Q24145 (SHARK_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase shark
EC=2.7.10.2

Gene names

Name:	shark
Synonyms:	Tk7
ORF Names:	CG18247

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	939 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May be involved in signal transduction on the apical surface of ectodermal epithelia regulating their polarity during invagination. Crumbs (crb) may be the intracellular signal. Ref.1
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subcellular location	Cytoplasm. Note: Apical expression in cephalic furrow and tracheal cells. Limited to luminal surface and absent from the basal surface. Ref.1
Tissue specificity	Gastrulation embryos show expression in ectodermal cells along the cephalic furrrow and ventral midline. Proctodeum, stomodeum and their derived structures (foregut, atrium, pharynx, esophagus and hindgut) continue to show expression from stage 8-9 to late embryos. Other ectodermally derived structures (frontal sac, salivary gland and labium) and developing tracheal system also show expression. Ref.1
Developmental stage	Embryos only. Ref.1
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Contains 3 ANK repeats. Contains 1 protein kinase domain. Contains 2 SH2 domains.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	ANK repeat Repeat SH2 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	JNK cascade Inferred from mutant phenotype. Source: FlyBase apoptotic cell clearance Inferred from mutant phenotype. Source: FlyBase dorsal appendage formation Inferred from mutant phenotype. Source: FlyBase dorsal closure, elongation of leading edge cells Inferred from mutant phenotype. Source: FlyBase maintenance of epithelial cell apical/basal polarity Inferred from expression pattern Ref.1. Source: UniProtKB
Cellular component	cell cortex Inferred from direct assay. Source: FlyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Non-traceable author statement. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 939	939	Tyrosine-protein kinase shark		PRO_0000088137
Regions
	Domain	10 – 106	97	SH2 1
	Repeat	153 – 185	33	ANK 1
	Repeat	186 – 218	33	ANK 2
	Repeat	220 – 252	33	ANK 3
	Domain	288 – 403	116	SH2 2
	Domain	662 – 921	260	Protein kinase
	Nucleotide binding	668 – 676	9	ATP By similarity
Sites
	Active site	789	1	Proton acceptor By similarity
	Binding site	698	1	ATP By similarity
Amino acid modifications
	Modified residue	927	1	Phosphotyrosine Potential
Experimental info
	Sequence conflict	19	1	A → V in AAA79851. Ref.1
	Sequence conflict	39	1	S → R in AAA79851. Ref.1
	Sequence conflict	50	1	L → F in AAA79851. Ref.1
	Sequence conflict	85	1	D → E in AAA79851. Ref.1
	Sequence conflict	129	1	S → T in AAA79851. Ref.1
	Sequence conflict	199	1	P → T in AAA79851. Ref.1
	Sequence conflict	341	1	C → S in AAA79851. Ref.1
	Sequence conflict	505 – 506	2	GT → RA in AAA79851. Ref.1
	Sequence conflict	597	1	M → V in AAA79851. Ref.1
	Sequence conflict	611	1	A → P in AAA79851. Ref.1
	Sequence conflict	732	1	A → S in AAA79851. Ref.1
	Sequence conflict	898	1	A → P in AAA79851. Ref.1
	Sequence conflict	935 – 939	5	QTVHI → KRFTFNPVSIFHFFRC in AAA79851. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q24145 [UniParc]. Last modified October 1, 2000. Version 2. Checksum: 37CC2C3DA25D3F52	FASTA	939	104,273
	10 20 30 40 50 60 MSRDSDPMKW YHGNLSREAA DELLKQGYED GTFLVRESST AAGDFVLSLL CQGEVCHYQV 70 80 90 100 110 120 RRHGGEDAFF SIDDKVQTKI LHGLDTLVDY YQQAANGLPT KLTVPLIRDL PPHNTRSHGV 130 140 150 160 170 180 TNLLHRATSK NESKVVFELL KCGYRNFDAK NQDGQTALHL AALHSDEDIL KHLLNAKVQV 190 200 210 220 230 240 NSSDSFGCQP LHYAARSKPA SFIRTLISAQ ANVQGRNIDN GYVPLHEAAK HGNLEAVQEL 250 260 270 280 290 300 LLAEAPPLPR TSSGEFPFDL AKEAGQTAVE EFLLNYKLPP ANTTRDQWYH GTLTREEAVA 310 320 330 340 350 360 ILKKHAKELL AKQPEVDTSG CFLVRYSESP AASGLVLTLL CDQVVKNFRI SQADLYQNGN 370 380 390 400 410 420 KVQSGGSKFL YIDDGPYWPS VEHLIAHFMR FSYGLPVSLK YPVPPQPKPE VPSFATIPRS 430 440 450 460 470 480 NMKPKAASPA TPPTPVSPHS HHQHPHVPAL TITKKKQKEN SSSMFNTLRL TSPKKALFDM 490 500 510 520 530 540 NSLRKNKSKG KRSDSESSVS GSLAGTEQEL QAAAPMLKSL SFSTEFSTFN ADGVTGSGAA 550 560 570 580 590 600 AAGEVYNVPR NNTPIEIDLP PIAQKTEAEV EYFTKSDVAI ERERAGQWIG NGYQPTMDVL 610 620 630 640 650 660 SLLDQQIKAP AVARLNSLGP NASTESEMAS YLHRKCSGTP STPSATEVEA AKLRFFIEPE 670 680 690 700 710 720 KLVLDREIGH GEFGSVHSGW LLRKSGAGEE SRLEVAIKML SDEHSNKQEF LREASVMMRL 730 740 750 760 770 780 EHKCIVRLIG IAKGEMLMMV QELAPLGSML QYILDHGHEI TANAELKVWA SQIACGMHYL 790 800 810 820 830 840 ESQHFVHRDL AARNILLTAR HQAKISDFGM SRSLRPGSTE YQFTQGGRWP IRWYAPESFN 850 860 870 880 890 900 LGIFSHASDV WSFGVTIWEM FSLGAPPYGE ISNVDAIKLV DSGERLPQPN LCPAYIYAVM 910 920 930 QSCWKERPKD RPTFVYLTEF FARDPDYQNL PELVQTVHI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Shark, a Src homology 2, ankyrin repeat, tyrosine kinase, is expressed on the apical surfaces of ectodermal epithelia." Ferrante A.W. Jr., Reinke R., Stanley E.R. Proc. Natl. Acad. Sci. U.S.A. 92:1911-1915(1995) [PubMed: 7892198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Embryo.
[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: 10731132] [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: 12537572] [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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Identification of seven novel protein-tyrosine kinase genes of Drosophila by the polymerase chain reaction." Shishido E., Emori Y., Saigo K. FEBS Lett. 289:235-238(1991) [PubMed: 1915852] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 793-849.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U37773 mRNA. Translation: AAA79851.1. AE013599 Genomic DNA. Translation: AAF58044.1. AY051937 mRNA. Translation: AAK93361.1. S55982 Genomic DNA. Translation: AAB19909.1.
PIR	S18015.
RefSeq	NP_524743.2. NM_080004.2.
UniGene	Dm.6764.
3D structure databases
ProteinModelPortal	Q24145.
SMR	Q24145. Positions 7-281, 284-403, 655-924.
ModBase	Search...
Protein-protein interaction databases
STRING	Q24145.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0087244; FBpp0086382; FBgn0015295.
GeneID	44353.
KEGG	dme:Dmel_CG18247.
NMPDR	fig|7227.3.peg.5542.
Organism-specific databases
CTD	44353.
FlyBase	FBgn0015295. shark.
Phylogenomic databases
eggNOG	inNOG07824.
GeneTree	EMGT00050000002730.
InParanoid	Q24145.
OMA	YAPESFN.
OrthoDB	EOG4JWSVT.
PhylomeDB	Q24145.
Enzyme and pathway databases
BRENDA	2.7.10.2. 1994.
Gene expression databases
Bgee	Q24145.
GermOnline	CG18247. Drosophila melanogaster.
Family and domain databases
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase. IPR000980. SH2. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. [Graphical view]
Gene3D	G3DSA:1.25.40.20. ANK. 1 hit. G3DSA:3.30.505.10. SH2. 2 hits.
KO	K08253.
Pfam	PF00023. Ank. 1 hit. PF12796. Ank_2. 1 hit. PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 2 hits. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00109. TYRKINASE.
SMART	SM00248. ANK. 4 hits. SM00252. SH2. 2 hits. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit. SSF56112. Kinase_like. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 3 hits. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS50001. SH2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	837182.

Entry information

Entry name

SHARK_DROME

Accession

Primary (citable) accession number: Q24145
Secondary accession number(s): Q26299, Q9V7K5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2003
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project