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   02-SEP-2026, entry version 180.
DE   RecName: Full=Septin-1 {ECO:0000303|PubMed:8590810};
DE   AltName: Full=DIFF6 protein homolog {ECO:0000303|PubMed:9520435};
DE   AltName: Full=Protein innocent bystander {ECO:0000303|PubMed:9520435};
GN   Name=Septin1 {ECO:0000303|PubMed:8590810,
GN   ECO:0000312|FlyBase:FBgn0011710};
GN   Synonyms=Diff6 {ECO:0000303|PubMed:9520435}, iby
GN   {ECO:0000303|PubMed:9520435}, Sep1 {ECO:0000303|PubMed:8590810};
GN   ORFNames=CG1403 {ECO:0000312|FlyBase:FBgn0011710};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; 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   PDB; 8DKT; X-ray; 2.38 A; A=33-306.
DR   AlphaFoldDB; P42207; -.
DR   SMR; P42207; -.
DR   BioGRID; 59391; 16.
DR   ComplexPortal; CPX-26526; Septin1-Septin2-pnut complex.
DR   DIP; DIP-18454N; -.
DR   FunCoup; P42207; 1502.
DR   IntAct; P42207; 40.
DR   STRING; 7227.FBpp0076897; -.
DR   iPTMnet; P42207; -.
DR   PaxDb; 7227-FBpp0076897; -.
DR   PeptideAtlas; P42207; -.
DR   EnsemblMetazoa; FBtr0077198; FBpp0076897; FBgn0011710.
DR   GeneID; 33114; -.
DR   KEGG; dme:Dmel_CG1403; -.
DR   UCSC; CG1403-RB; d. melanogaster.
DR   AGR; FB:FBgn0011710; -.
DR   CTD; 1731; -.
DR   FlyBase; FBgn0011710; Septin1.
DR   VEuPathDB; VectorBase:FBgn0011710; -.
DR   eggNOG; KOG2655; Eukaryota.
DR   HOGENOM; CLU_017718_0_0_1; -.
DR   InParanoid; P42207; -.
DR   OMA; EASHAEI; -.
DR   OrthoDB; 416553at2759; -.
DR   PhylomeDB; P42207; -.
DR   BioGRID-ORCS; 33114; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 33114; -.
DR   PRO; PR:P42207; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0011710; Expressed in adult enteroendocrine precursor cell in adult midgut (Drosophila) and 133 other cell types or tissues.
DR   ExpressionAtlas; P42207; baseline and differential.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0032154; C:cleavage furrow; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; EXP:UniProtKB.
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; IPI:ComplexPortal.
DR   GO; GO:0051015; F:actin filament binding; IDA:FlyBase.
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:0044837; P:actomyosin contractile ring organization; IMP:FlyBase.
DR   GO; GO:0007298; P:border follicle cell migration; IMP: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:0008104; P:intracellular protein localization; IBA:GO_Central.
DR   GO; GO:0000281; P:mitotic cytokinesis; IDA:ComplexPortal.
DR   GO; GO:0042461; P:photoreceptor cell development; NAS:ComplexPortal.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IDA:FlyBase.
DR   GO; GO:0042060; P:wound healing; IMP:FlyBase.
DR   CDD; cd01850; CDC_Septin; 1.
DR   FunFam; 3.40.50.300:FF:000064; Septin 4; 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   PANTHER; PTHR18884; SEPTIN; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51719; G_SEPTIN; 1.
DR   PDBsum; 8DKT; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cytoplasm; GTP-binding;
KW   Nucleotide-binding; 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"
FT   STRAND          36..41
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   HELIX           48..56
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   STRAND          80..88
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   STRAND          91..99
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   TURN            101..104
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   STRAND          106..108
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   TURN            110..113
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   HELIX           114..132
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   STRAND          146..151
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   HELIX           160..166
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   TURN            167..172
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   STRAND          175..180
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   HELIX           182..184
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   HELIX           187..204
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   HELIX           209..214
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   HELIX           220..232
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   STRAND          234..236
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   STRAND          252..256
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   STRAND          259..264
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   TURN            266..268
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   HELIX           271..280
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   HELIX           282..288
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   HELIX           289..294
FT                   /evidence="ECO:0007829|PDB:8DKT"
FT   HELIX           295..302
FT                   /evidence="ECO:0007829|PDB:8DKT"
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
//