PTK7_DROSE
ID PTK7_DROSE Reviewed; 1029 AA.
AC B4HNW4;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=GM20393;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1] {ECO:0000312|EMBL:EDW47479.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25 {ECO:0000312|EMBL:EDW47479.1};
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; CH480816; EDW47479.1; -; Genomic_DNA.
DR RefSeq; XP_002033466.1; XM_002033430.1.
DR AlphaFoldDB; B4HNW4; -.
DR SMR; B4HNW4; -.
DR STRING; 7238.B4HNW4; -.
DR EnsemblMetazoa; FBtr0203378; FBpp0201870; FBgn0175276.
DR GeneID; 6608743; -.
DR KEGG; dse:6608743; -.
DR HOGENOM; CLU_012268_0_0_1; -.
DR OMA; AYDKRVY; -.
DR PhylomeDB; B4HNW4; -.
DR ChiTaRS; otk; fly.
DR Proteomes; UP000001292; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1029
FT /note="Tyrosine-protein kinase-like otk"
FT /evidence="ECO:0000255"
FT /id="PRO_0000388691"
FT TOPO_DOM 19..577
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..1029
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..104
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 105..195
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 247..361
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 364..459
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT DOMAIN 464..554
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255"
FT DOMAIN 688..1024
FT /note="Protein kinase; inactive"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT REGION 613..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AWJ9"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 133..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 272..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 395..443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 486..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1029 AA; 113875 MW; CF91BA46AFC36E88 CRC64;
MISIYGLVMA LMMASVLASS SRFQRVPQSQ SVVENESVKF ECESTDSYSE LHYDWLHNAH
RIAYDKRVHQ IGSNLHIEAV RRTEDVGNYV CIATNLASGA REASPPAKLS VIYLESASVQ
LLGSNRNELL LKCHVEGASG DLEPLEIEWY RNSEKLSTWK NVQLDQHRLI IRQPGSEDDG
LYRCTASNAA GRVMSKQGYV YQSSVKCLPR LPRRKNQKMM ESWDKQTFLC RGKRGGAAGL
ESLPAAPEDL RIVQGPVGQS IIKEGEPTAL TCLYELPDEL KNQRIQLRWR KDGKLLRQVE
LGGSAPIIGH SFDSGKDALL REDARLVLHK QNGTLSFASI IASDAGQYQC QLQLEAHAPI
SSSPGILEVI EQLKFVPQPT SKNLELDAVV AKVHCKAQGT PTPQVQWIRD GENTTLPDQV
EVDANGTLIF RNVNSEHRGN YTCLATNTQG QINATVAINV VVTPKFSVPP VGPIETSEQG
TAVMHCQAIG DPKPTIQWDK DLKYLSENNT DRERFRFLEN GTLEIRNVQV EDEGSYGCTI
GNSAGLKRED VQLVVKTTGD GFAPEESGGD GFLVTRAVLI TMTVALAYIV LVVGLMLWCR
YRRQARKARL NDLSTKEAGG EQPDAAGNGK GSEQEPCLSK QHNGHSKSRS KSSGDAQKSD
DTACSQQSRA SKKSAHIYEQ LALPRSGLSE LIQIGRGEFG DVFVGKLKAT LVTSPSDKDA
DTEKQHSNSE NGSGGSGSGS TTLSTLNEKR RSKTSMDDIE EIKEEEQEQH NQSGLDQLVL
VKALNKVKDE QACQEFRRQL DLLRAISHKG VVRLFGLCRE KDPHYMVLEY TDWGDLKQFL
LATAGKVNTA TAGSSSPPPL TTSQVLAVAY QIARGMDAIY RARFTHRDLA TRNCVISSEF
IVKVSYPALC KDKYSREYHK HRNTLLPIRW LAPECIQEDE YTTKSDIFAY GVVVWELFNQ
ATKLPHEELT NEQVVQRSQA GSLEWSVAEA TPDSLREILL SCWVSNPKER PSFSQLGAAL
SKAMQIAEK
