PTK7_DROMO
ID PTK7_DROMO Reviewed; 1045 AA.
AC B4KPU0;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=GI18649;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1] {ECO:0000312|EMBL:EDW10217.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW10217.1};
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; CH933808; EDW10217.1; -; Genomic_DNA.
DR RefSeq; XP_002006282.1; XM_002006246.2.
DR AlphaFoldDB; B4KPU0; -.
DR SMR; B4KPU0; -.
DR STRING; 7230.FBpp0167866; -.
DR EnsemblMetazoa; FBtr0169374; FBpp0167866; FBgn0141388.
DR GeneID; 6580444; -.
DR KEGG; dmo:Dmoj_GI18649; -.
DR eggNOG; KOG1026; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR HOGENOM; CLU_012268_0_0_1; -.
DR InParanoid; B4KPU0; -.
DR OMA; AYDKRVY; -.
DR OrthoDB; 530072at2759; -.
DR PhylomeDB; B4KPU0; -.
DR ChiTaRS; otk; fly.
DR Proteomes; UP000009192; 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; 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; 5.
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1045
FT /note="Tyrosine-protein kinase-like otk"
FT /evidence="ECO:0000255"
FT /id="PRO_0000388688"
FT TOPO_DOM 26..587
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 609..1045
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..116
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 115..200
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 260..373
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 376..469
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 474..564
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255"
FT DOMAIN 695..1040
FT /note="Protein kinase; inactive"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT REGION 628..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AWJ9"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 139..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 285..362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 406..453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 496..548
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1045 AA; 114469 MW; 23396C81E7090221 CRC64;
MPIVMDMNML LMLSLAFTVM APASASSSRF TQPPQSQAIV ENDAADFSCE ATGPSGDLHY
EWLHNGQQIG YDSRVLQIGS NLRIESVQRE DAGDYVCIAA SAASGARQAS PPAKLSVIFL
DAVTVQLLGS NRNELLLKCH VEGASGDEPL QIEWYRDSAK LSSWQNVELQ QHRLLVRQPS
SADDGLYRCI ASNAAARVMS KQGYVYEHLA SVAPGSTKCL PKLKRNQKMP ESWGKQVFLC
RGKRGGSTGM DQSQSLPPSP EGLRIVQGPN DKLIIKEGEP TTLSCLYELP AELQNQRIQL
RWRKDGKILR HVELGDAVVP GLALDHGKDA LVREDGRLVL HKQNGTLSFN SIIASDAGQY
MCQIQLEGHA PVNSAPGALE VIEQLKFMPQ PTSKNLELGA LGKLHCKAQG TPTPQVQWLR
DAANGSLPEH VDDINGTLIF RNVSAEHRGN YTCVASNSQG QINATVAINV VVAPRFSVAP
EGPIESSEQG VAVIHCQAIG DPKPTIQWDK DLKYLSENNT DRQRFSFLEN GTLEIRNVQA
EDEGKYGCTI GNSAGLKREE VRLLVRGNGD GFITEESAGD GFLVTRAVLI TMTVALAYIV
LVVGLMLWCR YRRQARKARL NELSIKEAGG DQAESGKNTE QEPCLSKQRN GHGKSRTAAN
GDAQKSDDTA CSQQSKASKK SAHIYEQLAL PRSGLSELIQ IGRGEFGDVF VGKLKASLVA
AASPSDKDAD TEKQHSNSEN GSGASGASGC GSGSTTLSTL NEKRRSKTSM DDIEEIKEEE
QPQEQAQSES TADLLVMVKA LNKVKDEQAC QEFRRQLDLL RAISHKGVVR LFGLCREKDP
HYMVLEYTDW GDLKQFLLAT AGKVNTATAT SSPPPLTTSQ LLAVAYQIAR GMDAIYRARF
THRDLATRNC VISSEFIVKV AYPALCKDKY SREYHKHRNT LLPVRWLAPE CIQEDEYTTK
SDIFAFAVVV WELFNQATKL PHEDLSNEQV VQRSLANTLE WSVAEGTPDG LKEILLSCWL
TNPKERPSFS QLGAALSKAM QAAEK
