ID   RYK_AVIR3               Reviewed;         442 AA.
AC   P33497;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Tyrosine-protein kinase transforming protein RYK;
DE            EC=2.7.10.1;
GN   Name=V-RYK;
OS   Avian retrovirus RPL30.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=31671;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1527848; DOI=10.1128/jvi.66.10.5975-5987.1992;
RA   Jia R., Mayer B.J., Hanafusa T., Hanafusa H.;
RT   "A novel oncogene, v-ryk, encoding a truncated receptor tyrosine kinase is
RT   transduced into the RPL30 virus without loss of viral sequences.";
RL   J. Virol. 66:5975-5987(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SUBCELLULAR LOCATION: Host cell membrane.
CC   -!- MISCELLANEOUS: This protein is synthesized as an Env-Ryk polyprotein.
CC       An Env-Ryk precursor fusion protein is first synthesized and then
CC       cellular protease cleaves this precursor into gp85 and the putative
CC       oncogene termed gp69 (gp37-Ryk).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. AXL/UFO subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA42673.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M92847; AAA42673.1; ALT_INIT; mRNA.
DR   PIR; B43362; B43362.
DR   SMR; P33497; -.
DR   BRENDA; 2.7.10.1; 598.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Host cell membrane; Host membrane; Kinase; Membrane;
KW   Nucleotide-binding; Oncogene; Phosphoprotein; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN           1..442
FT                   /note="Tyrosine-protein kinase transforming protein RYK"
FT                   /id="PRO_0000088135"
FT   DOMAIN          45..316
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        181
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         51..59
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         77
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         212
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   442 AA;  49108 MW;  C91E9B8A949F24D4 CRC64;
     TTTVVNYTAK KSYCRRAVEL TLGSLGVSSE LQQKLQDVVI DRNALSLGKV LGEGEFGSVM
     EGRLSQPEGT PQKVAVKTMK LDNFSHREIE EFLSEAACIK DFDHPNVIKL LGVCIELSSQ
     QIPKPMVVLP FMKYGDLHSF LLRSRLEMAP QFVPLQMLLK FMVDIALGME YLSSRQFLHR
     DLAARNCMLR DDMTVCVADF GLSKKIYSGD YYRQGRIAKM PVKWIAIESL ADRVYTTKSD
     VWAFGVTMWE IATRGMTPYP GVQNHEIYEY LFHGQRLKKP ENCLDELYDI MSSCWRAEPA
     DRPTFSQLKV HLEKLLESLP APRGSKDVIY VNTSLPEESP DSTQDLGLDS VIPQADSDLD
     PGDIAEPCCS HTKAALVAVD IHDGGSRYVL ESEGSPTEDA YVPQLPHEGS AWTEASTLPV
     GSSLAAQLPC ADGCLEDSEA LL