PTK7_DROPE
ID PTK7_DROPE Reviewed; 1035 AA.
AC B4GBH0;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=GL11545;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1] {ECO:0000312|EMBL:EDW32272.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479181; EDW32272.1; -; Genomic_DNA.
DR RefSeq; XP_002016382.1; XM_002016346.1.
DR AlphaFoldDB; B4GBH0; -.
DR SMR; B4GBH0; -.
DR STRING; 7234.FBpp0175652; -.
DR EnsemblMetazoa; FBtr0177160; FBpp0175652; FBgn0149154.
DR GeneID; 6589898; -.
DR KEGG; dpe:6589898; -.
DR eggNOG; KOG1026; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR HOGENOM; CLU_012268_0_0_1; -.
DR OMA; AYDKRVY; -.
DR PhylomeDB; B4GBH0; -.
DR ChiTaRS; otk; fly.
DR Proteomes; UP000008744; Unassembled WGS sequence.
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; IPR013106; Ig_V-set.
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; SM00406; IGv; 3.
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 Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1035
FT /note="Tyrosine-protein kinase-like otk"
FT /evidence="ECO:0000255"
FT /id="PRO_0000388689"
FT TOPO_DOM 24..582
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..1035
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..109
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 110..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..464
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 469..559
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255"
FT DOMAIN 693..1029
FT /note="Protein kinase; inactive"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT REGION 623..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AWJ9"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 138..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 276..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 399..448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 491..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1035 AA; 113731 MW; 649EE23B27F0FCAE CRC64;
MDMDVMMISM CILASTLMAP GWASTSGFLR VPQSQSIVEN EAADFGCEAT DPASYLHYEW
LHNGREISYD KRVYRIGSHL HIEAVQREED VGDYVCIATS LASGAREASP PAKLSVIYLE
SASVQLLGSN RNELLLKCHV EGASGDEPLQ IEWYRDSARL ASWGNVHLEE HRLLVRQPSP
SDDGLYRCTA SNAAGRVMSK QGYVYQANIK CLPRLLKKNQ KLPESWGKQT FLCRGKRGGS
GGLDQALSPA PEDLRIVQGP AGQLLIKEGD SAALSCLYEL PAELQNQRIQ LRWRKDGKLL
RHVELGGAIP IPGHAHDSGK DALLREDARL VLHKQNGTLS FASIIASDAG QYQCQLQLEG
HAPLNSSPGL LEVIEQLKFV PQPTSKNLEL DAAVAKVHCK AQGTPSPQVQ WLREGSLNSS
LPDQVEVDIN GTLIFRNVRA EHRGNYTCQA RSSQGQISAT VSINVVVTPK FSVPPVGPIE
TTEQGTVVMH CQAIGDPKPT IQWDKDLKYL SENNTDRERF SFLENGTLEI RNVQVEDEGS
YGCTIGNSAG LKREDVQLVV RSTGDGFAPE ETGGDGFLVT RAVLITMTVA LAYIVLVVGL
MLWCRYRRQA RKARLNELSI KEAGGDQPDA SVTNGKGSEQ EPCLSKQRNG ASGKPKSKSN
GDAQKSDDTA CSQQSRSSKK SVYEQLVLPR SGLSELLQIG RGEFGDVFVG KLKASLVAAS
AQSDKDADTE KQHSNSENGS GGSGSGSGST TLSTLNEKRR SKTSMDDIEE IKEEEPEQSA
LEQLVLVKAL NKVKDEQACQ EFRRQLDLLR GISHKGVVRL FGLCREKDPH YMVLEYTDWG
DLKQFLLATA GKVNTATATS SPPALTTSQV LAVAYQIARG MDAIYRSRCT HRDLATRNCV
ISSEFVVKVS YPALCKDKYS REYHKHRNTL LPVRWLAPEC IQEDEYTTKS DIFAYGVLVW
ELFNQATKLP HEELTSEQVI QRSQAGTLEW TVAEATPDSL KEILLSCWLA NPKERPSFSQ
LGSALSKAMQ SVAEK
