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 16-JUN-2009, entry version 81. DE RecName: Full=Proto-oncogene tyrosine-protein kinase Fyn; DE EC=2.7.10.2; DE AltName: Full=p59-Fyn; GN Name=FYN; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; OC Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=White leghorn; TISSUE=Muscle; RX MEDLINE=93205395; 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 RT neural 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 RT with src-family protein tyrosine kinase Fyn."; RL Mol. Cell. Neurosci. 6:263-279(1995). CC -!- FUNCTION: Implicated in the control of cell growth. Plays a role CC in the regulation of intracellular calcium levels. Required in CC brain development and mature brain function with important roles CC in the regulation of axon growth, axon guidance, and neurite CC extension. Role in CNTN1-mediated signaling. CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a CC [protein]-L-tyrosine phosphate. CC -!- COFACTOR: Manganese. CC -!- ENZYME REGULATION: Inhibited by phosphorylation of Tyr-528 by CC leukocyte common antigen and activated by dephosphorylation of CC this site (By similarity). CC -!- SUBUNIT: Associates through its SH3 domain, to the p85 subunit of CC phosphatidylinositol 3-kinase. CC -!- TISSUE SPECIFICITY: Thymus and spleen. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. SRC subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC -!- SIMILARITY: Contains 1 SH2 domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X52841; CAA37025.1; -; mRNA. DR IPI; IPI00591143; -. DR PIR; S33568; S33568. DR RefSeq; NP_990680.1; -. DR UniGene; Gga.41929; -. DR PDB; 3CQT; X-ray; 1.60 A; A=85-142. DR PDBsum; 3CQT; -. DR SMR; Q05876; 85-534. DR DIP; DIP:738N; -. DR PRIDE; Q05876; -. DR Ensembl; ENSGALG00000015022; Gallus gallus. DR GeneID; 396294; -. DR KEGG; gga:396294; -. DR HOGENOM; Q05876; -. DR HOVERGEN; Q05876; -. DR BRENDA; 2.7.10.2; 4. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kina...; IEA:EC. DR GO; GO:0015631; F:tubulin binding; ISS:AgBase. DR GO; GO:0030900; P:forebrain development; ISS:AgBase. 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 InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR000980; SH2. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Gene3D; G3DSA:3.30.505.10; SH2; 1. DR Pfam; PF07714; Pkinase_Tyr; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR ProDom; PD000093; SH2; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 1. DR SMART; SM00219; TyrKc; 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; SH2 domain; SH3 domain; Transferase; KW Tyrosine-protein kinase. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 534 Proto-oncogene tyrosine-protein kinase FT Fyn. FT /FTId=PRO_0000088098. FT DOMAIN 82 143 SH3. FT DOMAIN 149 246 SH2. FT DOMAIN 268 521 Protein kinase. FT NP_BIND 274 282 ATP (By similarity). FT ACT_SITE 387 387 Proton acceptor (By similarity). FT BINDING 296 296 ATP (By similarity). FT MOD_RES 12 12 Phosphothreonine; by PKC (By similarity). FT MOD_RES 417 417 Phosphotyrosine; by autocatalysis (By FT similarity). FT MOD_RES 528 528 Phosphotyrosine (By similarity). FT LIPID 2 2 N-myristoyl glycine (By similarity). FT LIPID 3 3 S-palmitoyl cysteine (By similarity). FT LIPID 6 6 S-palmitoyl cysteine (By similarity). 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 //