GN Name=Septin2 {ECO:0000312|MGI:MGI:97298};
GN Synonyms=Nedd5 {ECO:0000303|PubMed:9203580},
GN Sept2 {ECO:0000312|MGI:MGI:97298};
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], FUNCTION, AND MUTAGENESIS OF GLY-47; SER-51 AND
RP GLN-125.
RC TISSUE=Neural tube;
RX PubMed=9203580; DOI=10.1101/gad.11.12.1535;
RA Kinoshita M., Kumar S., Noda M.;
RT "Nedd5, a mammalian septin, is a novel cytoskeletal component interacting
RT with actin-based structures.";
RL Genes Dev. 11:1535-1547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Placenta;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [5]
RP PROTEIN SEQUENCE OF 51-66; 97-112 AND 117-128, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH SEPTIN5 AND SEPTIN7, LACK OF INTERACTION WITH SEPTIN4, AND
RP DEVELOPMENTAL STAGE.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20558667; DOI=10.1126/science.1191054;
RA Hu Q., Milenkovic L., Jin H., Scott M.P., Nachury M.V., Spiliotis E.T.,
RA Nelson W.J.;
RT "A septin diffusion barrier at the base of the primary cilium maintains
RT ciliary membrane protein distribution.";
RL Science 329:436-439(2010).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22179047; DOI=10.1038/ncb2410;
RA Chih B., Liu P., Chinn Y., Chalouni C., Komuves L.G., Hass P.E.,
RA Sandoval W., Peterson A.S.;
RT "A ciliopathy complex at the transition zone protects the cilia as a
RT privileged membrane domain.";
RL Nat. Cell Biol. 14:61-72(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 33-306 IN COMPLEX WITH GPPNHP, AND
RP MUTAGENESIS OF SER-46 AND THR-78.
RX PubMed=19805342; DOI=10.1073/pnas.0902858106;
RA Sirajuddin M., Farkasovsky M., Zent E., Wittinghofer A.;
RT "GTP-induced conformational changes in septins and implications for
RT function.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16592-16597(2009).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase. Forms a filamentous
CC structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the
CC sperm annulus which is required for the structural integrity and
CC motility of the sperm tail during postmeiotic differentiation (By
CC similarity). Required for normal organization of the actin
CC cytoskeleton. Plays a role in the biogenesis of polarized columnar-
CC shaped epithelium by maintaining polyglutamylated microtubules, thus
CC facilitating efficient vesicle transport, and by impeding MAP4 binding
CC to tubulin. Required for the progression through mitosis. Forms a
CC scaffold at the midplane of the mitotic splindle required to maintain
CC CENPE localization at kinetochores and consequently chromosome
CC congression. During anaphase, may be required for chromosome
CC segregation and spindle elongation. Plays a role in ciliogenesis and
CC collective cell movements (By similarity). In cilia, required for the
CC integrity of the diffusion barrier at the base of the primary cilium
CC that prevents diffusion of transmembrane proteins between the cilia and
CC plasma membranes: probably acts by regulating the assembly of the
CC tectonic-like complex (also named B9 complex) by localizing TMEM231
CC protein. {ECO:0000250, ECO:0000250|UniProtKB:Q15019,
CC ECO:0000269|PubMed:20558667, ECO:0000269|PubMed:22179047,
CC ECO:0000269|PubMed:9203580}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and associate with cellular membranes, actin
CC filaments and microtubules (By similarity). GTPase activity is required
CC for filament formation (By similarity). Septin filaments are assembled
CC from asymmetrical heterotrimers, composed of SEPTIN2, SEPTIN6 and
CC SEPTIN7 that associate head-to-head to form a hexameric unit (By
CC similarity). Interaction between SEPTIN2 and SEPTIN7 seems indirect (By
CC similarity). Interacts also with SEPTIN9 and SEPTIN5 (PubMed:11739749).
CC Interaction with SEPTIN4 not detected (PubMed:11739749). Component of a
CC septin core octomeric complex consisting of SEPTIN12, SEPTIN7, SEPTIN6
CC and SEPTIN2 or SEPTIN4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-
CC 7-12 and located in the sperm annulus (By similarity). Interacts with
CC MAP4 (By similarity). Interacts with DZIP1L (By similarity).
CC {ECO:0000250|UniProtKB:Q15019, ECO:0000269|PubMed:11739749}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250}. Chromosome, centromere,
CC kinetochore {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody
CC {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell projection,
CC cilium membrane. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:Q15019}. Note=In metaphase cells, localized
CC within the microtubule spindle. At the metaphase plate, in close
CC apposition to the kinetochores of the congressed chromosomes. In cells
CC undergoing cytokinesis, localized to the midbody, the ingressing
CC cleavage furrow, and the central spindle (By similarity). In interphase
CC and postmitotic cells, localized to fibrous or granular structures,
CC depending on the growth state of the cell. Localizes at the base of the
CC cilia near the morphological distinction between the cilia and plasma
CC membranes. Found in the sperm annulus. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q15019}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DEVELOPMENTAL STAGE: Expressed at 17 dpc in the brain with levels
CC remaining relatively stable up to adulthood (at protein level).
CC {ECO:0000269|PubMed:11739749}.
CC -!- MISCELLANEOUS: Coordinated expression with SEPTIN6 and SEPTIN7.
CC {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}.
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DR EMBL; D49382; BAA08380.1; -; mRNA.
DR EMBL; AK028072; BAC25737.1; -; mRNA.
DR EMBL; AK146616; BAE27305.1; -; mRNA.
DR EMBL; AK151591; BAE30531.1; -; mRNA.
DR EMBL; AK171331; BAE42396.1; -; mRNA.
DR EMBL; CH466520; EDL39946.1; -; Genomic_DNA.
DR EMBL; CH466520; EDL39948.1; -; Genomic_DNA.
DR EMBL; BC138636; AAI38637.1; -; mRNA.
DR EMBL; BC138637; AAI38638.1; -; mRNA.
DR CCDS; CCDS15190.1; -.
DR RefSeq; NP_001153189.1; NM_001159717.1.
DR RefSeq; NP_001153190.1; NM_001159718.1.
DR RefSeq; NP_001153191.1; NM_001159719.1.
DR RefSeq; NP_035021.1; NM_010891.2.
DR RefSeq; XP_006529304.1; XM_006529241.2.
DR RefSeq; XP_006529305.1; XM_006529242.1.
DR PDB; 3FTQ; X-ray; 2.90 A; A/B/C/D=33-306.
DR PDBsum; 3FTQ; -.
DR AlphaFoldDB; P42208; -.
DR SMR; P42208; -.
DR BioGRID; 201724; 32.
DR DIP; DIP-32438N; -.
DR IntAct; P42208; 21.
DR MINT; P42208; -.
DR STRING; 10090.ENSMUSP00000027495; -.
DR iPTMnet; P42208; -.
DR PhosphoSitePlus; P42208; -.
DR SwissPalm; P42208; -.
DR REPRODUCTION-2DPAGE; IPI00114945; -.
DR REPRODUCTION-2DPAGE; P42208; -.
DR EPD; P42208; -.
DR jPOST; P42208; -.
DR MaxQB; P42208; -.
DR PaxDb; P42208; -.
DR PeptideAtlas; P42208; -.
DR PRIDE; P42208; -.
DR ProteomicsDB; 256963; -.
DR DNASU; 18000; -.
DR Ensembl; ENSMUST00000027495; ENSMUSP00000027495; ENSMUSG00000026276.
DR Ensembl; ENSMUST00000168776; ENSMUSP00000132850; ENSMUSG00000116048.
DR Ensembl; ENSMUST00000179353; ENSMUSP00000136366; ENSMUSG00000116048.
DR GeneID; 18000; -.
DR KEGG; mmu:18000; -.
DR UCSC; uc007cea.2; mouse.
DR CTD; 4735; -.
DR MGI; MGI:97298; Septin2.
DR VEuPathDB; HostDB:ENSMUSG00000026276; -.
DR VEuPathDB; HostDB:ENSMUSG00000116048; -.
DR eggNOG; KOG2655; Eukaryota.
DR GeneTree; ENSGT00940000155098; -.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; P42208; -.
DR OMA; XILDEIE; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; P42208; -.
DR TreeFam; TF101079; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 18000; 1 hit in 46 CRISPR screens.
DR ChiTaRS; Sept2; mouse.
DR EvolutionaryTrace; P42208; -.
DR PRO; PR:P42208; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P42208; protein.
DR Bgee; ENSMUSG00000026276; Expressed in yolk sac and 67 other tissues.
DR ExpressionAtlas; P42208; baseline and differential.
DR Genevisible; P42208; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005826; C:actomyosin contractile ring; NAS:UniProtKB.
DR GO; GO:0005930; C:axoneme; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; TAS:MGI.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0060170; C:ciliary membrane; IDA:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; IDA:MGI.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000145; C:exocyst; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; TAS:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0097730; C:non-motile cilium; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0031105; C:septin complex; IDA:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0097227; C:sperm annulus; ISO:MGI.
DR GO; GO:0005876; C:spindle microtubule; TAS:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0051258; P:protein polymerization; TAS:MGI.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0002036; P:regulation of L-glutamate import across plasma membrane; IDA:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IDA:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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; IPR008113; Septin2.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01740; SEPTIN2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Cell membrane;
KW Cell projection; Centromere; Chromosome; Cilium; Cytoplasm; Cytoskeleton;
KW Differentiation; Direct protein sequencing; Flagellum; GTP-binding;
KW Kinetochore; Membrane; Mitosis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..361
FT /note="Septin-2"
FT /id="PRO_0000173516"
FT DOMAIN 34..306
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 44..51
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 101..104
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 182..185
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 260..270
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT BINDING 44..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 183..186
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 241
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 258
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT SITE 156
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT MOD_RES 17
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 190
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15019"
FT MOD_RES 211
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15019"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MUTAGEN 46
FT /note="S->D: Loss of GTP-binding."
FT /evidence="ECO:0000269|PubMed:19805342"
FT MUTAGEN 47
FT /note="G->V: Loss of GTP-binding activity."
FT /evidence="ECO:0000269|PubMed:9203580"
FT MUTAGEN 51
FT /note="S->N: Loss of GTP-binding activity."
FT /evidence="ECO:0000269|PubMed:9203580"
FT MUTAGEN 78
FT /note="T->G: Reduces affinity for GTP 20-fold."
FT /evidence="ECO:0000269|PubMed:19805342"
FT MUTAGEN 125
FT /note="Q->L: Loss of GTP-binding activity."
FT /evidence="ECO:0000269|PubMed:9203580"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:3FTQ"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:3FTQ"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3FTQ"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:3FTQ"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:3FTQ"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3FTQ"
FT HELIX 111..133
FT /evidence="ECO:0007829|PDB:3FTQ"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:3FTQ"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:3FTQ"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:3FTQ"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:3FTQ"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:3FTQ"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3FTQ"
FT HELIX 189..205
FT /evidence="ECO:0007829|PDB:3FTQ"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:3FTQ"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:3FTQ"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:3FTQ"
FT STRAND 249..258
FT /evidence="ECO:0007829|PDB:3FTQ"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:3FTQ"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:3FTQ"
FT HELIX 273..293
FT /evidence="ECO:0007829|PDB:3FTQ"
FT HELIX 295..303
FT /evidence="ECO:0007829|PDB:3FTQ"
SQ SEQUENCE 361 AA; 41526 MW; C4BFFB3F1815E081 CRC64;
MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK STLINSLFLT
DLYPERIIPG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV DTPGYGDAIN CRDCFKTIIS
YIDEQFERYL HDESGLNRRH IIDNRVHCCF YFISPFGHGL KPLDVAFMKA IHNKVNIVPV
IAKADTLTLK ERERLKKRIL DEIEEHSIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV
GSNQLIEAKG KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR
SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG DSDSGALGQH
V
