SEPT1_DROME
ID SEPT1_DROME Reviewed; 361 AA.
AC P42207; Q8IQ47; Q9VRH5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Septin-1;
DE AltName: Full=DIFF6 protein homolog;
DE AltName: Full=Protein innocent bystander;
GN Name=Sep1; Synonyms=Diff6, iby; ORFNames=CG1403;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH PNUT, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=8590810; DOI=10.1091/mbc.6.12.1843;
RA Fares H., Peifer M., Pringle J.R.;
RT "Localization and possible functions of Drosophila septins.";
RL Mol. Biol. Cell 6:1843-1859(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RA Hayward D.C., Delaney S.J., Miklos G.L.G.;
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=9520435; DOI=10.1073/pnas.95.7.3731;
RA Maleszka R., de Couet H.G., Miklos G.L.G.;
RT "Data transferability from model organisms to human beings: insights from
RT the functional genomics of the flightless region of Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3731-3736(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP FUNCTION, INTERACTION WITH PARK, AND UBIQUITINATION.
RX PubMed=17456438; DOI=10.1016/j.ibmb.2007.01.007;
RA Bae Y.J., Kang S.J., Park K.S.;
RT "Drosophila melanogaster Parkin ubiquitinates peanut and septin1 as an E3
RT ubiquitin-protein ligase.";
RL Insect Biochem. Mol. Biol. 37:430-439(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
CC -!- FUNCTION: Involved in cytokinesis (Probable). May be involved in p53-
CC dependent apoptosis (PubMed:17456438). {ECO:0000269|PubMed:17456438,
CC ECO:0000305}.
CC -!- SUBUNIT: Likely part of a multicomponent septin complex that includes
CC pnut (PubMed:8590810). Interacts with pnut (PubMed:8590810). Interacts
CC with park (PubMed:17456438). {ECO:0000269|PubMed:17456438,
CC ECO:0000269|PubMed:8590810}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8590810}.
CC -!- TISSUE SPECIFICITY: Accumulates at the leading edge of the cleavage
CC furrow in dividing cells and cellularizing embryos (at protein level)
CC (PubMed:8590810). Also accumulates at the leading edge of the embryo
CC epithelium during dorsal closure, in the embryonic neurons, and at the
CC baso-lateral surfaces of ovarian follicle cells (at protein level)
CC (PubMed:8590810). {ECO:0000269|PubMed:8590810}.
CC -!- PTM: Ubiquitinated by park, leading to its degradation by the
CC proteasome. {ECO:0000269|PubMed:17456438}.
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; L33246; AAC34305.1; -; Genomic_DNA.
DR EMBL; X67202; CAA47638.1; -; mRNA.
DR EMBL; AF017777; AAC28401.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF50825.1; -; Genomic_DNA.
DR PIR; S25063; S25063.
DR RefSeq; NP_523430.1; NM_078706.4.
DR AlphaFoldDB; P42207; -.
DR SMR; P42207; -.
DR BioGRID; 59391; 15.
DR DIP; DIP-18454N; -.
DR IntAct; P42207; 2.
DR STRING; 7227.FBpp0076897; -.
DR iPTMnet; P42207; -.
DR PaxDb; P42207; -.
DR PRIDE; P42207; -.
DR EnsemblMetazoa; FBtr0077198; FBpp0076897; FBgn0011710.
DR GeneID; 33114; -.
DR KEGG; dme:Dmel_CG1403; -.
DR UCSC; CG1403-RB; d. melanogaster.
DR CTD; 33114; -.
DR FlyBase; FBgn0011710; Sep1.
DR VEuPathDB; VectorBase:FBgn0011710; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_0_0_1; -.
DR InParanoid; P42207; -.
DR OMA; EASHAEI; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; P42207; -.
DR BioGRID-ORCS; 33114; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Sep1; fly.
DR GenomeRNAi; 33114; -.
DR PRO; PR:P42207; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0011710; Expressed in ovary and 16 other tissues.
DR ExpressionAtlas; P42207; baseline and differential.
DR Genevisible; P42207; DM.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IDA:FlyBase.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0031105; C:septin complex; IDA:FlyBase.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:FlyBase.
DR GO; GO:0003924; F:GTPase activity; IDA:FlyBase.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase.
DR GO; GO:0007349; P:cellularization; TAS:FlyBase.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:FlyBase.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; 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 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; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..361
FT /note="Septin-1"
FT /id="PRO_0000173511"
FT DOMAIN 32..304
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 42..49
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 99..102
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 180..183
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT BINDING 42..49
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 181..189
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
SQ SEQUENCE 361 AA; 41131 MW; AE7D4860B625AB00 CRC64;
MADTKGFSSI ETPGYVGFAN LPNQVHRKSV KKGFEFTLMV VGESGLGKST LVNSLFLTDL
YPERIIPDAI EKQKQTVKLE ASTVEIEERG VKLRLTVVDT PGFGDAIDNS NSFGAILEYI
DEQYERFLRD ESGLNRRNIV DNRIHCCFYF ISPFGHGLKP LDVEFMKKLH SKVNIVPVIA
KADCLTKKEI LRLKCRIMQE IESHGIKIYP LPDCDSDEDE DYKEQVKQLK EAVPFAVCGA
NTLLEVKGKK VRGRLYPWGV VEVENPDHCD FIKLRTMLIT HMQDLQEVTQ EVHYENYRSD
RLAKGIKGKE NGVKAERDSS SQVVSNSVLG EKDRILQEKE AELRRMQEML AQMQARMQAQ
Q
