FYN_CHICK
ID FYN_CHICK Reviewed; 534 AA.
AC Q05876;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Tyrosine-protein kinase Fyn;
DE EC=2.7.10.2;
DE AltName: Full=Proto-oncogene c-Fyn;
DE AltName: Full=p59-Fyn;
GN Name=FYN;
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], AND TISSUE SPECIFICITY.
RC STRAIN=White leghorn; TISSUE=Muscle;
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).
RN [2]
RP FUNCTION.
RX PubMed=7496631; DOI=10.1006/mcne.1995.1021;
RA Zisch A.H., D'Alessandri L., Amrein K., Ranscht B., Winterhalter K.H.,
RA Vaughan L.;
RT "The glypiated neuronal cell adhesion molecule contactin/F11 complexes with
RT src-family protein tyrosine kinase Fyn.";
RL Mol. Cell. Neurosci. 6:263-279(1995).
CC -!- FUNCTION: Tyrosine-protein kinase implicated in the control of cell
CC growth. Plays a role in the regulation of intracellular calcium levels.
CC Required in brain development and mature brain function with important
CC roles in the regulation of axon growth, axon guidance, and neurite
CC extension. Role in CNTN1-mediated signaling.
CC {ECO:0000269|PubMed:7496631}.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- ACTIVITY REGULATION: Inhibited by phosphorylation of Tyr-528 by
CC leukocyte common antigen and activated by dephosphorylation of this
CC site. {ECO:0000250}.
CC -!- SUBUNIT: Associates through its SH3 domain, to the p85 subunit of
CC phosphatidylinositol 3-kinase.
CC -!- TISSUE SPECIFICITY: Thymus and spleen. {ECO:0000269|PubMed:8455940}.
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; X52841; CAA37025.1; -; mRNA.
DR PIR; S33568; S33568.
DR PDB; 2L2P; NMR; -; A=85-142.
DR PDB; 2LP5; NMR; -; A=85-142.
DR PDB; 3CQT; X-ray; 1.60 A; A=85-142.
DR PDBsum; 2L2P; -.
DR PDBsum; 2LP5; -.
DR PDBsum; 3CQT; -.
DR AlphaFoldDB; Q05876; -.
DR BMRB; Q05876; -.
DR SMR; Q05876; -.
DR DIP; DIP-738N; -.
DR MINT; Q05876; -.
DR STRING; 9031.ENSGALP00000024180; -.
DR VEuPathDB; HostDB:geneid_396294; -.
DR eggNOG; KOG0197; Eukaryota.
DR InParanoid; Q05876; -.
DR OrthoDB; 539311at2759; -.
DR PhylomeDB; Q05876; -.
DR BRENDA; 2.7.10.2; 1306.
DR EvolutionaryTrace; Q05876; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IDA:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; ISS:AgBase.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:AgBase.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0015631; F:tubulin binding; ISS:AgBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0030900; P:forebrain development; ISS:AgBase.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; ISS:AgBase.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:AgBase.
DR GO; GO:0008360; P:regulation of cell shape; ISS:AgBase.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd12006; SH3_Fyn_Yrk; 1.
DR Gene3D; 3.30.505.10; -; 1.
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 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; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 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.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Developmental protein; Kinase; Lipoprotein;
KW Manganese; Metal-binding; 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..534
FT /note="Tyrosine-protein kinase Fyn"
FT /id="PRO_0000088098"
FT DOMAIN 82..143
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 149..246
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 268..521
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 15..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 274..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 12
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 417
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 528
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"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3CQT"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2L2P"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:3CQT"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:3CQT"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:3CQT"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:3CQT"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3CQT"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3CQT"
SQ SEQUENCE 534 AA; 60265 MW; 00A170357C5374F9 CRC64;
MGCVQCKDKE ATKLTDERDG SLTQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHATGGQG
LTVFGGVNSS SHTGTLRTRG GTGVTLFEAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW
EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET
TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSEKADGLCF
NLTVIATNNT PQTVGLAKDA WEVARDSLFL EQKLGQGCFA EVWRGTWNGN TKVAIKTLKP
GTMSPESFLE EAQIMKKLKH DKLVQLYAVV SRRPIYIVTE YMSKGSLLIF LKDGEGRALK
LPNLVDMAAQ VAAGMAYIER MNYIHRDLRS ANILVGNGLI CKIADFGLAR LIEDNEYTAR
QGAKFPIKWT APEAALYGRF TIKSDVWSFG ILLTELVTKG RVPYPGMNNR EVLEQVERGY
RMPCPQDCPI SLHELMIHCW KKDPEERPTF EYLQGFLEDY FTATEPQYQP GDNL
