ID   YRK_CHICK               Reviewed;         536 AA.
AC   Q02977;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Proto-oncogene tyrosine-protein kinase Yrk;
DE            EC=2.7.10.2;
DE   AltName: Full=Yes-related kinase;
DE   AltName: Full=p60-Yrk;
GN   Name=YRK;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=White leghorn; TISSUE=Brain, and Kidney;
RX   PubMed=8455940;
RA   Sudol M., Greulich H., Newman L., Sarkar A., Sukegawa J., Yamamoto T.;
RT   "A novel Yes-related kinase, Yrk, is expressed at elevated levels in neural
RT   and hematopoietic tissues.";
RL   Oncogene 8:823-831(1993).
CC   -!- FUNCTION: May participate in signaling pathways.
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=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- TISSUE SPECIFICITY: There are elevated levels of this protein in neural
CC       and hematopoietic tissues.
CC   -!- PTM: Phosphorylated.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; X67786; CAA47996.1; -; mRNA.
DR   PIR; S33569; S33569.
DR   RefSeq; NP_001103257.1; NM_001109787.1.
DR   AlphaFoldDB; Q02977; -.
DR   SMR; Q02977; -.
DR   STRING; 9031.ENSGALP00000043829; -.
DR   PaxDb; 9031-ENSGALP00000007628; -.
DR   Ensembl; ENSGALT00000063550; ENSGALP00000043829; ENSGALG00000032199.
DR   Ensembl; ENSGALT00010040679.1; ENSGALP00010023644.1; ENSGALG00010016861.1.
DR   Ensembl; ENSGALT00015053184; ENSGALP00015031492; ENSGALG00015021774.
DR   GeneID; 777583; -.
DR   KEGG; gga:777583; -.
DR   CTD; 2268; -.
DR   VEuPathDB; HostDB:geneid_777583; -.
DR   eggNOG; KOG0197; Eukaryota.
DR   GeneTree; ENSGT00940000157554; -.
DR   InParanoid; Q02977; -.
DR   OMA; INHYTES; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; Q02977; -.
DR   BRENDA; 2.7.10.2; 1306.
DR   Reactome; R-GGA-2029481; FCGR activation.
DR   Reactome; R-GGA-432142; Platelet sensitization by LDL.
DR   Reactome; R-GGA-6798695; Neutrophil degranulation.
DR   PRO; PR:Q02977; -.
DR   Proteomes; UP000000539; Chromosome 23.
DR   Bgee; ENSGALG00000032199; Expressed in lung and 11 other cell types or tissues.
DR   ExpressionAtlas; Q02977; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0016235; C:aggresome; IEA:Ensembl.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0034988; F:Fc-gamma receptor I complex binding; IEA:Ensembl.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0032815; P:negative regulation of natural killer cell activation; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR   GO; GO:0043306; P:positive regulation of mast cell degranulation; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR   GO; GO:0045088; P:regulation of innate immune response; IEA:Ensembl.
DR   GO; GO:0050764; P:regulation of phagocytosis; IEA:Ensembl.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd14203; PTKc_Src_Fyn_like; 1.
DR   CDD; cd10418; SH2_Src_Fyn_isoform_a_like; 1.
DR   CDD; cd12006; SH3_Fyn_Yrk; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR047924; Fyn/Yrk_SH2.
DR   InterPro; IPR035750; Fyn/Yrk_SH3.
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; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF224; TYROSINE-PROTEIN KINASE FGR; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Lipoprotein; Myristate; Nucleotide-binding; Palmitate;
KW   Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain; SH3 domain;
KW   Transferase; Tyrosine-protein kinase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..536
FT                   /note="Proto-oncogene tyrosine-protein kinase Yrk"
FT                   /id="PRO_0000088188"
FT   DOMAIN          81..142
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          148..245
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          270..523
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          10..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        389
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         276..284
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         298
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         419
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         530
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           6
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   536 AA;  60002 MW;  61BB5DEE000EE993 CRC64;
     MGCVHCKEKI SGKGQGGSGT GTPAHPPSQY DPDPTQLSGA FTHIPDFNNF HAAAVSPPVP
     FSGPGFYPCN TLQAHSSITG GGVTLFIALY DYEARTEDDL SFQKGEKFHI INNTEGDWWE
     ARSLSSGATG YIPSNYVAPV DSIQAEEWYF GKIGRKDAER QLLCHGNCRG TFLIRESETT
     KGAYSLSIRD WDEAKGDHVK HYKIRKLDSG GYYITTRAQF DTIQQLVQHY IERAAGLCCR
     LAVPCPKGTP KLADLSVKTK DVWEIPRESL QLLQKLGNGQ FGEVWMGTWN GTTKVAVKTL
     KPGTMSPEAF LEEAQIMKRL RHDKLVQLYA VVSEEPIYIV TEFMSQGSLL DFLKDGDGRY
     LKLPQLVDMA AQIAAGMAYI ERMNYIHRDL RAANILVGDN LVCKIADFGL ARLIEDNEYT
     ARQGAKFPIK WTAPEAALFG KFTIKSDVWS FGILLTELVT KGRVPYPGMN NREVLEQVER
     GYRMQCPGGC PPSLHDVMVQ CWKREPEERP TFEYLQSFLE DYFTATEPQY QPGDNQ
//