PTK7_DROYA
ID PTK7_DROYA Reviewed; 1033 AA.
AC B4P5Q9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Tyrosine-protein kinase-like otk {ECO:0000250|UniProtKB:Q6AWJ9};
DE AltName: Full=Tyrosine-protein kinase-like 7 homolog;
DE Flags: Precursor;
GN Name=otk {ECO:0000250|UniProtKB:Q6AWJ9}; ORFNames=GE13482;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1] {ECO:0000312|EMBL:EDW90856.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW90856.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion
CC molecule that regulates neural recognition during the development of
CC the nervous system. Component of the repulsive Plexin signaling
CC response to regulate motor axon guidance at the embryonic stage. Also
CC component of a receptor complex that is required in the adult visual
CC system to innervate the lamina layer; specific targeting of R1-R6 axons
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with plexA; component of a receptor complex that
CC mediates the repulsive signaling in response to Semaphorin ligands.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- CAUTION: The D.melanogaster ortholog of this protein has been proposed
CC to undergo autophosphorylation on tyrosine residues which is induced in
CC response to cell adhesion (PubMed:1371458). However as mammalian
CC orthologs of this protein seem to lack kinase activity it may be that
CC this protein associates with, and is phosphorylated by, an unknown
CC active tyrosine kinase. {ECO:0000305}.
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DR EMBL; CM000158; EDW90856.1; -; Genomic_DNA.
DR RefSeq; XP_002091144.1; XM_002091108.2.
DR AlphaFoldDB; B4P5Q9; -.
DR SMR; B4P5Q9; -.
DR STRING; 7245.FBpp0258492; -.
DR EnsemblMetazoa; FBtr0260000; FBpp0258492; FBgn0231151.
DR GeneID; 6530206; -.
DR KEGG; dya:Dyak_GE13482; -.
DR eggNOG; KOG1026; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR HOGENOM; CLU_012268_0_0_1; -.
DR OMA; AYDKRVY; -.
DR OrthoDB; 530072at2759; -.
DR PhylomeDB; B4P5Q9; -.
DR ChiTaRS; otk; fly.
DR Proteomes; UP000002282; Chromosome 2R.
DR GO; GO:0030424; C:axon; IEA:EnsemblMetazoa.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:EnsemblMetazoa.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:EnsemblMetazoa.
DR GO; GO:0017147; F:Wnt-protein binding; IEA:EnsemblMetazoa.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0048804; P:imaginal disc-derived female genitalia morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0035260; P:internal genitalia morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IEA:EnsemblMetazoa.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 5.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein; Receptor;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1033
FT /note="Tyrosine-protein kinase-like otk"
FT /evidence="ECO:0000255"
FT /id="PRO_0000388694"
FT TOPO_DOM 23..581
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..1033
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..114
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 113..199
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 251..365
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 368..463
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 468..558
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255"
FT DOMAIN 692..1028
FT /note="Protein kinase; inactive"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT REGION 617..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AWJ9"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 137..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 276..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 399..447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 490..542
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1033 AA; 114148 MW; A81E7292E52A76A1 CRC64;
MTARMISIYG LVLASMMASV LASSSRFQRL PQSQSVVENE SVKFECESTD SYSELHYDWL
HNGHRIAYDK RVHQIGSNLH IEAVRRTEDV GSYVCIATNL ASGAREASPP AKLSVIYIES
ASVQLLGSNR NELLLKCHVE GASGDSEPLE IEWYRNSEKL STWRNVQLDQ HRLIVRQPGS
DDDGLYRCTA SNAAGRVMSK QGYVYQSSVK CLPRLARRKS QKVMESWDKQ TFLCRGKRGG
AAGLEALPAA PEDLRIVQGP IAQSIIKEGE PTALTCLYEL PDELKNQRIQ LRWRKDGKLL
RQVELGGSAP ISGHSFDSGK DALLREDARL VLHKQNGTLS FASIIASDAG QYQCQLQLEA
HVPVSSSPGV LEVIEQLKFV PQPTSKNLEL DAVVAKVHCK AQGTPTPQVQ WVREGENNTL
PDQVEVDANG TLIFRNVNSE HRGNYTCLAT NTQGQINATV AINVVVTPKF SVPPVGPIET
AELGTVVIHC QAIGDPKPTI QWDKDLKYLS ENNTDRERFR FLENGTLEIR NVQVEDEGSY
GCTIGNSAGL KREDVQLIVK TTGDGFAPEE SGGDGFLVTR AVLITMTVAL AYIVLVVGLM
LWCRYRRQAR KARLNDLSTK EAGGDQPDAT GNGKGSEQEP CLSKQHNGHS KSRSKSSGDA
QKSDDTACSQ QSRASKKSAH IYEQLALPRS GLSELIQIGR GEFGDVFVGK LKATLVTSPS
DKDADTEKQH SNSENGSGGS GSGSTTLSTL NEKRRSKTSM DDIEEIKEEE QEQHNQSGLE
QLVLVKALNK VKDEQACQEF RRQLDLLRAI SHKGVVRLFG LCREKDPHYM VLEYTDWGDL
KQFLLATAGK VNTATAGSSS PPPLTTSQVL AVAYQIARGM DAIYRARFTH RDLATRNCVI
SSEFIVKVSY PALCKDKYSR EYHKHRNTLL PIRWLAPECI QEDEYTTKSD IFAYGVVVWE
LFNQATKLPH EELTNEQVVQ RSQAGSLEWS VAESTPDSLR EILLSCWVAN PKERPSFSQL
GAALSKAMQS AEK
