TEC_MOUSE
ID TEC_MOUSE Reviewed; 630 AA.
AC P24604; Q9R1M9; Q9WVN0; Q9WVN1; Q9WVN2; Q9WVN3;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Tyrosine-protein kinase Tec;
DE EC=2.7.10.2;
GN Name=Tec;
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 1).
RX PubMed=7678927;
RA Mano H., Mano K., Tang B., Koehler M., Yi T., Gilbert D.J., Jenkins N.A.,
RA Copeland N.G., Ihle J.N.;
RT "Expression of a novel form of Tec kinase in hematopoietic cells and
RT mapping of the gene to chromosome 5 near Kit.";
RL Oncogene 8:417-424(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 4; 5 AND 6).
RC STRAIN=129;
RX PubMed=10343129; DOI=10.1159/000015240;
RA Merkel A.L., Atmosukarto I.I.C., Stevens K., Rathjen P.D., Booker G.W.;
RT "Splice variants of the mouse Tec gene are differentially expressed in
RT vivo.";
RL Cytogenet. Cell Genet. 84:132-139(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 82-630 (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=2284097;
RA Mano H., Ishikawa F., Nishida J., Hirai H., Takaku F.;
RT "A novel protein-tyrosine kinase, tec, is preferentially expressed in
RT liver.";
RL Oncogene 5:1781-1786(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 485-553.
RX PubMed=2482828; DOI=10.1016/0378-1119(89)90465-4;
RA Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.;
RT "The application of the polymerase chain reaction to cloning members of the
RT protein tyrosine kinase family.";
RL Gene 85:67-74(1989).
RN [5]
RP PHOSPHORYLATION, ACTIVITY REGULATION, AND INTERACTION WITH VAV1.
RX PubMed=8877094;
RA Miyazato A., Yamashita Y., Hatake K., Miura Y., Ozawa K., Mano H.;
RT "Tec protein tyrosine kinase is involved in the signaling mechanism of
RT granulocyte colony-stimulating factor receptor.";
RL Cell Growth Differ. 7:1135-1139(1996).
RN [6]
RP PHOSPHORYLATION BY LYN, ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-397.
RX PubMed=8621063; DOI=10.1096/fasebj.10.5.8621063;
RA Mano H., Yamashita Y., Miyazato A., Miura Y., Ozawa K.;
RT "Tec protein-tyrosine kinase is an effector molecule of Lyn protein-
RT tyrosine kinase.";
RL FASEB J. 10:637-642(1996).
RN [7]
RP FUNCTION, PHOSPHORYLATION OF JAK2, AND PHOSPHORYLATION AT TYR-518.
RX PubMed=9473212;
RA Yamashita Y., Watanabe S., Miyazato A., Ohya K., Ikeda U., Shimada K.,
RA Komatsu N., Hatake K., Miura Y., Ozawa K., Mano H.;
RT "Tec and Jak2 kinases cooperate to mediate cytokine-driven activation of c-
RT fos transcription.";
RL Blood 91:1496-1507(1998).
RN [8]
RP ACTIVITY REGULATION, AND FUNCTION IN THE CD28 SIGNALING PATHWAY.
RX PubMed=10382746;
RX DOI=10.1002/(sici)1521-4141(199906)29:06<1842::aid-immu1842>3.0.co;2-d;
RA Yang W.C., Olive D.;
RT "Tec kinase is involved in transcriptional regulation of IL-2 and IL-4 in
RT the CD28 pathway.";
RL Eur. J. Immunol. 29:1842-1849(1999).
RN [9]
RP INTERACTION WITH CD28, ACTIVITY REGULATION, AND FUNCTION IN PHOSPHORYLATION
RP OF DOK1.
RX PubMed=9872994; DOI=10.1074/jbc.274.2.607;
RA Yang W.C., Ghiotto M., Barbarat B., Olive D.;
RT "The role of Tec protein-tyrosine kinase in T cell signaling.";
RL J. Biol. Chem. 274:607-617(1999).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=15214045; DOI=10.1002/eji.200324777;
RA Garcon F., Ghiotto M., Gerard A., Yang W.C., Olive D., Nunes J.A.;
RT "The SH3 domain of Tec kinase is essential for its targeting to activated
RT CD28 costimulatory molecule.";
RL Eur. J. Immunol. 34:1972-1980(2004).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=15817477; DOI=10.1074/jbc.m412913200;
RA Kane L.P., Watkins S.C.;
RT "Dynamic regulation of Tec kinase localization in membrane-proximal
RT vesicles of a T cell clone revealed by total internal reflection
RT fluorescence and confocal microscopy.";
RL J. Biol. Chem. 280:21949-21954(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-518, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [13]
RP FUNCTION.
RX PubMed=19688741; DOI=10.1002/eji.200838839;
RA Schmidt U., Abramova A., Boucheron N., Eckelhart E., Schebesta A.,
RA Bilic I., Kneidinger M., Unger B., Hammer M., Sibilia M., Valent P.,
RA Ellmeier W.;
RT "The protein tyrosine kinase Tec regulates mast cell function.";
RL Eur. J. Immunol. 39:3228-3238(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-518, 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 [15]
RP SUBCELLULAR LOCATION.
RX PubMed=20543088; DOI=10.1152/ajpheart.00273.2010;
RA Zhang M.J., Franklin S., Li Y., Wang S., Ru X., Mitchell-Jordan S.A.,
RA Mano H., Stefani E., Ping P., Vondriska T.M.;
RT "Stress signaling by Tec tyrosine kinase in the ischemic myocardium.";
RL Am. J. Physiol. 299:H713-H722(2010).
RN [16]
RP FUNCTION IN THE HGF-INDUCED ERK SIGNALING PATHWAY.
RX PubMed=21094130; DOI=10.1016/j.bbrc.2010.11.068;
RA Li F., Jiang Y., Zheng Q., Yang X., Wang S.;
RT "TEC protein tyrosine kinase is involved in the Erk signaling pathway
RT induced by HGF.";
RL Biochem. Biophys. Res. Commun. 404:79-85(2011).
RN [17]
RP STRUCTURE BY NMR OF 179-245.
RX PubMed=11684687; DOI=10.1074/jbc.m108318200;
RA Pursglove S.E., Mulhern T.D., Mackay J.P., Hinds M.G., Booker G.W.;
RT "The solution structure and intramolecular associations of the Tec kinase
RT SRC homology 3 domain.";
RL J. Biol. Chem. 277:755-762(2002).
CC -!- FUNCTION: Non-receptor tyrosine kinase that contributes to signaling
CC from many receptors and participates as a signal transducer in multiple
CC downstream pathways, including regulation of the actin cytoskeleton.
CC Plays a redundant role to ITK in regulation of the adaptive immune
CC response. Regulates the development, function and differentiation of
CC conventional T-cells and nonconventional NKT-cells. Required for TCR-
CC dependent IL2 gene induction. Phosphorylates DOK1, one CD28-specific
CC substrate, and contributes to CD28-signaling. Mediates signals that
CC negatively regulate IL2RA expression induced by TCR cross-linking.
CC Plays a redundant role to BTK in BCR-signaling for B-cell development
CC and activation, especially by phosphorylating STAP1, a BCR-signaling
CC protein. Required in mast cells for efficient cytokine production.
CC Involved in both growth and differentiation mechanisms of myeloid cells
CC through activation by the granulocyte colony-stimulating factor CSF3, a
CC critical cytokine to promoting the growth, differentiation, and
CC functional activation of myeloid cells. Participates in platelet
CC signaling downstream of integrin activation. Cooperates with JAK2
CC through reciprocal phosphorylation to mediate cytokine-driven
CC activation of FOS transcription. GRB10, a negative modifier of the FOS
CC activation pathway, is another substrate of TEC. TEC is involved in G
CC protein-coupled receptor- and integrin-mediated signalings in blood
CC platelets. Plays a role in hepatocyte proliferation and liver
CC regeneration and is involved in HGF-induced ERK signaling pathway. TEC
CC regulates also FGF2 unconventional secretion (endoplasmic reticulum
CC (ER)/Golgi-independent mechanism) under various physiological
CC conditions through phosphorylation of FGF2 'Tyr-82'. May also be
CC involved in the regulation of osteoclast differentiation.
CC {ECO:0000269|PubMed:10382746, ECO:0000269|PubMed:15214045,
CC ECO:0000269|PubMed:19688741, ECO:0000269|PubMed:21094130,
CC ECO:0000269|PubMed:9473212, ECO:0000269|PubMed:9872994}.
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=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by tyrosine phosphorylation by a wide
CC range of cytokine stimulations. When T-cells or B-cells receptors are
CC activated, a series of phosphorylation leads to the recruitment of TEC
CC to the cell membrane, where it is phosphorylated at Tyr-518. Also
CC activated in response to SCF. Integrin engagement induces tyrosine
CC phosphorylation of TEC in platelets. STAP1 participates in a positive
CC feedback loop by increasing the activity of TEC. SOCS1 is an inhibitor
CC of TEC kinase activity. {ECO:0000269|PubMed:10382746,
CC ECO:0000269|PubMed:8621063, ECO:0000269|PubMed:8877094,
CC ECO:0000269|PubMed:9872994}.
CC -!- SUBUNIT: Interacts with INPP5D/SHIP1 and INPPL1/SHIP2. Interacts with
CC CD28, FASLG, FGF2, GRB10 and KIT (By similarity). Interacts with VAV1
CC and JAK2. Interacts with LYN. {ECO:0000250, ECO:0000269|PubMed:8877094,
CC ECO:0000269|PubMed:9872994}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC protein. Cytoplasm, cytoskeleton. Note=Following B-cell or T-cell
CC receptors activation by antigen, translocates to the plasma membrane
CC through its PH domain. Thrombin and integrin engagement induces
CC translocation of TEC to the cytoskeleton during platelet activation. In
CC cardiac myocytes, assumes a diffuse intracellular localization under
CC basal conditions but is recruited to striated structures upon various
CC stimuli, including ATP (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=TecIV;
CC IsoId=P24604-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P24604-2; Sequence=VSP_005012, VSP_005015;
CC Name=3; Synonyms=TecIIb;
CC IsoId=P24604-3; Sequence=VSP_005016;
CC Name=4; Synonyms=TecIIa;
CC IsoId=P24604-4; Sequence=VSP_005015, VSP_005016;
CC Name=5; Synonyms=TecIII;
CC IsoId=P24604-5; Sequence=VSP_005015;
CC Name=6; Synonyms=TecI;
CC IsoId=P24604-6; Sequence=VSP_005013, VSP_005014;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in liver. Expression is
CC also seen in the hematopoietic cells such as bone marrow, thymus and
CC spleen. Lower expression is seen in the heart, kidney and ovary.
CC -!- DOMAIN: The PH domain mediates the binding to inositol polyphosphate
CC and phosphoinositides, leading to its targeting to the plasma membrane.
CC It is extended in the BTK kinase family by a region designated the TH
CC (Tec homology) domain, which consists of about 80 residues preceding
CC the SH3 domain. {ECO:0000269|PubMed:15214045}.
CC -!- DOMAIN: The SH3 domain is essential for its targeting to activated CD28
CC costimulatory molecule. {ECO:0000250}.
CC -!- PTM: Following B-cell or T-cell receptors engagement, translocates to
CC the plasma membrane where it gets phosphorylated at Tyr-518. Undergoes
CC also tyrosine phosphorylation during platelet activation.
CC {ECO:0000269|PubMed:8621063, ECO:0000269|PubMed:8877094,
CC ECO:0000269|PubMed:9473212}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. TEC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; S53716; AAA13515.2; -; mRNA.
DR EMBL; AF071938; AAD43404.1; -; Genomic_DNA.
DR EMBL; AF071936; AAD43404.1; JOINED; Genomic_DNA.
DR EMBL; AF071937; AAD43404.1; JOINED; Genomic_DNA.
DR EMBL; AF071946; AAD43402.1; -; Genomic_DNA.
DR EMBL; AF071936; AAD43402.1; JOINED; Genomic_DNA.
DR EMBL; AF071937; AAD43402.1; JOINED; Genomic_DNA.
DR EMBL; AF071938; AAD43402.1; JOINED; Genomic_DNA.
DR EMBL; AF071939; AAD43402.1; JOINED; Genomic_DNA.
DR EMBL; AF071940; AAD43402.1; JOINED; Genomic_DNA.
DR EMBL; AF071941; AAD43402.1; JOINED; Genomic_DNA.
DR EMBL; AF071942; AAD43402.1; JOINED; Genomic_DNA.
DR EMBL; AF071943; AAD43402.1; JOINED; Genomic_DNA.
DR EMBL; AF071944; AAD43402.1; JOINED; Genomic_DNA.
DR EMBL; AF071945; AAD43402.1; JOINED; Genomic_DNA.
DR EMBL; AF071946; AAD43405.1; -; Genomic_DNA.
DR EMBL; AF071936; AAD43405.1; JOINED; Genomic_DNA.
DR EMBL; AF071937; AAD43405.1; JOINED; Genomic_DNA.
DR EMBL; AF071938; AAD43405.1; JOINED; Genomic_DNA.
DR EMBL; AF071939; AAD43405.1; JOINED; Genomic_DNA.
DR EMBL; AF071940; AAD43405.1; JOINED; Genomic_DNA.
DR EMBL; AF071941; AAD43405.1; JOINED; Genomic_DNA.
DR EMBL; AF071942; AAD43405.1; JOINED; Genomic_DNA.
DR EMBL; AF071943; AAD43405.1; JOINED; Genomic_DNA.
DR EMBL; AF071944; AAD43405.1; JOINED; Genomic_DNA.
DR EMBL; AF071945; AAD43405.1; JOINED; Genomic_DNA.
DR EMBL; AF071946; AAD43406.1; -; Genomic_DNA.
DR EMBL; AF071936; AAD43406.1; JOINED; Genomic_DNA.
DR EMBL; AF071937; AAD43406.1; JOINED; Genomic_DNA.
DR EMBL; AF071938; AAD43406.1; JOINED; Genomic_DNA.
DR EMBL; AF071940; AAD43406.1; JOINED; Genomic_DNA.
DR EMBL; AF071941; AAD43406.1; JOINED; Genomic_DNA.
DR EMBL; AF071942; AAD43406.1; JOINED; Genomic_DNA.
DR EMBL; AF071943; AAD43406.1; JOINED; Genomic_DNA.
DR EMBL; AF071944; AAD43406.1; JOINED; Genomic_DNA.
DR EMBL; AF071945; AAD43406.1; JOINED; Genomic_DNA.
DR EMBL; AF071946; AAD43407.1; -; Genomic_DNA.
DR EMBL; AF071936; AAD43407.1; JOINED; Genomic_DNA.
DR EMBL; AF071937; AAD43407.1; JOINED; Genomic_DNA.
DR EMBL; AF071938; AAD43407.1; JOINED; Genomic_DNA.
DR EMBL; AF071940; AAD43407.1; JOINED; Genomic_DNA.
DR EMBL; AF071941; AAD43407.1; JOINED; Genomic_DNA.
DR EMBL; AF071942; AAD43407.1; JOINED; Genomic_DNA.
DR EMBL; AF071943; AAD43407.1; JOINED; Genomic_DNA.
DR EMBL; AF071944; AAD43407.1; JOINED; Genomic_DNA.
DR EMBL; AF071945; AAD43407.1; JOINED; Genomic_DNA.
DR EMBL; X55663; CAA39196.1; -; mRNA.
DR EMBL; M33427; AAA40018.1; -; mRNA.
DR CCDS; CCDS51515.1; -. [P24604-5]
DR CCDS; CCDS51516.1; -. [P24604-1]
DR PIR; JU0215; JU0215.
DR PIR; S13763; S13763.
DR PIR; T01380; T01380.
DR RefSeq; NP_001106931.1; NM_001113460.2.
DR RefSeq; NP_001106932.1; NM_001113461.2.
DR RefSeq; NP_001106935.1; NM_001113464.2.
DR RefSeq; XP_006503908.1; XM_006503845.3.
DR RefSeq; XP_006503909.1; XM_006503846.3.
DR RefSeq; XP_011239020.1; XM_011240718.2.
DR RefSeq; XP_011239021.1; XM_011240719.2.
DR PDB; 1GL5; NMR; -; A=181-244.
DR PDBsum; 1GL5; -.
DR AlphaFoldDB; P24604; -.
DR BMRB; P24604; -.
DR SMR; P24604; -.
DR BioGRID; 204103; 20.
DR IntAct; P24604; 2.
DR MINT; P24604; -.
DR STRING; 10090.ENSMUSP00000071836; -.
DR iPTMnet; P24604; -.
DR PhosphoSitePlus; P24604; -.
DR EPD; P24604; -.
DR MaxQB; P24604; -.
DR PaxDb; P24604; -.
DR PeptideAtlas; P24604; -.
DR PRIDE; P24604; -.
DR ProteomicsDB; 262858; -. [P24604-1]
DR ProteomicsDB; 262859; -. [P24604-2]
DR ProteomicsDB; 262860; -. [P24604-3]
DR ProteomicsDB; 262861; -. [P24604-4]
DR ProteomicsDB; 262862; -. [P24604-5]
DR ProteomicsDB; 262863; -. [P24604-6]
DR DNASU; 21682; -.
DR GeneID; 21682; -.
DR KEGG; mmu:21682; -.
DR CTD; 7006; -.
DR MGI; MGI:98662; Tec.
DR eggNOG; KOG0197; Eukaryota.
DR InParanoid; P24604; -.
DR OrthoDB; 1047190at2759; -.
DR PhylomeDB; P24604; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-MMU-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR BioGRID-ORCS; 21682; 2 hits in 74 CRISPR screens.
DR EvolutionaryTrace; P24604; -.
DR PRO; PR:P24604; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P24604; protein.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid 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; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IBA:GO_Central.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0010543; P:regulation of platelet activation; ISO:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0042246; P:tissue regeneration; IBA:GO_Central.
DR CDD; cd11905; SH3_Tec; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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; IPR035572; Tec_SH3.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR001562; Znf_Btk_motif.
DR Pfam; PF00779; BTK; 1.
DR Pfam; PF00169; PH; 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; PR00402; TECBTKDOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00107; BTK; 1.
DR SMART; SM00233; PH; 1.
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; PS50003; PH_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.
DR PROSITE; PS51113; ZF_BTK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; ATP-binding;
KW Cell membrane; Cytoplasm; Cytoskeleton; Immunity; Kinase; Lipid-binding;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; SH2 domain; SH3 domain; Transferase;
KW Tyrosine-protein kinase; Zinc; Zinc-finger.
FT CHAIN 1..630
FT /note="Tyrosine-protein kinase Tec"
FT /id="PRO_0000088171"
FT DOMAIN 4..111
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 178..238
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 246..344
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 369..622
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 113..149
FT /note="Btk-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT ACT_SITE 488
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 375..383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 205
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P42680"
FT MOD_RES 227
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P42680"
FT MOD_RES 518
FT /note="Phosphotyrosine; by autocatalysis, LYN and JAK2"
FT /evidence="ECO:0000269|PubMed:9473212,
FT ECO:0007744|PubMed:17947660, ECO:0007744|PubMed:19144319"
FT VAR_SEQ 1..94
FT /note="MNFNTILEEILIKRSQQKKKTSLLNYKERLCVLPKSVLSYYEGRAEKKYRKG
FT VIDISKIKCVEIVKNDDGVIPCQNKFPFQVVHDANTLYIFAP -> MMVSFPVKINFHS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2284097"
FT /id="VSP_005012"
FT VAR_SEQ 82..100
FT /note="VVHDANTLYIFAPSPQSRD -> STKQGPMGEEVKRRNKEQQ (in
FT isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_005013"
FT VAR_SEQ 101..630
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_005014"
FT VAR_SEQ 224..245
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:2284097"
FT /id="VSP_005015"
FT VAR_SEQ 604..630
FT /note="RPEGRPSLEDLLRTIDELVECEETFGR -> ESCLCRVAQDLSSKNLIGSRF
FT (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005016"
FT MUTAGEN 397
FT /note="K->M: Impairs kinase activity."
FT /evidence="ECO:0000269|PubMed:8621063"
FT CONFLICT 23
FT /note="L -> P (in Ref. 2; AAD43404/AAD43402/AAD43405/
FT AAD43406/AAD43407)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="C -> F (in Ref. 2; AAD43404/AAD43402/AAD43405/
FT AAD43406/AAD43407)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="P -> T (in Ref. 2; AAD43404/AAD43402/AAD43405/
FT AAD43406/AAD43407)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="V -> E (in Ref. 4; AAA40018)"
FT /evidence="ECO:0000305"
FT CONFLICT 550..553
FT /note="FGVL -> YGIP (in Ref. 4; AAA40018)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="T -> S (in Ref. 2; AAD43402/AAD43405/AAD43406/
FT AAD43407)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="L -> F (in Ref. 2; AAD43404/AAD43402/AAD43405/
FT AAD43406/AAD43407 and 3; CAA39196)"
FT /evidence="ECO:0000305"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1GL5"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:1GL5"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:1GL5"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:1GL5"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1GL5"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1GL5"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:1GL5"
FT TURN 237..241
FT /evidence="ECO:0007829|PDB:1GL5"
SQ SEQUENCE 630 AA; 73426 MW; 262640EE90D4A6D2 CRC64;
MNFNTILEEI LIKRSQQKKK TSLLNYKERL CVLPKSVLSY YEGRAEKKYR KGVIDISKIK
CVEIVKNDDG VIPCQNKFPF QVVHDANTLY IFAPSPQSRD RWVKKLKEEI KNNNNIMIKY
HPKFWADGSY QCCRQTEKLA PGCEKYNLFE SSIRKTLPPA PEIKKRRPPP PIPPEEENTE
EIVVAMYDFQ ATEAHDLRLE RGQEYIILEK NDLHWWRARD KYGSEGYIPS NYVTGKKSNN
LDQYEWYCRN TNRSKAEQLL RTEDKEGGFM VRDSSQPGLY TVSLYTKFGG EGSSGFRHYH
IKETATSPKK YYLAEKHAFG SIPEIIEYHK HNAAGLVTRL RYPVSTKGKN APTTAGFSYD
KWEINPSELT FMRELGSGLF GVVRLGKWRA QYKVAIKAIR EGAMCEEDFI EEAKVMMKLT
HPKLVQLYGV CTQQKPIYIV TEFMERGCLL NFLRQRQGHF SRDMLLSMCQ DVCEGMEYLE
RNSFIHRDLA ARNCLVNEAG VVKVSDFGMA RYVLDDQYTS SSGAKFPVKW CPPEVFNYSR
FSSKSDVWSF GVLMWEIFTE GRMPFEKNTN YEVVTMVTRG HRLHRPKLAT KYLYEVMLRC
WQERPEGRPS LEDLLRTIDE LVECEETFGR
