PTK7_DROWI
ID PTK7_DROWI Reviewed; 1059 AA.
AC B4MR28;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=GK21983;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1] {ECO:0000312|EMBL:EDW74567.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24 {ECO:0000312|EMBL:EDW74567.1};
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; CH963849; EDW74567.1; -; Genomic_DNA.
DR RefSeq; XP_002063581.2; XM_002063545.2.
DR AlphaFoldDB; B4MR28; -.
DR SMR; B4MR28; -.
DR STRING; 7260.FBpp0251126; -.
DR EnsemblMetazoa; FBtr0415618; FBpp0373824; FBgn0223968.
DR eggNOG; KOG1026; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR HOGENOM; CLU_012268_0_0_1; -.
DR InParanoid; B4MR28; -.
DR OMA; AYDKRVY; -.
DR PhylomeDB; B4MR28; -.
DR ChiTaRS; otk; fly.
DR Proteomes; UP000007798; 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; 3.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1059
FT /note="Tyrosine-protein kinase-like otk"
FT /evidence="ECO:0000255"
FT /id="PRO_0000388693"
FT TOPO_DOM 24..597
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 619..1059
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..112
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 113..202
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 258..377
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 380..475
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 480..570
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255"
FT DOMAIN 712..1055
FT /note="Protein kinase; inactive"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT REGION 639..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AWJ9"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
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 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 141..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 283..366
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 411..459
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 502..554
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1059 AA; 117097 MW; C5EBBAE79D3F8729 CRC64;
MDMLMMWSIC LFVCIFMAPF SCGSGSSSRF IQVPESQSIV ENDSVDFNCE ATTDPSTDLH
YEWLHNGHQI VYDKRVYQIG ANLHIESVQR GEDVGDYVCI AMSLSSGARE ASPTAKLSVI
FLDSASVQLL GSNRNELLLK CHVEGASGNE ALQIEWYRNS AKLSSWQNIE LDEHRLLVRQ
PTGSDDGLYR CIASNAAGRV MSKQGFVYQH QQQQQAGAKC LPRLKKNQKF LPESWGKQIF
LCRGKRGGNV EAGLAPSPEG LRLVQGPDDQ ITIKEGEPAT LSCLYEIPAE LQNQRIQLRW
RKDGKLLRQV ELGASLPRGM GNPHNGHSLD GKDALLREDA RLVLHKANGT LSFGTVIASD
AGQYQCQLQM EGHLAINSSP GILEVIEQLK FMPQPTSKNL ELDAAVAKVH CKAQGTPTPQ
VQWFRDGVNT TLPDQVEVDL NGTLIFRNVN ADHRGNYTCL ATNLQGQINA TVSINVVVAP
KFSVPPNVPM EIAEQSTVVI HCQAIGDPKP TIQWDKDLLY LSENNTDRQR FSFLENGTLE
IRNVQAEDEG RYGCTIGNSA GLKREEAVLT VKTSSTGGGG YVTEESSGDG GFLATRAVLI
TMTVALAYIV LVVGLMLWCR YRRQARKARL NELSIKEAGG EQAGGEGSTS GNPKASEQEP
CLGKQQRNGR NGKSKSNGDP QKSDDTACSQ QSRASKKSAH IYEQLALPRS GLSELIQIGR
GDFGDVFVGK LKASLVNNAQ ANDKDSDNDK QHSNSENGSG GSSGSTTLST LNEKRRSKTS
MDDIEEIKEE EQEQQQSQQQ QQQDQLVMVK ALNKVKDEQA CQEFRRQLDL LRALSHKGIV
RLYGLCREKD PHYLVLEYTD WGDLKQFLLA TAGKVNTATT ATSSTTPLPP LTTSQVLAVA
YQIARGMDAI YRARFTHRDL ATRNCVISSE FIVKVSYPAL CKDKYSREYH KHRNSLLPIR
WLAPECIQED EYTTKSDIFS YGVVVWELFN QATKLPHEDL TNEQVIEKSQ DGTLKWTVAE
STPESLKEIL LSCWSVNPKQ RPSFSQLGAA LSKAMQNSE
