ID G3UR27_MELGA Unreviewed; 800 AA.
AC G3UR27;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000632};
DE EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000632};
GN Name=FER {ECO:0000313|Ensembl:ENSMGAP00000018126.2};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000018126.2, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000018126.2, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000018126.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001149,
CC ECO:0000256|PIRNR:PIRNR000632};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|PIRNR:PIRNR000632}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fes/fps subfamily. {ECO:0000256|PIRNR:PIRNR000632}.
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DR AlphaFoldDB; G3UR27; -.
DR Ensembl; ENSMGAT00000020039.2; ENSMGAP00000018126.2; ENSMGAG00000006831.3.
DR GeneTree; ENSGT00940000154997; -.
DR InParanoid; G3UR27; -.
DR Proteomes; UP000001645; Chromosome Z.
DR Bgee; ENSMGAG00000004008; Expressed in testis and 15 other cell types or tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0008289; F:lipid binding; IEA:Ensembl.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:Ensembl.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IEA:Ensembl.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IEA:Ensembl.
DR GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; IEA:Ensembl.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
DR GO; GO:0006935; P:chemotaxis; IEA:Ensembl.
DR GO; GO:0050904; P:diapedesis; IEA:Ensembl.
DR GO; GO:0035426; P:extracellular matrix-cell signaling; IEA:Ensembl.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0038109; P:Kit signaling pathway; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010762; P:regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0036119; P:response to platelet-derived growth factor; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR CDD; cd05085; PTKc_Fer; 1.
DR CDD; cd10361; SH2_Fps_family; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.287.160; HR1 repeat; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR035849; Fes/Fps/Fer_SH2.
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; IPR016250; Tyr-prot_kinase_Fes/Fps.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF227; TYROSINE-PROTEIN KINASE FER; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR PIRSF; PIRSF000632; TyrPK_fps; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS51741; F_BAR; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000632, ECO:0000256|PIRSR:PIRSR000632-
KW 2};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Cytoplasm {ECO:0000256|PIRNR:PIRNR000632};
KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR000632};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000632};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000632,
KW ECO:0000256|PIRSR:PIRSR000632-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000632};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000632}.
FT DOMAIN 1..237
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 438..528
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 541..795
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT COILED 331..358
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 662
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-1"
FT BINDING 547..555
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-2"
FT BINDING 569
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 800 AA; 92061 MW; 2E30ED0058CC9CC8 CRC64;
MGFGSDLKYS HDALLKLQDW ELRLLETVKK FMVMRVKSDK EYASTLQNLC NQVDKESTCQ
LDYISNVSKS WLLVVQQTEQ LSKIMKTHAE DLNSGPLHRL TMMIKDKQQV KKSYIGVHQQ
IEAEMYKVTK TELEKLKSRK ETEKAKDRCD KATMKLHMLH NQYVLALKGA QLYQHQYYDT
TLPLLLDSLQ KMQEEMIKAL KGILDEYSQI TSLVTEEIVN VHKEIQTSVE QIDPNSEYND
FIDTHRSSEV VEQEIEFDTS LLEENENLQA NEIMWNNLTA ESLQVMLKTV IEELIQTQQT
LLSKEELVLE LEKKIEDSSK TCEKKSDIVL LLSQKQALEE LKQTVQQLRC SEAKFAAQKE
LLEQKVQEND GKEPPPVVNY EEDARSVTSM DKKDKVSRFD TIRHSIAGII RSPKSMLGSS
SFFDVISTTE KPLAEQDWYH GAIPRIEAQE LLKQQGDFLV RESHGKPGEY VLSVFSDGQR
RHFIIQYADN QYRFEGTGFP TIPQLIEHHY TTKQVITKKS GVVLLNPVVK DKKWVLNHED
VTLGELLGKG NFGEVYKGTL KDKTPVAVKT CKEDLPQELK IKFLSEARIL KQYDHPNIVK
LIGVCTQRQP IYIVMELVPG GDFLSFLRKK KDELKTKQLV KFSLDAASGM AYLESKNCIH
RDLAARNCLV GESNILKISD FGMSRQEDDG VYSSSGLKQI PIKWTAPEAL NYGRYTSESD
VWSFGILLWE TFSLGVCPYP GMTNQQAREQ VEKGYRMSAP QKCPEEIYKI MQRCWDYHPE
NRPKFSEIQK ELSSIKKKVT
//
