ID FYNA_DANRE Reviewed; 537 AA. AC Q6EWH2; F8W4M2; Q58HR4; Q6DI27; Q9I8J8; DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2012, sequence version 2. DT 27-MAR-2024, entry version 147. DE RecName: Full=Tyrosine-protein kinase fyna; DE EC=2.7.10.2; DE AltName: Full=Proto-oncogene c-Fyna; GN Name=fyna; Synonyms=fyn; 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 [MRNA] (ISOFORM 1), FUNCTION, AND MUTAGENESIS OF RP LYS-299. RC TISSUE=Embryo; RX PubMed=16112104; DOI=10.1016/j.ydbio.2005.07.018; RA Sharma D., Holets L., Zhang X., Kinsey W.H.; RT "Role of Fyn kinase in signaling associated with epiboly during zebrafish RT development."; RL Dev. Biol. 285:462-476(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=15815683; DOI=10.1038/sj.embor.7400386; RA Jopling C., den Hertog J.; RT "Fyn/Yes and non-canonical Wnt signalling converge on RhoA in vertebrate RT gastrulation cell movements."; RL EMBO Rep. 6:426-431(2005). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Embryo; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-153, SUBCELLULAR LOCATION, ACTIVITY RP REGULATION, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX PubMed=10993948; RX DOI=10.1002/1097-0185(20001001)260:2<115::aid-ar10>3.0.co;2-c; RA Rongish B.J., Kinsey W.H.; RT "Transient nuclear localization of Fyn kinase during development in RT zebrafish."; RL Anat. Rec. 260:115-123(2000). 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). Required CC for convergent extension cell movements during gastrulation, acting CC with yes via rhoa. May be required for epiboly to occur, possibly CC through its effects in calcium signaling. {ECO:0000250, CC ECO:0000269|PubMed:15815683, ECO:0000269|PubMed:16112104}. 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 (By similarity). Relatively inactive in the unfertilized oocyte, CC undergoes rapid activation immediately following fertilization. Total CC activity increases progressively during later development and remains CC elevated during sphere and epiboly stage. {ECO:0000250, CC ECO:0000269|PubMed:10993948}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10993948}. Nucleus CC {ECO:0000269|PubMed:10993948}. Note=Transiently expressed in the CC nucleus at mid-blastula stage (3.3 hpf) in a large subset of cells. CC Nuclear localization is not observed from late blastula stage onward. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6EWH2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6EWH2-2; Sequence=VSP_044087, VSP_044088; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10993948, CC ECO:0000269|PubMed:15815683}. CC -!- DEVELOPMENTAL STAGE: Expressed in the pre-gastrula embryo (at protein CC level). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=AAX47959.1; Type=Frameshift; Evidence={ECO:0000305}; 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; AY948197; AAX47959.1; ALT_FRAME; mRNA. DR EMBL; AJ620748; CAF06179.1; -; mRNA. DR EMBL; CU306817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC075763; AAH75763.1; -; mRNA. DR EMBL; AF269145; AAF81748.1; -; mRNA. DR RefSeq; NP_001315092.1; NM_001328163.1. [Q6EWH2-1] DR AlphaFoldDB; Q6EWH2; -. DR SMR; Q6EWH2; -. DR STRING; 7955.ENSDARP00000123888; -. DR PaxDb; 7955-ENSDARP00000123888; -. DR GeneID; 373872; -. DR KEGG; dre:373872; -. DR AGR; ZFIN:ZDB-GENE-030903-5; -. DR CTD; 373872; -. DR ZFIN; ZDB-GENE-030903-5; fyna. DR eggNOG; KOG0197; Eukaryota. DR HOGENOM; CLU_000288_7_2_1; -. DR InParanoid; Q6EWH2; -. DR OMA; XWYFGKL; -. DR OrthoDB; 1614410at2759; -. DR PhylomeDB; Q6EWH2; -. DR TreeFam; TF351634; -. DR PRO; PR:Q6EWH2; -. DR Proteomes; UP000000437; Chromosome 17. DR Bgee; ENSDARG00000011370; Expressed in mature ovarian follicle and 25 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IDA:ZFIN. DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IDA:ZFIN. 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:0004672; F:protein kinase activity; IDA:ZFIN. DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central. DR GO; GO:0034334; P:adherens junction maintenance; IGI:ZFIN. 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:0001702; P:gastrulation with mouth forming second; IMP:ZFIN. DR GO; GO:0045087; P:innate immune response; IBA:GO_Central. DR GO; GO:0042552; P:myelination; IMP:ZFIN. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:ZFIN. 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; cd05070; PTKc_Fyn; 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:SF432; TYROSINE-PROTEIN KINASE FYNA; 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 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cytoplasm; Developmental protein; KW Kinase; Lipoprotein; Manganese; Metal-binding; Myristate; KW Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Proto-oncogene; KW 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 fyna" FT /id="PRO_0000418878" 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 REGION 13..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 VAR_SEQ 293 FT /note="N -> H (in isoform 2)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_044087" FT VAR_SEQ 294..537 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_044088" FT MUTAGEN 299 FT /note="K->M: Loss of activity." FT /evidence="ECO:0000269|PubMed:16112104" FT CONFLICT 5 FT /note="Q -> R (in Ref. 4; AAH75763)" FT /evidence="ECO:0000305" FT CONFLICT 60..62 FT /note="GVT -> RVP (in Ref. 2; CAF06179)" FT /evidence="ECO:0000305" FT CONFLICT 148 FT /note="D -> E (in Ref. 1; AAX47959)" FT /evidence="ECO:0000305" SQ SEQUENCE 537 AA; 60569 MW; 1C7CB34990049B96 CRC64; MGCVQCKDKE ATKLTDERET SVSQHAGYRY GSDPTPQHYP SFGVTAIPNY NNFHAPVSQG VTVFGGVNSS SHSGTLRSRG GTGVTLFVAL YDYEARSEDD LSFRKGEKFQ ILNSTEGDWW EARSLTTGGT GYIPSNYVAP VDSIQAEDWY FGKLGRKDAE RQLLSNGNPR GTFLIRESET TKGAYSLSIQ DWDETKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVHH YSARAAGLCC RLIVPCHKGM PRLADLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAVKT LKPGTMSPES FLEEAQIMKK LRHDKLVQLY AVVSEEPIYI VTEYMSKGSL LDFLKDGEGR GLKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGD SLVCKIADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE RGYRMPCPQD CPSSLHELML QCWKRDPEER PTFEYLQAFL EDYFTATEPQ YQPGDNL //