ID   FYN_XIPHE               Reviewed;         537 AA.
AC   P27446;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-NOV-2023, entry version 128.
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   Xiphophorus hellerii (Green swordtail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Rio Lancetilla;
RX   PubMed=1707152;
RA   Hannig G., Ottilie S., Schartl M.;
RT   "Conservation of structure and expression of the c-yes and fyn genes in
RT   lower vertebrates.";
RL   Oncogene 6:361-369(1991).
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 (By similarity). {ECO:0000250}.
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-531 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   -!- 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; X54971; CAA38715.1; -; mRNA.
DR   PIR; I51592; I51592.
DR   AlphaFoldDB; P27446; -.
DR   SMR; P27446; -.
DR   BRENDA; 2.7.10.2; 6732.
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; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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:SF44; TYROSINE-PROTEIN KINASE FYN; 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; Developmental protein; Kinase; Lipoprotein; Manganese;
KW   Metal-binding; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein;
KW   Proto-oncogene; SH2 domain; SH3 domain; Transferase;
KW   Tyrosine-protein kinase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..537
FT                   /note="Tyrosine-protein kinase Fyn"
FT                   /id="PRO_0000088102"
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          271..524
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        390
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         277..285
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         299
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         420
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         531
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   537 AA;  60447 MW;  6AC5486B13C3876B CRC64;
     MGCVQCKDKE ATKLTDDRDA SISQGAGYRY GADPTPQHYP SFGVTAIPNY NNFHAPVGQG
     VTVFGGVNTS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFRKGERFQ ILNSTEGDWW
     DARSLTTGGS GYIPSNYVAP VDSIQAEDWY FGKLGRKDAE RQLLSTGNPR GTYLIRESET
     TKGAFSLSIR DWDDEKGDHV KHYKIRKLDS GGYYITTRAQ FDTLQQLVQH YSDRAAGLCC
     RLVVPCHKGM PRLADLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGTTKVAVKT
     LKPGTMSPES FLEEAQIMKK LRHDKLVQLY AVVSEEPIYI VTEYMSKGSL LDFLKDGEGR
     ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGD NLVCKIADFG LARLIEDNEY
     TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE
     RGYRMPCPQD CPASLHELML QCWKKDPEER PTFEYLQAFL EDYFTATEPQ YQPGDNL
//