FYN_MOUSE
ID FYN_MOUSE Reviewed; 537 AA.
AC P39688; Q3TAT3; Q3U0T5; Q8K2A3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 4.
DT 03-AUG-2022, entry version 219.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=2488273;
RA Cooke M.P., Perlmutter R.M.;
RT "Expression of a novel form of the fyn proto-oncogene in hematopoietic
RT cells.";
RL New Biol. 1:66-74(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=T-cell;
RX PubMed=9895129;
RA Lee C., Kim M.G., Jeon S.H., Park D.E., Park S.D., Seong R.H.;
RT "Two species of mRNAs for the fyn proto-oncogene are produced by an
RT alternative polyadenylation.";
RL Mol. Cells 8:746-749(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=1361685; DOI=10.1126/science.1361685;
RA Grant S.G., O'Dell T.J., Karl K.A., Stein P.L., Soriano P., Kandel E.R.;
RT "Impaired long-term potentiation, spatial learning, and hippocampal
RT development in fyn mutant mice.";
RL Science 258:1903-1910(1992).
RN [6]
RP INTERACTION WITH CSF1R.
RX PubMed=7681396; DOI=10.1002/j.1460-2075.1993.tb05735.x;
RA Courtneidge S.A., Dhand R., Pilat D., Twamley G.M., Waterfield M.D.,
RA Roussel M.F.;
RT "Activation of Src family kinases by colony stimulating factor-1, and their
RT association with its receptor.";
RL EMBO J. 12:943-950(1993).
RN [7]
RP PHOSPHORYLATION AT TYR-420 AND TYR-531, AND ACTIVITY REGULATION.
RX PubMed=8441403; DOI=10.1128/mcb.13.3.1651-1656.1993;
RA Hurley T.R., Hyman R., Sefton B.M.;
RT "Differential effects of expression of the CD45 tyrosine protein
RT phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src
RT tyrosine protein kinases.";
RL Mol. Cell. Biol. 13:1651-1656(1993).
RN [8]
RP PALMITOYLATION AT CYS-3 AND CYS-6, AND MUTAGENESIS OF CYS-3 AND CYS-6.
RX PubMed=8413237; DOI=10.1128/mcb.13.10.6385-6392.1993;
RA Shenoy-Scaria A.M., Timson L.K., Kwong J., Shaw A.S., Lublin D.M.;
RT "Palmitylation of an amino-terminal cysteine motif of protein tyrosine
RT kinases p56lck and p59fyn mediates interaction with glycosyl-
RT phosphatidylinositol-anchored proteins.";
RL Mol. Cell. Biol. 13:6385-6392(1993).
RN [9]
RP PALMITOYLATION AT CYS-3 AND CYS-6, AND MUTAGENESIS OF GLY-2; CYS-3 AND
RP CYS-6.
RX PubMed=7980442; DOI=10.1042/bj3030749;
RA Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I.;
RT "Palmitoylation of multiple Src-family kinases at a homologous N-terminal
RT motif.";
RL Biochem. J. 303:749-753(1994).
RN [10]
RP INTERACTION WITH CD79A.
RX PubMed=8168489; DOI=10.1002/j.1460-2075.1994.tb06460.x;
RA Clark M.R., Johnson S.A., Cambier J.C.;
RT "Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels of
RT binding specificity and tyrosine phosphorylated Ig-alpha stimulation of Fyn
RT activity.";
RL EMBO J. 13:1911-1919(1994).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8007959; DOI=10.1128/mcb.14.7.4554-4564.1994;
RA Davidson D., Viallet J., Veillette A.;
RT "Unique catalytic properties dictate the enhanced function of p59fynT, the
RT hemopoietic cell-specific isoform of the Fyn tyrosine protein kinase, in T
RT cells.";
RL Mol. Cell. Biol. 14:4554-4564(1994).
RN [12]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=8655574; DOI=10.1083/jcb.133.5.1007;
RA Gauen L.K.T., Linder M.E., Shaw A.S.;
RT "Multiple features of the p59fyn src homology 4 domain define a motif for
RT immune-receptor tyrosine-based activation motif (ITAM) binding and for
RT plasma membrane localization.";
RL J. Cell Biol. 133:1007-1015(1996).
RN [13]
RP INTERACTION WITH CSF1R.
RX PubMed=9312046; DOI=10.1093/emboj/16.19.5880;
RA Bourette R.P., Myles G.M., Choi J.L., Rohrschneider L.R.;
RT "Sequential activation of phoshatidylinositol 3-kinase and phospholipase C-
RT gamma2 by the M-CSF receptor is necessary for differentiation signaling.";
RL EMBO J. 16:5880-5893(1997).
RN [14]
RP PALMITOYLATION AT CYS-3, AND MUTAGENESIS OF CYS-3.
RX PubMed=9201723; DOI=10.1091/mbc.8.6.1159;
RA Wolven A., Okamura H., Rosenblatt Y., Resh M.D.;
RT "Palmitoylation of p59fyn is reversible and sufficient for plasma membrane
RT association.";
RL Mol. Biol. Cell 8:1159-1173(1997).
RN [15]
RP INTERACTION WITH TOM1L1.
RX PubMed=11711534; DOI=10.1074/jbc.m106813200;
RA Seykora J.T., Mei L., Dotto G.P., Stein P.L.;
RT "'Srcasm: a novel Src activating and signaling molecule.";
RL J. Biol. Chem. 277:2812-2822(2002).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12218089; DOI=10.4049/jimmunol.169.6.2813;
RA Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T., Minaki Y.,
RA Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.;
RT "Fyn is essential for tyrosine phosphorylation of Csk-binding
RT protein/phosphoprotein associated with glycolipid-enriched microdomains in
RT lipid rafts in resting T cells.";
RL J. Immunol. 169:2813-2817(2002).
RN [17]
RP FUNCTION IN PHOSPHORYLATING CLNK, AND INTERACTION WITH SKAP1 AND FYB1.
RX PubMed=12681493; DOI=10.1016/s0014-5793(03)00234-5;
RA Fujii Y., Wakahara S., Nakao T., Hara T., Ohtake H., Komurasaki T.,
RA Kitamura K., Tatsuno A., Fujiwara N., Hozumi N., Ra C., Kitamura D.,
RA Goitsuka R.;
RT "Targeting of MIST to Src-family kinases via SKAP55-SLAP-130 adaptor
RT complex in mast cells(1).";
RL FEBS Lett. 540:111-116(2003).
RN [18]
RP FUNCTION IN PHOSPHORYLATION OF CTNNB1.
RX PubMed=12640114; DOI=10.1128/mcb.23.7.2287-2297.2003;
RA Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N.,
RA Garcia de Herreros A., Dunach M.;
RT "p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin
RT Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction.";
RL Mol. Cell. Biol. 23:2287-2297(2003).
RN [19]
RP SUBCELLULAR LOCATION.
RX PubMed=14645715; DOI=10.1073/pnas.2432139100;
RA Shima T., Nada S., Okada M.;
RT "Transmembrane phosphoprotein Cbp senses cell adhesion signaling mediated
RT by Src family kinase in lipid rafts.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:14897-14902(2003).
RN [20]
RP FUNCTION IN PHOSPHORYLATION OF MAPT.
RX PubMed=14999081; DOI=10.1523/jneurosci.4162-03.2004;
RA Lee G., Thangavel R., Sharma V.M., Litersky J.M., Bhaskar K., Fang S.M.,
RA Do L.H., Andreadis A., Van Hoesen G., Ksiezak-Reding H.;
RT "Phosphorylation of tau by fyn: implications for Alzheimer's disease.";
RL J. Neurosci. 24:2304-2312(2004).
RN [21]
RP REVIEW ON ROLE IN KIT SIGNALING.
RX PubMed=16129412; DOI=10.1016/j.bbrc.2005.08.055;
RA Roskoski R. Jr.;
RT "Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor.";
RL Biochem. Biophys. Res. Commun. 337:1-13(2005).
RN [22]
RP INTERACTION WITH KDR.
RX PubMed=16966330; DOI=10.1074/jbc.m603928200;
RA Lamalice L., Houle F., Huot J.;
RT "Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck
RT and activation of Fyn leading to SAPK2/p38 activation and endothelial cell
RT migration in response to VEGF.";
RL J. Biol. Chem. 281:34009-34020(2006).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185 AND TYR-531, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [25]
RP PALMITOYLATION BY ZDHHC21.
RX PubMed=19956733; DOI=10.1371/journal.pgen.1000748;
RA Mill P., Lee A.W., Fukata Y., Tsutsumi R., Fukata M., Keighren M.,
RA Porter R.M., McKie L., Smyth I., Jackson I.J.;
RT "Palmitoylation regulates epidermal homeostasis and hair follicle
RT differentiation.";
RL PLoS Genet. 5:e1000748-e1000748(2009).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [27]
RP INTERACTION WITH PTPRH; PTPRO AND PTPRB.
RX PubMed=20398064; DOI=10.1111/j.1365-2443.2010.01398.x;
RA Murata Y., Mori M., Kotani T., Supriatna Y., Okazawa H., Kusakari S.,
RA Saito Y., Ohnishi H., Matozaki T.;
RT "Tyrosine phosphorylation of R3 subtype receptor-type protein tyrosine
RT phosphatases and their complex formations with Grb2 or Fyn.";
RL Genes Cells 15:513-524(2010).
RN [28]
RP DISRUPTION PHENOTYPE.
RX PubMed=21872217; DOI=10.1016/j.brainres.2011.07.059;
RA Babus L.W., Little E.M., Keenoy K.E., Minami S.S., Chen E., Song J.M.,
RA Caviness J., Koo S.Y., Pak D.T., Rebeck G.W., Turner R.S., Hoe H.S.;
RT "Decreased dendritic spine density and abnormal spine morphology in Fyn
RT knockout mice.";
RL Brain Res. 1415:96-102(2011).
RN [29]
RP INTERACTION WITH DSCAM, AND PHOSPHORYLATION.
RX PubMed=22685302; DOI=10.1074/jbc.m112.340174;
RA Purohit A.A., Li W., Qu C., Dwyer T., Shao Q., Guan K.L., Liu G.;
RT "Down syndrome cell adhesion molecule (DSCAM) associates with
RT uncoordinated-5C (UNC5C) in netrin-1-mediated growth cone collapse.";
RL J. Biol. Chem. 287:27126-27138(2012).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 81-239.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of a SH3 and SH2 domains of fyn protein (proto-concogene
RT tyrosine-protein kinase fyn) from Mus musculus at 1.98 a resolution.";
RL Submitted (DEC-2011) to the PDB data bank.
CC -!- FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in
CC many biological processes including regulation of cell growth and
CC survival, cell adhesion, integrin-mediated signaling, cytoskeletal
CC remodeling, cell motility, immune response and axon guidance. Inactive
CC FYN is phosphorylated on its C-terminal tail within the catalytic
CC domain. Following activation by PKA, the protein subsequently
CC associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation,
CC activation and targeting to focal adhesions. Involved in the regulation
CC of cell adhesion and motility through phosphorylation of CTNNB1 (beta-
CC catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling
CC by phosphorylating several proteins including the actin regulator WAS
CC and the microtubule-associated proteins MAP2 and MAPT. Promotes cell
CC survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic
CC cleavage. Participates in signal transduction pathways that regulate
CC the integrity of the glomerular slit diaphragm (an essential part of
CC the glomerular filter of the kidney) by phosphorylating several slit
CC diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role
CC in neural processes by phosphorylating DPYSL2, a multifunctional
CC adapter protein within the central nervous system, ARHGAP32, a
CC regulator for Rho family GTPases implicated in various neural
CC functions, and SNCA, a small pre-synaptic protein. Participates in the
CC downstream signaling pathways that lead to T-cell differentiation and
CC proliferation following T-cell receptor (TCR) stimulation.
CC Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation.
CC Also participates in negative feedback regulation of TCR signaling
CC through phosphorylation of PAG1, thereby promoting interaction between
CC PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK
CC and FYN in an inactive form. Promotes CD28-induced phosphorylation of
CC VAV1. In mast cells, phosphorylates CLNK after activation of
CC immunoglobulin epsilon receptor signaling (PubMed:12681493).
CC {ECO:0000250|UniProtKB:P06241, ECO:0000269|PubMed:12218089,
CC ECO:0000269|PubMed:12640114, ECO:0000269|PubMed:12681493,
CC ECO:0000269|PubMed:14999081, ECO:0000269|PubMed:8007959}.
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:0000269|PubMed:8441403}.
CC -!- SUBUNIT: Interacts (via its SH3 domain) with PIK3R1 and PRMT8 (By
CC similarity). Interacts with FYB1, PAG1, and SH2D1A (By similarity).
CC Interacts with CD79A (tyrosine-phosphorylated form); the interaction
CC increases FYN activity (PubMed:8168489). Interacts with TOM1L1
CC (phosphorylated form) (PubMed:11711534). Interacts with SH2D1A and
CC SLAMF1 (By similarity). Interacts with and phosphorylates ITCH, down-
CC regulating its activity (By similarity). Interacts with FASLG (By
CC similarity). Interacts with RUNX3 (By similarity). Interacts with KIT
CC (By similarity). Interacts with EPHA8; possible downstream effector of
CC EPHA8 in regulation of cell adhesion (By similarity). Interacts with
CC PTK2/FAK1; this interaction leads to PTK2/FAK1 phosphorylation and
CC activation (By similarity). Interacts with CAV1; this interaction
CC couples integrins to the Ras-ERK pathway (By similarity). Interacts
CC (via SH3 domain) with KLHL2 (via N-terminus) (By similarity). Interacts
CC with KDR (tyrosine phosphorylated) (PubMed:16966330). Interacts (via
CC SH2 domain) with CSF1R (tyrosine phosphorylated) (PubMed:7681396,
CC PubMed:9312046). Interacts with UNC119 (By similarity). Interacts (via
CC SH2 domain) with PTPRH (phosphorylated form) (PubMed:20398064).
CC Interacts with PTPRO (phosphorylated form) (PubMed:20398064). Interacts
CC with PTPRB (phosphorylated form) (PubMed:20398064). Interacts with FYB2
CC (By similarity). Interacts with DSCAM (PubMed:22685302). Interacts with
CC SKAP1 and FYB1; this interaction promotes the phosphorylation of CLNK
CC (PubMed:12681493). {ECO:0000250|UniProtKB:P06241,
CC ECO:0000250|UniProtKB:Q62844, ECO:0000269|PubMed:11711534,
CC ECO:0000269|PubMed:12681493, ECO:0000269|PubMed:16966330,
CC ECO:0000269|PubMed:20398064, ECO:0000269|PubMed:22685302,
CC ECO:0000269|PubMed:7681396, ECO:0000269|PubMed:8168489,
CC ECO:0000269|PubMed:9312046}.
CC -!- INTERACTION:
CC P39688; P22682: Cbl; NbExp=5; IntAct=EBI-524514, EBI-640919;
CC P39688; P51807: Dynlt1; NbExp=3; IntAct=EBI-524514, EBI-642797;
CC P39688; Q60749: Khdrbs1; NbExp=15; IntAct=EBI-524514, EBI-519077;
CC P39688; Q9WU01: Khdrbs2; NbExp=2; IntAct=EBI-524514, EBI-8339046;
CC P39688; P05622: Pdgfrb; NbExp=3; IntAct=EBI-524514, EBI-1554855;
CC P39688; Q9QUM4: Slamf1; NbExp=4; IntAct=EBI-524514, EBI-7910086;
CC P39688; Q9JIA7: Sphk2; NbExp=2; IntAct=EBI-524514, EBI-985434;
CC P39688; P22681: CBL; Xeno; NbExp=3; IntAct=EBI-524514, EBI-518228;
CC P39688; Q14332: FZD2; Xeno; NbExp=4; IntAct=EBI-524514, EBI-6254477;
CC P39688; P35570: Irs1; Xeno; NbExp=4; IntAct=EBI-524514, EBI-520230;
CC P39688; O75051: PLXNA2; Xeno; NbExp=3; IntAct=EBI-524514, EBI-308264;
CC P39688; P18433: PTPRA; Xeno; NbExp=2; IntAct=EBI-524514, EBI-2609645;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cell membrane {ECO:0000250}. Note=Present and active in lipid rafts.
CC Palmitoylation is crucial for proper trafficking (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=B;
CC IsoId=P39688-1; Sequence=Displayed;
CC Name=2; Synonyms=T;
CC IsoId=P39688-2; Sequence=VSP_024111, VSP_024112;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in the brain, isoform
CC 2 is expressed in cells of hemopoietic lineages, especially T-
CC lymphocytes. {ECO:0000269|PubMed:1361685, ECO:0000269|PubMed:8007959}.
CC -!- PTM: Autophosphorylated at Tyr-420 (PubMed:8441403). Phosphorylation on
CC the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an
CC inactive state (PubMed:8441403). PTPRC/CD45 dephosphorylates Tyr-531
CC leading to activation. Ultraviolet B (UVB) strongly increase
CC phosphorylation at Thr-15 and kinase activity, and promotes
CC translocation from the cytoplasm to the nucleus. Dephosphorylation at
CC Tyr-420 by PTPN2 negatively regulates T-cell receptor signaling (By
CC similarity). Phosphorylated at tyrosine residues, which can be enhanced
CC by NTN1 (PubMed:22685302). {ECO:0000250|UniProtKB:P06241,
CC ECO:0000269|PubMed:22685302, ECO:0000269|PubMed:8441403}.
CC -!- PTM: Palmitoylated (PubMed:19956733, PubMed:7980442, PubMed:8413237,
CC PubMed:9201723). Palmitoylation at Cys-3 and Cys-6, probably by
CC ZDHHC21, regulates subcellular location (PubMed:7980442,
CC PubMed:8413237, PubMed:9201723, PubMed:19956733).
CC {ECO:0000269|PubMed:19956733, ECO:0000269|PubMed:7980442,
CC ECO:0000269|PubMed:8413237, ECO:0000269|PubMed:9201723}.
CC -!- PTM: Myristoylation is required prior to palmitoylation.
CC {ECO:0000269|PubMed:8655574}.
CC -!- DISRUPTION PHENOTYPE: Mice have various neural defects, including
CC defective long term potentiation, impaired spatial memory,
CC hypomyelination, abnormal dendrite orientation and uncoordinated
CC hippocampal structure. {ECO:0000269|PubMed:1361685,
CC ECO:0000269|PubMed:21872217}.
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; M27266; AAA37644.1; -; mRNA.
DR EMBL; U70324; AAB09568.1; -; mRNA.
DR EMBL; AK156584; BAE33766.1; -; mRNA.
DR EMBL; AK171646; BAE42585.1; -; mRNA.
DR EMBL; BC032149; AAH32149.1; -; mRNA.
DR EMBL; BC092217; AAH92217.1; -; mRNA.
DR CCDS; CCDS23788.1; -. [P39688-2]
DR CCDS; CCDS48538.1; -. [P39688-1]
DR PIR; A44991; A44991.
DR RefSeq; NP_001116364.1; NM_001122892.1. [P39688-2]
DR RefSeq; NP_001116365.1; NM_001122893.1. [P39688-1]
DR RefSeq; NP_032080.2; NM_008054.2. [P39688-2]
DR RefSeq; XP_006512602.1; XM_006512539.3. [P39688-1]
DR RefSeq; XP_006512603.1; XM_006512540.3. [P39688-1]
DR RefSeq; XP_011241419.1; XM_011243117.2. [P39688-1]
DR PDB; 3UF4; X-ray; 1.98 A; A=82-244.
DR PDBsum; 3UF4; -.
DR AlphaFoldDB; P39688; -.
DR BMRB; P39688; -.
DR SMR; P39688; -.
DR BioGRID; 199773; 20.
DR CORUM; P39688; -.
DR DIP; DIP-198N; -.
DR ELM; P39688; -.
DR IntAct; P39688; 42.
DR MINT; P39688; -.
DR STRING; 10090.ENSMUSP00000097547; -.
DR BindingDB; P39688; -.
DR ChEMBL; CHEMBL4517; -.
DR iPTMnet; P39688; -.
DR PhosphoSitePlus; P39688; -.
DR SwissPalm; P39688; -.
DR EPD; P39688; -.
DR jPOST; P39688; -.
DR MaxQB; P39688; -.
DR PaxDb; P39688; -.
DR PeptideAtlas; P39688; -.
DR PRIDE; P39688; -.
DR ProteomicsDB; 266899; -. [P39688-1]
DR ProteomicsDB; 266900; -. [P39688-2]
DR Antibodypedia; 3559; 1038 antibodies from 47 providers.
DR DNASU; 14360; -.
DR Ensembl; ENSMUST00000063091; ENSMUSP00000057707; ENSMUSG00000019843. [P39688-2]
DR Ensembl; ENSMUST00000099967; ENSMUSP00000097547; ENSMUSG00000019843. [P39688-1]
DR Ensembl; ENSMUST00000126486; ENSMUSP00000115233; ENSMUSG00000019843. [P39688-2]
DR Ensembl; ENSMUST00000135242; ENSMUSP00000117111; ENSMUSG00000019843. [P39688-2]
DR Ensembl; ENSMUST00000146287; ENSMUSP00000114188; ENSMUSG00000019843. [P39688-2]
DR GeneID; 14360; -.
DR KEGG; mmu:14360; -.
DR UCSC; uc007evx.2; mouse. [P39688-1]
DR UCSC; uc007evy.2; mouse. [P39688-2]
DR CTD; 2534; -.
DR MGI; MGI:95602; Fyn.
DR VEuPathDB; HostDB:ENSMUSG00000019843; -.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000155462; -.
DR InParanoid; P39688; -.
DR OMA; WMEKADG; -.
DR OrthoDB; 539311at2759; -.
DR PhylomeDB; P39688; -.
DR TreeFam; TF351634; -.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR Reactome; R-MMU-1227986; Signaling by ERBB2.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-1433559; Regulation of KIT signaling.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-2029481; FCGR activation.
DR Reactome; R-MMU-210990; PECAM1 interactions.
DR Reactome; R-MMU-2424491; DAP12 signaling.
DR Reactome; R-MMU-373753; Nephrin family interactions.
DR Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-MMU-389356; CD28 co-stimulation.
DR Reactome; R-MMU-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-MMU-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-MMU-389513; CTLA4 inhibitory signaling.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-MMU-3928664; Ephrin signaling.
DR Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-MMU-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-MMU-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
DR Reactome; R-MMU-418885; DCC mediated attractive signaling.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-5621480; Dectin-2 family.
DR Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-MMU-8866376; Reelin signalling pathway.
DR Reactome; R-MMU-9032759; NTRK2 activates RAC1.
DR Reactome; R-MMU-912631; Regulation of signaling by CBL.
DR BioGRID-ORCS; 14360; 5 hits in 79 CRISPR screens.
DR ChiTaRS; Fyn; mouse.
DR PRO; PR:P39688; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P39688; protein.
DR Bgee; ENSMUSG00000019843; Expressed in cranial nerve II and 288 other tissues.
DR ExpressionAtlas; P39688; baseline and differential.
DR Genevisible; P39688; MM.
DR GO; GO:0005884; C:actin filament; IDA:MGI.
DR GO; GO:0044297; C:cell body; IDA:ARUK-UCL.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IMP:ParkinsonsUK-UCL.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0097386; C:glial cell projection; IDA:ARUK-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:ARUK-UCL.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IMP:ParkinsonsUK-UCL.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:ARUK-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042609; F:CD4 receptor binding; ISO:MGI.
DR GO; GO:0042610; F:CD8 receptor binding; ISO:MGI.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0046875; F:ephrin receptor binding; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:UniProtKB.
DR GO; GO:0070851; F:growth factor receptor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0051428; F:peptide hormone receptor binding; ISO:MGI.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:MGI.
DR GO; GO:0016004; F:phospholipase activator activity; ISO:MGI.
DR GO; GO:0043274; F:phospholipase binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0042608; F:T cell receptor binding; ISO:MGI.
DR GO; GO:0048156; F:tau protein binding; IPI:ARUK-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0015631; F:tubulin binding; IDA:MGI.
DR GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0050798; P:activated T cell proliferation; IMP:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI.
DR GO; GO:1905430; P:cellular response to glycine; ISO:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:1905232; P:cellular response to L-glutamate; ISO:MGI.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IDA:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IGI:MGI.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0003015; P:heart process; IGI:ARUK-UCL.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IGI:MGI.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0042552; P:myelination; TAS:MGI.
DR GO; GO:1902951; P:negative regulation of dendritic spine maintenance; IGI:ARUK-UCL.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:1903202; P:negative regulation of oxidative stress-induced cell death; ISO:MGI.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IGI:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IGI:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; IGI:ARUK-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IGI:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:MGI.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IGI:ARUK-UCL.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:CACAO.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
DR GO; GO:1905664; P:regulation of calcium ion import across plasma membrane; IGI:ARUK-UCL.
DR GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR GO; GO:1900449; P:regulation of glutamate receptor signaling pathway; IGI:ARUK-UCL.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IGI:ARUK-UCL.
DR GO; GO:1904645; P:response to amyloid-beta; IGI:ARUK-UCL.
DR GO; GO:0045471; P:response to ethanol; IGI:MGI.
DR GO; GO:0000304; P:response to singlet oxygen; ISO:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; ATP-binding;
KW Cell membrane; Cytoplasm; Developmental protein; Immunity; Kinase;
KW Lipoprotein; Manganese; Membrane; 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 CHAIN 2..537
FT /note="Tyrosine-protein kinase Fyn"
FT /id="PRO_0000088100"
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 14..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Polar residues"
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 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06241"
FT MOD_RES 185
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 420
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:8441403"
FT MOD_RES 531
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:8441403,
FT ECO:0007744|PubMed:18034455"
FT MOD_RES 531
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:8655574"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:7980442,
FT ECO:0000269|PubMed:8413237, ECO:0000269|PubMed:9201723"
FT LIPID 6
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:7980442,
FT ECO:0000305|PubMed:8413237"
FT VAR_SEQ 234..236
FT /note="RAA -> KAD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:2488273,
FT ECO:0000303|PubMed:9895129"
FT /id="VSP_024111"
FT VAR_SEQ 240..287
FT /note="CRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWM ->
FT FNLTVVSSSCTPQTSGLAKDAWEVARDSLFLEKKLGQGCFAEVWL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:2488273,
FT ECO:0000303|PubMed:9895129"
FT /id="VSP_024112"
FT MUTAGEN 2
FT /note="G->A: Abolishes myristoylation and palmitoylation."
FT /evidence="ECO:0000269|PubMed:7980442"
FT MUTAGEN 3
FT /note="C->A: Abolishes palmitoylation and plasma membrane
FT association; when associated with A-6."
FT /evidence="ECO:0000269|PubMed:7980442,
FT ECO:0000269|PubMed:8413237, ECO:0000269|PubMed:9201723"
FT MUTAGEN 3
FT /note="C->S: Abolishes palmitoylation and plasma membrane
FT association; when associated with S-6. Abolishes plasma
FT membrane association."
FT /evidence="ECO:0000269|PubMed:7980442,
FT ECO:0000269|PubMed:8413237, ECO:0000269|PubMed:9201723"
FT MUTAGEN 6
FT /note="C->A: Abolishes palmitoylation and plasma membrane
FT association; when associated with A-3."
FT /evidence="ECO:0000269|PubMed:7980442,
FT ECO:0000269|PubMed:8413237"
FT MUTAGEN 6
FT /note="C->S: Abolishes palmitoylation and plasma membrane
FT association; when associated with S-3."
FT /evidence="ECO:0000269|PubMed:7980442,
FT ECO:0000269|PubMed:8413237"
FT CONFLICT 179
FT /note="E -> Q (in Ref. 1; AAA37644 and 2; AAB09568)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="W -> R (in Ref. 3; BAE42585)"
FT /evidence="ECO:0000305"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3UF4"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:3UF4"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:3UF4"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:3UF4"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:3UF4"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3UF4"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3UF4"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:3UF4"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:3UF4"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3UF4"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:3UF4"
FT STRAND 194..207
FT /evidence="ECO:0007829|PDB:3UF4"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:3UF4"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3UF4"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:3UF4"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:3UF4"
SQ SEQUENCE 537 AA; 60675 MW; 99558702596DAEE0 CRC64;
MGCVQCKDKE AAKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHAAGGQG
LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW
EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET
TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC
RLVVPCHKGM PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT
LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMSKGSL LDFLKDGEGR
ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN GLICKIADFG LARLIEDNEY
TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE
RGYRMPCPQD CPISLHELMI HCWKKDPEER PTFEYLQGFL EDYFTATEPQ YQPGENL
