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
//
