SUB_DROME
ID SUB_DROME Reviewed; 628 AA.
AC Q9V877;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Kinesin-like protein subito;
DE AltName: Full=Protein double or nothing;
GN Name=sub; Synonyms=Dub; ORFNames=CG12298;
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 {ECO:0000312|EMBL:AAL39742.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, MUTAGENESIS OF CYS-152 AND GLU-385, AND DISRUPTION PHENOTYPE.
RC STRAIN=Berkeley {ECO:0000269|PubMed:11973304};
RC TISSUE=Embryo {ECO:0000269|PubMed:11973304};
RX PubMed=11973304; DOI=10.1093/genetics/160.4.1489;
RA Giunta K.L., Jang J.K., Manheim E.A., Subramanian G., McKim K.S.;
RT "subito encodes a kinesin-like protein required for meiotic spindle pole
RT formation in Drosophila melanogaster.";
RL Genetics 160:1489-1501(2002).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [3]
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 [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-607; THR-609 AND SER-612, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Required during female meiosis for bipolar spindle formation
CC in the absence of the centrosomes and chromosome homolog segregation.
CC Also has roles in male meiosis and mitotic divisions of the early
CC embryo. {ECO:0000269|PubMed:11973304}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11973304}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11973304}.
CC Note=Microtubule-associated.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:11973304}.
CC -!- DISRUPTION PHENOTYPE: Mutant female meiotic spindles can be unipolar,
CC multipolar or frayed with no defined poles.
CC {ECO:0000269|PubMed:11973304}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE013599; AAF57799.1; -; Genomic_DNA.
DR EMBL; AY069597; AAL39742.1; -; mRNA.
DR RefSeq; NP_001286548.1; NM_001299619.1.
DR RefSeq; NP_611260.1; NM_137416.3.
DR AlphaFoldDB; Q9V877; -.
DR SMR; Q9V877; -.
DR BioGRID; 69344; 17.
DR IntAct; Q9V877; 3.
DR STRING; 7227.FBpp0086041; -.
DR iPTMnet; Q9V877; -.
DR PaxDb; Q9V877; -.
DR PRIDE; Q9V877; -.
DR DNASU; 44870; -.
DR EnsemblMetazoa; FBtr0086881; FBpp0086041; FBgn0003545.
DR EnsemblMetazoa; FBtr0340277; FBpp0309241; FBgn0003545.
DR GeneID; 44870; -.
DR KEGG; dme:Dmel_CG12298; -.
DR CTD; 44870; -.
DR FlyBase; FBgn0003545; sub.
DR VEuPathDB; VectorBase:FBgn0003545; -.
DR eggNOG; KOG0247; Eukaryota.
DR GeneTree; ENSGT00940000172712; -.
DR HOGENOM; CLU_027535_0_0_1; -.
DR InParanoid; Q9V877; -.
DR OMA; IDGDHTF; -.
DR OrthoDB; 314538at2759; -.
DR PhylomeDB; Q9V877; -.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-68884; Mitotic Telophase/Cytokinesis.
DR Reactome; R-DME-983189; Kinesins.
DR BioGRID-ORCS; 44870; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 44870; -.
DR PRO; PR:Q9V877; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003545; Expressed in ovary and 11 other tissues.
DR ExpressionAtlas; Q9V877; baseline and differential.
DR Genevisible; Q9V877; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:1990385; C:meiotic spindle midzone; IDA:FlyBase.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051233; C:spindle midzone; IDA:FlyBase.
DR GO; GO:0000922; C:spindle pole; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140496; F:gamma-tubulin complex binding; IDA:FlyBase.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IMP:UniProtKB.
DR GO; GO:0040016; P:embryonic cleavage; IMP:UniProtKB.
DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP:FlyBase.
DR GO; GO:0033566; P:gamma-tubulin complex localization; IDA:FlyBase.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0051257; P:meiotic spindle midzone assembly; IDA:FlyBase.
DR GO; GO:0000212; P:meiotic spindle organization; IMP:FlyBase.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007020; P:microtubule nucleation; IDA:FlyBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR GO; GO:0007056; P:spindle assembly involved in female meiosis; IGI:FlyBase.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Meiosis; Microtubule; Mitosis; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..628
FT /note="Kinesin-like protein subito"
FT /id="PRO_0000125427"
FT DOMAIN 87..479
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 28..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 509..612
FT /evidence="ECO:0000255"
FT COMPBIAS 28..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q02241,
FT ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 609
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 152
FT /note="C->Y: In allele sub-1794; elevated levels of X
FT chromosome non-disjunction."
FT /evidence="ECO:0000269|PubMed:11973304"
FT MUTAGEN 385
FT /note="E->K: In allele sub-Dub; meiotic non-disjunction in
FT males and females."
FT /evidence="ECO:0000269|PubMed:11973304"
SQ SEQUENCE 628 AA; 71387 MW; AB03C13EEC8EC029 CRC64;
MDSKEVSEVP RREVRSFLMA RDPSIDRRFR PRPNKKMRLF DNIQESEEES FSEYSDTESE
YKYQSSEATE GASCATSAAD SSNVETGPQV FLRLRPVKDA SKAYIVSEEA NVLITSCKVD
STSNNVNRME KHFGFTSIFD STVGQRDIYD TCVGPKIMEE ECVTIMTYGT SGSGKTYTLL
GDDVRAGIIP RALENIFTIY QDTVFRSPKL KLINGSIVFL QDDASLKELQ IRKKLLDLCP
DISAHHQRLK QVIDGDHMFE TKASTDVSVL VWVSFVEIYN ELVYDLLAIP PKQDKLGEVP
RKNLKIVGNK GHVFIKGLTS VFVTSSEEAL RLLRLGQQRS TYASTSVNAN SSRSHCVFTV
DILKYNRSGI TTQSSYKFCD LAGSERVNNT GTSGLRLKEA KNINTSLMVL GRCLDAASTV
QKKKNADIIP YRDSKLTMLL QAALLGKEKL AMIVTVTPLD KYYEENLNVL NFASIAKNII
FKEPVIKQHR VSYCGFMEFS KMSTCEGGDY TKELEDENVR LQLEIEQLKY DHVLQMQLLE
EKLRRELTAT YQEIIQNNKK QYEDECEKKL LIAQRESEFM LSSQRRRYEE QIEDLKDEIE
ELKNPASDTD ISDDPNESKS PIEILDDD
