FYN_XIPHE
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 03-AUG-2022, entry version 124.
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 helleri (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 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 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
