ID   FYNB_DANRE              Reviewed;         544 AA.
AC   F1RDG9; Q4KMJ8;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Tyrosine-protein kinase fynb;
DE            EC=2.7.10.2;
DE   AltName: Full=Proto-oncogene c-Fynb;
GN   Name=fynb;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {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; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by phosphorylation of Tyr-538 by
CC       leukocyte common antigen and activated by dephosphorylation of this
CC       site. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AL954744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FP015917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC098534; AAH98534.1; -; mRNA.
DR   RefSeq; NP_001025140.1; NM_001029969.1.
DR   RefSeq; XP_005160359.1; XM_005160302.3.
DR   AlphaFoldDB; F1RDG9; -.
DR   SMR; F1RDG9; -.
DR   STRING; 7955.ENSDARP00000037198; -.
DR   PaxDb; 7955-ENSDARP00000037198; -.
DR   GeneID; 574422; -.
DR   KEGG; dre:574422; -.
DR   AGR; ZFIN:ZDB-GENE-050706-89; -.
DR   CTD; 574422; -.
DR   ZFIN; ZDB-GENE-050706-89; fynb.
DR   eggNOG; KOG0197; Eukaryota.
DR   InParanoid; F1RDG9; -.
DR   OMA; MIMNINC; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; F1RDG9; -.
DR   TreeFam; TF351634; -.
DR   Reactome; R-DRE-1227986; Signaling by ERBB2.
DR   Reactome; R-DRE-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-DRE-1433557; Signaling by SCF-KIT.
DR   Reactome; R-DRE-1433559; Regulation of KIT signaling.
DR   Reactome; R-DRE-210990; PECAM1 interactions.
DR   Reactome; R-DRE-2424491; DAP12 signaling.
DR   Reactome; R-DRE-373753; Nephrin family interactions.
DR   Reactome; R-DRE-375165; NCAM signaling for neurite out-growth.
DR   Reactome; R-DRE-389356; CD28 co-stimulation.
DR   Reactome; R-DRE-389357; CD28 dependent PI3K/Akt signaling.
DR   Reactome; R-DRE-389359; CD28 dependent Vav1 pathway.
DR   Reactome; R-DRE-389513; CTLA4 inhibitory signaling.
DR   Reactome; R-DRE-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-DRE-3928663; EPHA-mediated growth cone collapse.
DR   Reactome; R-DRE-3928664; Ephrin signaling.
DR   Reactome; R-DRE-3928665; EPH-ephrin mediated repulsion of cells.
DR   Reactome; R-DRE-399954; Sema3A PAK dependent Axon repulsion.
DR   Reactome; R-DRE-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR   Reactome; R-DRE-399956; CRMPs in Sema3A signaling.
DR   Reactome; R-DRE-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-DRE-5621480; Dectin-2 family.
DR   Reactome; R-DRE-5621575; CD209 (DC-SIGN) signaling.
DR   Reactome; R-DRE-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-DRE-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-DRE-8866376; Reelin signalling pathway.
DR   Reactome; R-DRE-9032759; NTRK2 activates RAC1.
DR   Reactome; R-DRE-912631; Regulation of signaling by CBL.
DR   PRO; PR:F1RDG9; -.
DR   Proteomes; UP000000437; Chromosome 20.
DR   Bgee; ENSDARG00000025319; Expressed in retina and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
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:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0060027; P:convergent extension involved in gastrulation; IGI:ZFIN.
DR   GO; GO:0031101; P:fin regeneration; IMP:ZFIN.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; Cytoplasm; 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..544
FT                   /note="Tyrosine-protein kinase fynb"
FT                   /id="PRO_0000418879"
FT   DOMAIN          89..150
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          156..253
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          278..531
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        397
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         284..292
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         306
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         427
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         538
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        65
FT                   /note="S -> P (in Ref. 2; AAH98534)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   544 AA;  61030 MW;  287C2FCF09C51B15 CRC64;
     MGCVQCKDKE AAKLTDDRDT SLSQSGVGYR YGVDPTPQHY PAFSGTGTAV AAIPNYNNFH
     GAAVSQGMTV FGGISTSTHQ GTLRTRGGTG VTLFVALYDY EARTEDDLSF RKGEKFQIIN
     STEGDWWDAR SLTTGGTGYI PSNYVAPVDS IQAEDWYFGK LGRKDAERQL LSTGNPRGTF
     LIRESETTKG AFSLSIRDWD DVKGDHVKHY KIRKLDSGGY YITTRAQFET LQQLVQHYTE
     RAAGLCCRLV VPCHKGMPRL TDLSVKTKDV WEIPRESLQL IKRLGNGQFG EVWMGTWNGN
     TKVAIKTLKP GTMSPESFLE EAQIMKKLRH DKLVQLYAVV SEEPIYIVTE YMGKGSLLDF
     LKDGEGRALK LPNLVDMAAQ VAGGMAYIER MNYIHRDLRS ANILVGDSLV CKIADFGLAR
     LIEDNEYTAR QGAKFPIKWT APEAALYGKF TIKSDVWSFG ILLTELVTKG RVPYPGMNNR
     EVLEQVERGY RMQCPQDCPS SLHELMVQCW KKDAEERPTF EYLQAFLEDY FTATEPQYQP
     GDNL
//