FYN_XENLA
ID FYN_XENLA Reviewed; 537 AA.
AC P13406; Q7ZYK3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 145.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2179818;
RA Steele R.E., Deng J.C., Ghosn C.R., Fero J.B.;
RT "Structure and expression of fyn genes in Xenopus laevis.";
RL Oncogene 5:369-376(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=11422288; DOI=10.1046/j.1440-169x.2001.00568.x;
RA Saito R., Fujita N., Nagata S.;
RT "Overexpression of Fyn tyrosine kinase causes abnormal development of
RT primary sensory neurons in Xenopus laevis embryos.";
RL Dev. Growth Differ. 43:229-238(2001).
RN [4]
RP FUNCTION.
RX PubMed=15557120; DOI=10.1083/jcb.200405053;
RA Meriane M., Tcherkezian J., Webber C.A., Danek E.I., Triki I.,
RA McFarlane S., Bloch-Gallego E., Lamarche-Vane N.;
RT "Phosphorylation of DCC by Fyn mediates Netrin-1 signaling in growth cone
RT guidance.";
RL J. Cell Biol. 167:687-698(2004).
CC -!- FUNCTION: Tyrosine-protein kinase implicated in the control of cell
CC growth. Plays a role in the regulation of intracellular calcium levels
CC (By similarity). Required in brain development and mature brain
CC function with important roles in the regulation of axon growth, axon
CC guidance, and neurite extension. Blocks axon outgrowth and attraction
CC induced by ntn1 by phosphorylating its receptor ddc. {ECO:0000250,
CC ECO:0000269|PubMed:15557120}.
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.
CC -!- SUBUNIT: Associates through its SH3 domain, to the p85 subunit of
CC phosphatidylinositol 3-kinase.
CC -!- DEVELOPMENTAL STAGE: Expressed in early tail-bud embryos at stage 20 in
CC the brain region of the neural tube and at lower levels throughout the
CC remaining length of the neural tube. Present at stage 32 in the
CC forebrain, midbrain, the ventral half of the hindbrain and the spinal
CC cord. {ECO:0000269|PubMed:11422288}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X52188; CAA36435.1; -; Genomic_DNA.
DR EMBL; M27502; AAA49719.1; -; mRNA.
DR EMBL; BC043749; AAH43749.1; -; mRNA.
DR PIR; A43806; A43806.
DR RefSeq; NP_001079077.1; NM_001085608.2.
DR RefSeq; NP_001080120.1; NM_001086651.1.
DR AlphaFoldDB; P13406; -.
DR BMRB; P13406; -.
DR SMR; P13406; -.
DR DNASU; 379812; -.
DR GeneID; 373609; -.
DR GeneID; 379812; -.
DR KEGG; xla:373609; -.
DR KEGG; xla:379812; -.
DR CTD; 373609; -.
DR CTD; 379812; -.
DR Xenbase; XB-GENE-6252893; fyn.L.
DR Xenbase; XB-GENE-6053528; fyn.S.
DR OrthoDB; 539311at2759; -.
DR BRENDA; 2.7.10.2; 6725.
DR Proteomes; UP000186698; Chromosome 5L.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 373609; Expressed in internal ear and 19 other tissues.
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; Reference proteome; 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_0000088101"
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"
FT CONFLICT 102
FT /note="S -> N (in Ref. 2; AAH43749)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="T -> A (in Ref. 2; AAH43749)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="R -> A (in Ref. 2; AAH43749)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="I -> N (in Ref. 2; AAH43749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 60846 MW; 771E5799682A1326 CRC64;
MGCVQCKDKE ATKLTDERDN SLTQSLGYRY GTDPTPQHYP SFTVTTIPNY NNFHATAGQG
LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFQKGEKFQ ILNSSEGDWW
EARSLTTGGT GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTYLIRESET
TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC
RLVVPCHKGM PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT
LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMSKGSL LDFLKDGEGR
ALKLPNLVDM AAQVARGMAY IERMNYIHRD LRSANILVGN GLICKIADFG LARLIEDNEY
TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE
RGYRMPCPQD CPISLHELML NCWKKDPEER PTFEYLQGFL EDYFTATEPQ YQPGDNL
