Q9V422 (RYK2_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase Dnt
EC=2.7.10.1

Alternative name(s):
Protein doughnut

Gene names

Name:	dnt
ORF Names:	CG17559

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	584 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May play an essential role in neuronal pathway recognition and ventral muscle attachment site selection. Ref.1
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subcellular location	Cell membrane; Single-pass membrane protein Potential.
Tissue specificity	Expressed in dynamic domains in the embryonic epidermis, many of which border on sites of epithelial invagination into the embryo interior, including ventral furrow, cephalic furrow, fore- and hindgut, optic lobe and tracheal pits. Later in embryogenesis, expression is seen in imaginal tissues. Ref.1 Ref.2
Developmental stage	Expressed both maternally and zygotically from embryos to adults. High expression is seen in embryos, pupae and adults (highest in early pupae) and low expression in larvae. Ref.1 Ref.2
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Contains 1 protein kinase domain. Contains 1 WIF domain.
Sequence caution	The sequence AAD31179.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA11918.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	axon guidance Inferred from mutant phenotype Ref.1. Source: UniProtKB muscle attachment Inferred from mutant phenotype Ref.1. Source: UniProtKB salivary gland morphogenesis Inferred from mutant phenotype. Source: FlyBase
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW transmembrane receptor protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 40	40	Potential
	Chain	41 – 584	544	Tyrosine-protein kinase Dnt		PRO_0000024467
Regions
	Topological domain	41 – 208	168	Extracellular Potential
	Transmembrane	209 – 229	21	Helical; Potential
	Topological domain	230 – 584	355	Cytoplasmic Potential
	Domain	49 – 180	132	WIF
	Domain	317 – 577	261	Protein kinase
	Nucleotide binding	323 – 331	9	ATP By similarity
Sites
	Active site	442	1	Proton acceptor By similarity
	Binding site	345	1	ATP By similarity
Amino acid modifications
	Modified residue	472	1	Phosphotyrosine; by autocatalysis By similarity
	Glycosylation	124	1	N-linked (GlcNAc...) Potential
	Glycosylation	163	1	N-linked (GlcNAc...) Potential
	Glycosylation	168	1	N-linked (GlcNAc...) Potential
	Glycosylation	183	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	448	1	C → Y in AAX33387. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9V422 [UniParc]. Last modified January 27, 2003. Version 2. Checksum: F46FCD024BD8447E	FASTA	584	64,938
	10 20 30 40 50 60 MESVNKCGKS ASTRNCTVKM SRKMWVLSLL ALAALQLHSG SEVAAHLNVF LNPVEVMRLL 70 80 90 100 110 120 GVSAEVYYVR EGHINNYALN FIVPVPANVK DISFTWQSLA GRGLPYSINV VSSDQEVLPR 130 140 150 160 170 180 PAINVSHSGE IPTTIQTWSI ALKCSGLKAA EVDVTVSLEV VLNRSLNNVT HLVFRRKKIC 190 200 210 220 230 240 LMNDSAEDLS EDVDDPQLLE TVMLPPTGLI TLVVGVSVAM GSVCLLLMIA YCVKGAANKR 250 260 270 280 290 300 QHHQHGGQPM RTSSFQRLNT HPPCQSSMGS AAYMTPSIIA PIHGSSLPRK VPVSVEQQHP 310 320 330 340 350 360 EELHRRISEL TVERCRVRLS SLLQEGTFGR VYRGTYNDTQ DVLVKTVAQH ASQMQVLLLL 370 380 390 400 410 420 QEGMLLYGAS HPGILSVLGV SIEDHTTPFV LYPALNNTRN LKQFLLDPAC ARTVTTIQIV 430 440 450 460 470 480 MMASQLSMAL DHLHSHGVVH KDIATRNCVI DDQLRVKLSD SSLSRDLFPS DYNCLGDSEN 490 500 510 520 530 540 RPVKWMSLEA LQHKQFSEAS DSWAFGVLMW ELCTSAKQPY AEVDPFEMEH YLKDGYRLAQ 550 560 570 580 PFNCPDELFT IMAYCWALLP AERPTFAQLQ SCLSEFYSQI TRYV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Embryonic expression and activity of doughnut, a second RYK homolog in Drosophila." Oates A.C., Bonkovsky J.L., Irvine D.V., Kelly L.E., Thomas J.B., Wilks A.F. Mech. Dev. 78:165-169(1998) [PubMed: 9858720] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Embryo.
[2]	"A Drosophila derailed homolog, doughnut, expressed in invaginating cells during embryogenesis." Savant-Bhonsale S., Friese M., McCoon P., Montell D.J. Gene 231:155-161(1999) [PubMed: 10231580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[3]	"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.
[4]	"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.
[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 (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[6]	"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] OF 244-584. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ224361 mRNA. Translation: CAA11918.1. Different initiation. AF123572 mRNA. Translation: AAD31179.1. Different initiation. AE014134 Genomic DNA. Translation: AAF53783.2. BT021239 mRNA. Translation: AAX33387.1. BT057997 mRNA. Translation: ACM16707.1. AY058760 mRNA. Translation: AAL13989.1.
RefSeq	NP_477341.2. NM_057993.3.
UniGene	Dm.4769.
3D structure databases
ProteinModelPortal	Q9V422.
SMR	Q9V422. Positions 317-580.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-20351N.
MINT	MINT-1565021.
STRING	Q9V422.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0081224; FBpp0080765; FBgn0024245.
GeneID	35207.
KEGG	dme:Dmel_CG17559.
NMPDR	fig|7227.3.peg.2963.
Organism-specific databases
CTD	35207.
FlyBase	FBgn0024245. dnt.
Phylogenomic databases
eggNOG	inNOG08705.
GeneTree	EMGT00050000002734.
InParanoid	Q9V422.
OMA	QRCRVRL.
OrthoDB	EOG44TMQ9.
PhylomeDB	Q9V422.
Gene expression databases
Bgee	Q9V422.
GermOnline	CG17559. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR001245. Ser-Thr/Tyr_kinase. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. IPR003306. WIF. [Graphical view]
KO	K05128.
Pfam	PF07714. Pkinase_Tyr. 1 hit. PF02019. WIF. 1 hit. [Graphical view]
PRINTS	PR00109. TYRKINASE.
ProDom	PD013948. WIF. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00219. TyrKc. 1 hit. SM00469. WIF. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS50814. WIF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	792369.

Entry information

Entry name

RYK2_DROME

Accession

Primary (citable) accession number: Q9V422
Secondary accession number(s): B9EQS2 , O62533, Q5BII5, Q95TI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 27, 2003
Last sequence update:	January 27, 2003
Last modified:	January 25, 2012
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project