PTK7_DROAN
ID PTK7_DROAN Reviewed; 1037 AA.
AC B3MH43;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=GF12649;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1] {ECO:0000312|EMBL:EDV35802.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV35802.1};
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 this protein may
CC associate with, and be phosphorylated by, an unknown active tyrosine
CC kinase. {ECO:0000305}.
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DR EMBL; CH902619; EDV35802.1; -; Genomic_DNA.
DR RefSeq; XP_001958980.1; XM_001958944.2.
DR AlphaFoldDB; B3MH43; -.
DR SMR; B3MH43; -.
DR STRING; 7217.FBpp0115841; -.
DR EnsemblMetazoa; FBtr0117349; FBpp0115841; FBgn0089685.
DR GeneID; 6495498; -.
DR KEGG; dan:6495498; -.
DR eggNOG; KOG1026; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR HOGENOM; CLU_012268_0_0_1; -.
DR InParanoid; B3MH43; -.
DR OMA; AYDKRVY; -.
DR OrthoDB; 530072at2759; -.
DR PhylomeDB; B3MH43; -.
DR ChiTaRS; otk; fly.
DR Proteomes; UP000007801; 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; 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; 2.
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 Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1037
FT /note="Tyrosine-protein kinase-like otk"
FT /evidence="ECO:0000255"
FT /id="PRO_0000388686"
FT TOPO_DOM 23..582
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..1037
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..115
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 114..200
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 252..366
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 369..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 694..1035
FT /note="Protein kinase; inactive"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT REGION 618..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AWJ9"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
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 458
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 46..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 138..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 277..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 400..448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 491..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1037 AA; 114234 MW; 7942944D4A6C663D CRC64;
MAALRISVWI LVQALMMALV SSNSSHFLQL PQSQSVVENE SVDFECQAST DPSSELHYEW
LHNGHRIAYD KRVYQIGSHL HIEAVQRAED VGDYVCIATS LASGAREASP PAKLSVIYID
SASVQLLGSN RNELLLKCHV EAVSGSDDPL QIEWYRNSAK LSSWQNVQLD QHRLIIRQPS
AADDGLYRCT ASNAAGRVMS KQGYVYRSSL KCLPRLPRRK NQKLPESWSK EVFLCRGKRG
GSGGVEALPS APEDLRIVQG PASHAIIKEG DPAALTCLYE LPAELQNQRI QLRWRKDGKL
LRHVELGNSL PLPGISSDSG KDALLREDAR LVLHKQNGTL SFASIIASDA GQYQCQLQLE
GYAPINSSPG TLEVIEQLKF VPQPTSKNLE LDAPIAKVHC KAQGTPTPQV QWMRDDANTS
LPDQVEVDAN GTLIFRNVNA DHRGNYTCLA TNSQGQINAT VAINVVVTPK FSVPPVGPIE
TAEQGNVVIH CQAIGDPKPT IQWDKDLTYL SENNTDRERF RFLENGTLEI RNVQAEDEGS
YGCTIGNSAG LKREDVQLVV KTAGDGFPPE ESGGDGFLVT RAVLITMTVA LAYIVLVVGL
MLWCRYRRQA RKARLNELST KEAGGDQPDG AANGKGSEQE PCLSKQRNGH GGQSRSKSNG
DAQKSDDTAC SQQSRASKKS AHIYEQLALP RSGLTELIQI GRGEFGDVFV GKLKASLVAT
GSPSDKDADT EKQHSNSENG SGGSGSGSTT LSTLNEKRRS KTSMDDIEEI KEEEQEQQQS
DLDQLVLVKA LNKVKDEQAC QEFRRQLDLL RGISHKGVVR LFGLCREKDP HYMVLEYTDW
GDLKQFLLAT AGKVNTASAA ATSSPPPLTT SQVLAVAYQI ARGMDAIYRA RFTHRDLATR
NCVISSEFIV KVSYPALCKD KYSREYHKHR NTLLPIRWLA PECIQEDEYT TKSDIFAYGV
VVWELFNQAT KLPHEELTNE QVIQKSQAGT LEWTVAESTP DSLREILLSC WVSNPKERPS
FSQLGAALSK AMQSLEK
