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Q6AWJ9 (PTK7_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase-like otk
Alternative name(s):
Gp160-Dtrk
Short name=Dtrk
Off-track
Tyrosine-protein kinase-like 7 homolog
Gene names
Name:otk
ORF Names:CG8967
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1033 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in the adult visual system to innervate the lamina layer; specific targeting of R1-R6 axons. Ref.1 Ref.5 Ref.6

Subunit structure

Interacts with plexA; component of a receptor complex that mediates the repulsive signaling in response to Semaphorin ligands. Ref.5

Subcellular location

Cell membrane; Single-pass type I membrane protein Ref.1.

Tissue specificity

Dynamically expressed during embryogenesis in several areas of the developing nervous system, including neurons and fasciculating axons. Expression in stage 7 embryos is seen in the anterior midgut primordia, cephalic furrow and along the germinal band. At stage 11, expression is in 15 stripes over the trunk region, and in the anterior and posterior midgut primordia. Stage 12 shows expression in the developing nervous system, procephalic lobe and maxillar bud. Stage 13 shows expression in the ventral cord, maxillar segment and in three regions of the gut. At stage 16 expression is preferentially detected throughout the nervous system, including the neuromers in the ventral cord and the supraoesophageal ganglion (at protein level). In larva, expression is seen in developing R cells and is localized predominantly to R1-R6 growth cones. Ref.1 Ref.6

Developmental stage

Expressed both maternally and zygotically, during early to mid embryogenesis and early pupation. Ref.1

Disruption phenotype

Axon guidance defects. R-cell differentiation and cell fate determination are normal, but many R1-R6 axons connect abnormally to medulla instead of innervating lamina. Ref.5 Ref.6

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.

Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Caution

This protein has been proposed to undergo autophosphorylation on tyrosine residues which is induced in response to cell adhesion (Ref.1). However as mammalian orthologs of this protein seem to lack kinase activity this protein may associate with, and be phosphorylated by, an unknown active tyrosine kinase.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 10331011Tyrosine-protein kinase-like otk
PRO_5000145927

Regions

Topological domain23 – 581559Extracellular Potential
Transmembrane582 – 60221Helical; Potential
Topological domain603 – 1033431Cytoplasmic Potential
Domain25 – 11490Ig-like C2-type 1
Domain113 – 19987Ig-like C2-type 2
Domain251 – 365115Ig-like C2-type 3
Domain368 – 46396Ig-like C2-type 4
Domain468 – 55891Ig-like C2-type 5
Domain692 – 1028337Protein kinase; inactive

Amino acid modifications

Modified residue6781Phosphoserine Ref.7
Glycosylation391N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4291N-linked (GlcNAc...) Potential
Glycosylation4441N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential
Glycosylation5121N-linked (GlcNAc...) Potential
Glycosylation5241N-linked (GlcNAc...) Ref.8
Disulfide bond46 ↔ 95 By similarity
Disulfide bond137 ↔ 188 By similarity
Disulfide bond276 ↔ 354 By similarity
Disulfide bond399 ↔ 447 By similarity
Disulfide bond490 ↔ 542 By similarity

Experimental info

Sequence conflict2211E → Q in CAA45053. Ref.1
Sequence conflict2391G → S in ACQ91629. Ref.4
Sequence conflict2711P → H in CAA45053. Ref.1
Sequence conflict3111I → F in CAA45053. Ref.1
Sequence conflict4021Q → L in ACQ91629. Ref.4
Sequence conflict6291V → I in CAA45053. Ref.1
Sequence conflict7721D → E in CAA45053. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6AWJ9 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 559659540BDE66F5

FASTA1,033114,267
        10         20         30         40         50         60 
MTARMISICG LVMALMMASV LASSSRFQRV PQSQSVVENE SVKFECESTD SYSELHYDWL 

        70         80         90        100        110        120 
HNGHRIAYDK RVHQIGSNLH IEAVRRTEDV GNYVCIATNL ASGAREASPP AKLSVIYLES 

       130        140        150        160        170        180 
ASVQLLGSNR NELLLKCHVE GASGDLEPLE IEWYRNSEKL STWKNVQLDQ HRLIIRQPGS 

       190        200        210        220        230        240 
EDDGLYRCTA SNAAGRVMSK QGYVYQSSVK CLPRLPRRKN EKMMESWDKQ TFLCRGKRGG 

       250        260        270        280        290        300 
AAGLEALPAA PEDLRIVQGP IGQSIIKEGE PTALTCLYEL PDELKNQRIQ LRWRKDGKLL 

       310        320        330        340        350        360 
RQVELGGSAP IPGHSFDSGK DALLREDARL VLHKQNGTLS FASIIASDAG QYQCQLQLEA 

       370        380        390        400        410        420 
HAPINSSPGI LEVIEQLKFV PQPTSKNLEL DAVVAKVHCK AQGTPTPQVQ WVRDGENTTL 

       430        440        450        460        470        480 
PDHVEVDANG TLIFRNVNSE HRGNYTCLAT NSQGQINATV AINVVVTPKF SVPPVGPIET 

       490        500        510        520        530        540 
SEQGTVVMHC QAIGDPKPTI QWDKDLKYLS ENNTDRERFR FLENGTLEIR NVQVEDEGSY 

       550        560        570        580        590        600 
GCTIGNSAGL KREDVQLVVK TTGDGFAPEE SGGDGFLVTR AVLITMTVAL AYIVLVVGLM 

       610        620        630        640        650        660 
LWCRYRRQAR KARLNDLSTK EAGGDQPDVA GNGKGSEQEP CLSKQHNGHS KSRSKSSGDA 

       670        680        690        700        710        720 
QKSDDTACSQ QSRASKKSAH IYEQLALPRS GLSELIQIGR GEFGDVFVGK LKATLVTSPS 

       730        740        750        760        770        780 
DKDADTEKQH SNSENGSGGS GSGSTTLSTL NEKRRSKTSM DDIEEIKEEE QDQHNQSGLE 

       790        800        810        820        830        840 
QLVLVKALNK VKDEQACQEF RRQLDLLRAI SHKGVVRLFG LCREKDPHYM VLEYTDWGDL 

       850        860        870        880        890        900 
KQFLLATAGK VNTATAGSSS PPPLTTSQVL AVAYQIARGM DAIYRARFTH RDLATRNCVI 

       910        920        930        940        950        960 
SSEFIVKVSY PALCKDKYSR EYHKHRNTLL PIRWLAPECI QEDEYTTKSD IFAYGVVVWE 

       970        980        990       1000       1010       1020 
LFNQATKLPH EELTNEQVVQ RSQAGSLEWS VAEATPDSLR EILLSCWVSN PKERPSFSQL 

      1030 
GAALSKAMQS AEK 

« Hide

References

« Hide 'large scale' references
[1]"Dtrk, a Drosophila gene related to the trk family of neurotrophin receptors, encodes a novel class of neural cell adhesion molecule."
Pulido D., Campuzano S., Koda T., Modolell J., Barbacid M.
EMBO J. 11:391-404(1992) [PubMed: 1371458] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Canton-S.
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. expand/collapse author list , 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. expand/collapse author list , 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]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 (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Larva and Pupae.
[5]"The transmembrane protein Off-track associates with Plexins and functions downstream of Semaphorin signaling during axon guidance."
Winberg M.L., Tamagnone L., Bai J., Comoglio P.M., Montell D., Goodman C.S.
Neuron 32:53-62(2001) [PubMed: 11604138] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PLEXA, DISRUPTION PHENOTYPE.
[6]"The receptor tyrosine kinase Off-track is required for layer-specific neuronal connectivity in Drosophila."
Cafferty P., Yu L., Rao Y.
Development 131:5287-5295(2004) [PubMed: 15456725] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[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: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, MASS SPECTROMETRY.
Tissue: Embryo.
[8]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-524, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63453 mRNA. Translation: CAA45053.1.
AE013599 Genomic DNA. Translation: AAF58596.1.
BT015249 mRNA. Translation: AAT94478.1.
BT083425 mRNA. Translation: ACQ91629.1.
PIRS19247.
RefSeqNP_523705.2. NM_078981.2.
UniGeneDm.2582.

3D structure databases

ProteinModelPortalQ6AWJ9.
SMRQ6AWJ9. Positions 23-205, 334-563, 683-1030.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6AWJ9.

Proteomic databases

PRIDEQ6AWJ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088028; FBpp0087135; FBgn0004839.
GeneID36283.
KEGGdme:Dmel_CG8967.
NMPDRfig|7227.3.peg.4735.
UCSCCG8967-RA. d. melanogaster.

Organism-specific databases

CTD36283.
FlyBaseFBgn0004839. otk.

Phylogenomic databases

GeneTreeEMGT00050000001149.
InParanoidQ6AWJ9.
OMASENNTDR.
OrthoDBEOG4866TH.
PhylomeDBQ6AWJ9.

Gene expression databases

ArrayExpressQ6AWJ9.
BgeeQ6AWJ9.

Family and domain databases

InterProIPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR001245. Ser-Thr/Tyr_kinase.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 5 hits.
KOK05127.
PfamPF07679. I-set. 4 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00409. IG. 2 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS50835. IG_LIKE. 5 hits.
PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio797729.

Entry information

Entry namePTK7_DROME
AccessionPrimary (citable) accession number: Q6AWJ9
Secondary accession number(s): C4IXZ4, Q24327
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: October 3, 2006
Last modified: January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families