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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
 
 
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