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PTK7_DROSI
ID   PTK7_DROSI              Reviewed;        1029 AA.
AC   B4QC63;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-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=GD25868;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1] {ECO:0000312|EMBL:EDX06694.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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; CM000362; EDX06694.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4QC63; -.
DR   SMR; B4QC63; -.
DR   STRING; 7240.B4QC63; -.
DR   PRIDE; B4QC63; -.
DR   HOGENOM; CLU_012268_0_0_1; -.
DR   OMA; AYDKRVY; -.
DR   PhylomeDB; B4QC63; -.
DR   ChiTaRS; otk; fly.
DR   Proteomes; UP000000304; Chromosome 2r.
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_0000388692"
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..110
FT                   /note="Ig-like C2-type 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          109..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;  113903 MW;  D4AD9E3246540A7C CRC64;
     MISIYGLVMA LMMASVLASS SRFQRVPQSQ SVVENESVKF ECESTDSYSE LHYDWLHNGH
     RIAYDKRVHQ IGSNLHIEAV RRTEDVGNYV CIATNLASGA REASPPAKLS VIYLESASVQ
     LLGSNRNELL LKCHVEGASG DLEPLEIEWY RNSEKLSTWK NVQLDQHRLI IRQPGSEDDG
     LYRCTASNAA GRVMSKQGYV YQSSVKCLPR LPRRKNQKMM ESWDKQTFLC RGKRGGAAGL
     EALPAVPEDL RIVQGPIAQS IIKEGEPTAL TCLYELPDEL KNQRIQLRWR KDGKLLRQVE
     LGGSAPILGH SFDSGKDALL REDARLVLHK QNGTLSFASI IASDAGQYQC QLQLEAHAPI
     SSSPGILEVI EQLKFVPQPT SKNLELDAVV AKVHCKAQGT PTPQVQWIRD GENTTLPDQV
     EVDANGTLIF RNVNSEHRGN YTCLATNTQG QINATVAINV VVTPKFSVPP VGPIETSEQG
     TVVMHCQAIG DPKPTIQWDK DLKYLSENNT DRERFRFLEN GTLEIRNVQV EDEGSYGCTI
     GNSAGLKRED VQLVVKTTGD GFAPEESGGD GFLVTRAVLI TMTVALAYIV LVVGLMLWCR
     YRRQARKARL NDLSTKEAGG DQPDAAGNGK GSEQEPCLSK QHNGHSKSRS KSSGDAQKSD
     DTACSQQSRA SKKSAHIYEQ LALPRSGLSE LIQIGRGEFG DVFVGKLKAT LVTSPSDKDA
     DTEKQHSNSE NGSGGSGSGS TTLSTLNEKR RSKTSMDDIE EIKEEEQEQH NQSGLEQLVL
     VKALNKVKDE QACQEFRRQL DLLRAISHKG VVRLFGLCRE KDPHYMVLEY TDWGDLKQFL
     LATAGKVNTA TAGSSSPPPL TTSQVLAVAY QIARGMDAIY RARFTHRDLA TRNCVISSEF
     IVKVSYPALC KDKYSREYHK HRNTLLPIRW LAPECIQEDE YTTKSDIFAY GVVVWELFNQ
     ATKLPHEELT NEQVVQRSQA GSLEWSVAEA TPDSLREILL SCWVSNPKER PSFSQLGAAL
     SKAMQSAEK
 
 
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