O16844 (COS_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kinesin-like protein costa

Alternative name(s):
Kinesin-like protein costal2

Gene names

Name:	cos
Synonyms:	cos2, costal-2
ORF Names:	CG1708

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1201 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulates cubitus interruptus (ci) processing by recruiting multiple kinases to promote its efficient phosphorylation. Scaffolds multiple kinases and ci into proximity to promote its hyperphosphorylation, which then targets it for SCFSlimb/proteasome-mediated processing to generate its repressor form. Hh signaling inhibits ci phosphorylation by interfering with the cos-ci-kinases complex formation. Ref.1 Ref.6
Subunit structure	Homodimer Potential. Binds microtubules. Interacts with ci, smo, sgg, CkIalpha and protein kinase A catalytic subunit. Ref.1 Ref.6
Subcellular location	Cytoplasm › cytoskeleton Ref.1.
Developmental stage	Present at high levels during the first 4 hours of embryogenesis and at moderate levels between 4-12 hours. Ref.1
Sequence similarities	Belongs to the kinesin-like protein family. KIF27 subfamily. Contains 1 kinesin-motor domain.
Sequence caution	The sequence AAN71259.1 differs from that shown. Reason: Frameshift at position 415.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytoplasmic sequestering of transcription factor Inferred from mutant phenotype PubMed 11090136. Source: FlyBase imaginal disc-derived wing morphogenesis Inferred from mutant phenotype PubMed 16648592. Source: FlyBase microtubule-based movement Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase negative regulation of sequence-specific DNA binding transcription factor activity Inferred from mutant phenotype PubMed 11090136. Source: FlyBase negative regulation of smoothened signaling pathway Traceable author statement PubMed 15104233. Source: FlyBase ovarian follicle cell development Traceable author statement PubMed 10822261. Source: FlyBase positive regulation of hh target transcription factor activity Inferred from mutant phenotype PubMed 10862750. Source: FlyBase positive regulation of smoothened signaling pathway Traceable author statement PubMed 15104233. Source: FlyBase regulation of protein stability Inferred from direct assay PubMed 17671093. Source: FlyBase regulation of proteolysis Non-traceable author statement PubMed 12850443. Source: FlyBase
Cellular_component	Hedgehog signaling complex Inferred from physical interaction PubMed 10825151. Source: FlyBase cytoplasm Inferred from direct assay Ref.1. Source: FlyBase kinesin complex Inferred from sequence or structural similarity PubMed 10908588Ref.1. Source: FlyBase microtubule Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay PubMed 14645371. Source: FlyBase vesicle membrane Inferred from direct assay PubMed 14645371. Source: FlyBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule binding Inferred from direct assay Ref.1. Source: FlyBase microtubule motor activity Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ci	P19538	12	EBI-102069,EBI-94976
fu	P23647	4	EBI-102069,EBI-165536
smo	P91682	5	EBI-102069,EBI-142245

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1201	1201	Kinesin-like protein costa		PRO_0000307148
Regions
	Domain	86 – 363	278	Kinesin-motor
	Nucleotide binding	175 – 182	8	ATP Potential
	Coiled coil	652 – 821	170	Potential
	Coiled coil	968 – 1001	34	Potential
	Compositional bias	622 – 625	4	Poly-Pro
	Compositional bias	1119 – 1124	6	Poly-Ala
	Compositional bias	1130 – 1154	25	Thr-rich
Amino acid modifications
	Modified residue	599	1	Phosphoserine Ref.7
	Modified residue	605	1	Phosphoserine Ref.7
Experimental info
	Sequence conflict	7	1	V → L in AAB66813. Ref.1
	Sequence conflict	471	1	E → D in AAB66813. Ref.1
	Sequence conflict	568	1	A → E in AAT94488. Ref.5
	Sequence conflict	736	1	D → G in AAB66813. Ref.1
	Sequence conflict	807	1	A → V in AAB66813. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O16844 [UniParc]. Last modified October 23, 2007. Version 2. Checksum: 6DC898F8B4C8F20F	FASTA	1,201	133,148
	10 20 30 40 50 60 MEIPIQVAVR IFPHRELKDL LRSFGPTEPK KDAQAVDEGA DSKDSEAQVP AAEKDNPSIS 70 80 90 100 110 120 ETDPNGNAEQ DSAADSKTIP DANGNDSGQK DYPDSAYCVQ AIPISASALG LPSALPGGDP 130 140 150 160 170 180 MDSIAAGLIQ VGPHTVPVTH ALPSSSSQEQ VYHQTVFPLI TLFLEGFDAS VVTYGQRGQG 190 200 210 220 230 240 KSYTLYGNVQ DPTLTDSTEG VVQLCVRDIF SHISLHPERT YAINVGFVEI CGGDVCDLLG 250 260 270 280 290 300 MGNIHCTNVD AVFHWLQVGL SARQSLPAHT LFTLTLEQQW VSKEGLLQHR LSTASFSDLC 310 320 330 340 350 360 GTERCGDQPP GRPLDAGLCM LEQVISTLTD PGLMYGVNGN IPYGQTTLTT LLKDSFGGRA 370 380 390 400 410 420 QTLVILCVSP LEEHLPETLG NLQFAFKVQC VRNFVIMNTY SDDNTMIVQP AEPVPESNSS 430 440 450 460 470 480 AGPLSQAGPG DNFGLQFAAS QWSKLVTNAE GLFSKLIDSK LITEVEKEQI EEWLFLKQEC 490 500 510 520 530 540 EECLSSTEAM RQQKQLVPIL EAEEPEDVNS EAANSESPNS DNENDTDNES HRPDLDDKIE 550 560 570 580 590 600 SLMEEFRDKT DALILEKHAE YLSKHPKAVM QSQDREIEAQ PPEENGDDRK VSIGSRRRSV 610 620 630 640 650 660 QPGASLSTAE LAMLNRVASQ QPPPPIDPES VVDPLESSSG EGIRQAALAA AAATAPIEQL 670 680 690 700 710 720 QKKLRKLVAE IEGKQRQLRE IEETIQVKQN IIAELVKNSD TRSHAKQRFH KKRAKLEAEC 730 740 750 760 770 780 DKAKKQLGKA LVQGRDQSEI ERWTTIIGHL ERRLEDLSSM KHIAGESGQK VKKLQQSVGE 790 800 810 820 830 840 SRKQADDLQK KLRKECKLRC QMEAELAKLR ESRETGKELV KAQGSPEQQG RQLKAVQARI 850 860 870 880 890 900 THLNHILREK SDNLEEQPGP EQQETLRHEI RNLRGTRDLL LEERCHLDRK LKRDKVLTQK 910 920 930 940 950 960 EERKLLECDE AIEAIDAAIE FKNEMITGHR SIDTSDRIQR EKGEQMLMAR LNRLSTEEMR 970 980 990 1000 1010 1020 TLLYKYFTKV IDLRDSSRKL ELQLVQLERE RDAWEWKERV LSNAVRQARL EGERNAVLLQ 1030 1040 1050 1060 1070 1080 RQHEMKLTLM LRHMAEETSA SSASYGERAL APACVAPPVQ ASSDFDYDHF YKGGGNPSKA 1090 1100 1110 1120 1130 1140 LIKAPKPMPT GSALDKYKDK EQRSGRNIFA KFHVLTRYAS AAAAGSSGST AEESTALIES 1150 1160 1170 1180 1190 1200 TTTATATTTS TTTTGAVGKV KDKALVSFRP EQLKRLMPAP TATKVTRQKN KIIIQDASRR N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Costal2, a novel kinesin-related protein in the Hedgehog signaling pathway." Sisson J.C., Ho K.S., Suyama K., Scott M.P. Cell 90:235-245(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DEVELOPMENTAL STAGE, INTERACTION WITH CI.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E. Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[6]	"Hedgehog-regulated Costal2-kinase complexes control phosphorylation and proteolytic processing of Cubitus interruptus." Zhang W., Zhao Y., Tong C., Wang G., Wang B., Jia J., Jiang J. Dev. Cell 8:267-278(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SMO; SGG; CKI ALPHA AND PROTEIN KINASE A CATALYTIC SUBUNIT.
[7]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599 AND SER-605, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF019250 mRNA. Translation: AAB66813.1. AE013599 Genomic DNA. Translation: AAF59270.1. BT001504 mRNA. Translation: AAN71259.1. Frameshift. BT015259 mRNA. Translation: AAT94488.1. BT044167 mRNA. Translation: ACH92232.1.
PIR	T08603.
RefSeq	NP_001260765.1. NM_001273836.1. NP_477092.1. NM_057744.3.
UniGene	Dm.5775.
3D structure databases
HSSP	HSSP built from PDB template 1F9T based on UniProtKB P17119.
ProteinModelPortal	O16844.
SMR	O16844. Positions 142-389.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-22550N.
IntAct	O16844. 5 interactions.
STRING	7227.FBpp0088087.
Proteomic databases
PaxDb	O16844.
PRIDE	O16844.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0089015; FBpp0088087; FBgn0000352.
GeneID	35653.
KEGG	dme:Dmel_CG1708.
Organism-specific databases
CTD	35653.
FlyBase	FBgn0000352. cos.
Phylogenomic databases
eggNOG	COG5059.
HOGENOM	HOG000263945.
InParanoid	O16844.
KO	K06227.
OMA	WRLATIN.
OrthoDB	EOG4GQNM1.
PhylomeDB	O16844.
Gene expression databases
Bgee	O16844.
Family and domain databases
Gene3D	3.40.850.10. 2 hits.
InterPro	IPR001752. Kinesin_motor_dom. [Graphical view]
Pfam	PF00225. Kinesin. 2 hits. [Graphical view]
PRINTS	PR00380. KINESINHEAVY.
SMART	SM00129. KISc. 1 hit. [Graphical view]
PROSITE	PS00411. KINESIN_MOTOR_DOMAIN1. False negative. PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	35653.
NextBio	794555.

Entry information

Entry name

COS_DROME

Accession

Primary (citable) accession number: O16844
Secondary accession number(s): A1Z6X4 , B5RIP3, Q6AWI9, Q8IH04

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	October 23, 2007
Last modified:	May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project