ID   COS_DROPS               Reviewed;        1223 AA.
AC   Q292S8;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Kinesin-like protein costa;
DE   AltName: Full=Kinesin-like protein costal2;
GN   Name=cos; Synonyms=costal-2; ORFNames=GA14314;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Regulates cubitus interruptus (ci) processing by recruiting
CC       multiple kinases to promote its efficient phosphorylation. Scaffolds
CC       multiple kinases and ci into proximity to promote its
CC       hyperphosphorylation, which then targets it for SCFSlimb/proteasome-
CC       mediated processing to generate its repressor form. Hh signaling
CC       inhibits ci phosphorylation by interfering with the cos-ci-kinases
CC       complex formation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer (Potential). Binds microtubules. Interacts with ci,
CC       smo, sgg, CkIalpha and protein kinase A catalytic subunit (By
CC       similarity). {ECO:0000250, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIF27 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
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DR   EMBL; CM000071; EAL24783.2; -; Genomic_DNA.
DR   RefSeq; XP_001360209.2; XM_001360172.3.
DR   AlphaFoldDB; Q292S8; -.
DR   SMR; Q292S8; -.
DR   STRING; 7237.FBpp0277104; -.
DR   EnsemblMetazoa; FBtr0278666; FBpp0277104; FBgn0074342.
DR   GeneID; 4803492; -.
DR   KEGG; dpo:Dpse_GA14314; -.
DR   eggNOG; ENOG502QUYG; Eukaryota.
DR   HOGENOM; CLU_010897_0_0_1; -.
DR   InParanoid; Q292S8; -.
DR   OMA; SDLCGTE; -.
DR   Proteomes; UP000001819; Chromosome 3.
DR   Bgee; FBgn0074342; Expressed in female reproductive system and 3 other tissues.
DR   GO; GO:0005929; C:cilium; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0035301; C:Hedgehog signaling complex; IEA:EnsemblMetazoa.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005875; C:microtubule associated complex; IEA:EnsemblMetazoa.
DR   GO; GO:0012506; C:vesicle membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0019901; F:protein kinase binding; IEA:EnsemblMetazoa.
DR   GO; GO:0140311; F:protein sequestering activity; IEA:EnsemblMetazoa.
DR   GO; GO:0035591; F:signaling adaptor activity; IEA:EnsemblMetazoa.
DR   GO; GO:0005119; F:smoothened binding; IEA:EnsemblMetazoa.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:EnsemblMetazoa.
DR   GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IEA:EnsemblMetazoa.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0042073; P:intraciliary transport; IEA:EnsemblMetazoa.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:EnsemblMetazoa.
DR   GO; GO:0030707; P:ovarian follicle cell development; IEA:EnsemblMetazoa.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:EnsemblMetazoa.
DR   GO; GO:0007224; P:smoothened signaling pathway; IEA:EnsemblMetazoa.
DR   Gene3D; 3.40.850.10; -; 2.
DR   InterPro; IPR027640; Kinesin-like_fam.
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; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding; Reference proteome; Repressor.
FT   CHAIN           1..1223
FT                   /note="Kinesin-like protein costa"
FT                   /id="PRO_0000307149"
FT   DOMAIN          4..394
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          13..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          625..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          774..799
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1162..1188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          658..743
FT                   /evidence="ECO:0000255"
FT   COILED          773..825
FT                   /evidence="ECO:0000255"
FT   COILED          982..1015
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        42..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..597
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..799
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1162..1182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         178..185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1223 AA;  135215 MW;  83E6A7D0BF409A55 CRC64;
     MEIPIQVAVR ICPYTEPSEN RKPVAGAEAD ASAFGNAEAK AESFSDSEDN KNDASNRQRP
     EESTDANGNS EGGRQLKKET LPTDSNGNEN GTIVPLGSGC CVQAIPISAS ALGLPSALPG
     GRAQDSIAAG LIQVGAHTVP VTHALGSGTT QSQLYYQTVF PLISLFLEGF DASVVTYGQR
     GQGKTYTLYG PGFECVYGEA DQGVVQRCVR DIFAHIAGHS ERTYAVNVGF VEICEGEVCD
     LLDMGNVHCQ SVEEVFRWLQ IGLATRQPKS AHSLFTLTLE QQWVSKEGLI QHRLSTASFS
     DLCATERWGE PPPGNPRDAG LQMLELVVNT LTDPSIMYGV NGNIPYGQTT LTTLLKDSFG
     GRAQTLVILC VSPQEQHVAE TLGNLQFAFK VQCVRNYVIM NTYSDDNTPI SPETMPNGSS
     NPGAGPLAQV AAGDNFGLQF AASQWFKLVS NAEGLFAKLM ASNLISELEK EQIEEWLFLK
     QECEECLSST EAMRSQKQLV PIQEAEEPEE SVSEPPNSDN DTDNESQRPD LADKLESLME
     EFRAKTDALI QSKHAEFLTK HPKAVMQSQE RDKESKLDAP PEKDKEKIEE RKTSIAGRRR
     SIQPGASLST AELALLNRVA LQQPTAQPPP SVLDPESSID PLESSAGEGL RQAAIAAAAA
     NAPIEQLQKK LRKLHAEIEG RQRQLKEIEQ TMQVKQNIIS ELVKNSDTRS HAKQRFQKKK
     AKLEAECDKA KKHLAKALIQ GREKGETERW SAIIAHIEHR LEDLSSMKHI AGESGQKLKK
     LQQSMAESRK QQEELEKKIR KESKLRDQLE TELAKLKESR DGASGGKELV KLDSPEQQGR
     QLKAVQARIT HLNHILREKS DNLEECAGGE GPAPAQQESL RHEIRNLRGT RDLLLDERCH
     LDRKLKRDKM LTQREERKLL ECDEAIEAID AAIEFKNELI CGHKSIDTSD RLQREKGEQM
     LMARLNKLSP EEMRTLLYKY FNKVIDLRDS SRKLELQLVQ LERERDAWEW KERVLSNAVR
     QARLEGERNA VLLQRQHEMK LTLMLRHLAE ETSASSASYG ERALAPGHQT SSGDFDYELD
     FYKAAATTTT TTNHKALVKP PKSTPSGAAL EKYKDKEQRG AGRNIFAKFQ VLTRYASSAA
     SAAAAGSCSS TVDESTALIE STTTATATTT TTTTTTTTGG KGKERGLPNI RQDQLKRLMP
     APTVTKVTRQ KNKIIIQDAS RRN