ID LCK_MOUSE STANDARD; PRT; 508 AA. AC P06240; Q61794; Q61795; Q62320; DT 01-JAN-1988 (Rel. 06, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE PROTO-ONCOGENE TYROSINE-PROTEIN KINASE LCK (EC 2.7.1.112) (P56-LCK) DE (LSK). GN LCK OR LSK-T. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86079521; PubMed=2416464; RA Marth J.D., Peet R., Krebs E.G., Perlmutter R.M.; RT "A lymphocyte-specific protein-tyrosine kinase gene is rearranged and RT overexpressed in the murine T cell lymphoma LSTRA."; RL Cell 43:393-404(1985). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=86146842; PubMed=3081813; RA Voronova A.F., Sefton B.M.; RT "Expression of a new tyrosine protein kinase is stimulated by RT retrovirus promoter insertion."; RL Nature 319:682-685(1986). RN [3] RP SEQUENCE OF 1-34 FROM N.A. RX MEDLINE=89096891; PubMed=2850479; RA Garvin A.M., Pawar S., Marth J.D., Perlmutter R.M.; RT "Structure of the murine lck gene and its rearrangement in a murine RT lymphoma cell line."; RL Mol. Cell. Biol. 8:3058-3064(1988). RN [4] RP SEQUENCE OF 1-10 FROM N.A. RX MEDLINE=88142832; PubMed=3501824; RA Voronova A.F., Adler H.T., Sefton B.M.; RT "Two lck transcripts containing different 5' untranslated regions are RT present in T cells."; RL Mol. Cell. Biol. 7:4407-4413(1987). RN [5] RP MUTAGENESIS OF TYR-504. RX MEDLINE=88248001; PubMed=3380790; RA Amrein K.E., Sefton B.M.; RT "Avian reovirus mRNAs are nonfunctional in infected mouse cells: RT translational basis for virus host-range restriction."; RL Proc. Natl. Acad. Sci. U.S.A. 85:4257-4261(1988). RN [6] RP MUTAGENESIS. RX MEDLINE=93059694; PubMed=1279202; RA Hurley T.R., Amrein K.E., Sefton B.M.; RT "Creation and characterization of temperature-sensitive mutants of the RT lck tyrosine protein kinase."; RL J. Virol. 66:7406-7413(1992). RN [7] RP MUTAGENESIS OF LYS-272. RX MEDLINE=91163633; PubMed=1706070; RA Abraham N., Miceli M.C., Parnes J.C., Veillette A.; RT "Enhancement of T-cell responsiveness by the lymphocyte-specific RT tyrosine protein kinase p56lck."; RL Nature 350:62-66(1991). RN [8] RP MUTAGENESIS OF TYR-504. RX MEDLINE=91219495; PubMed=1708890; RA Abraham K.M., Levin S.D., Marth J.D., Forbush K.A., Perlmutter R.M.; RT "Thymic tumorigenesis induced by overexpression of p56lck."; RL Proc. Natl. Acad. Sci. U.S.A. 88:3977-3981(1991). RN [9] RP MUTAGENESIS. RX MEDLINE=93133805; PubMed=8421674; RA Carrera A.C., Alexandrov K., Roberts T.M.; RT "The conserved lysine of the catalytic domain of protein kinases is RT actively involved in the phosphotransfer reaction and not required for RT anchoring ATP."; RL Proc. Natl. Acad. Sci. U.S.A. 90:442-446(1993). RN [10] RP PALMITOYLATION. RX MEDLINE=94019312; PubMed=8413237; 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 [11] RP PALMITOYLATION. RX MEDLINE=95071286; PubMed=7980442; 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- RT terminal motif."; RL Biochem. J. 303:749-753(1994). CC -!- FUNCTION: MAY PARTICIPATE IN ANTIGEN-INDUCED T-CELL ACTIVATION. CC ITS EARLY EXPRESSION IS ESSENTIAL FOR EARLY T-LYMPHOCYTE CC DEVELOPMENT. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + CC PROTEIN TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: BOUND TO THE CYTOPLASMIC DOMAIN OF EITHER CC CD4 OR CD8. CC -!- TISSUE SPECIFICITY: PRESENT AT A LOW LEVEL IN MOST T CELLS, AND CC AT AN ELEVATED LEVEL IN LSTRA AND THY 19 (T-CELL LYMPHOMA) CELLS. CC -!- DEVELOPMENTAL STAGE: LEVELS REMAIN RELATIVELY CONSTANT THROUGHOUT CC T-CELL ONTOGENY. CC -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN. CC -!- SIMILARITY: TO OTHER PROTEIN-TYROSINE KINASES IN THE CATALYTIC CC DOMAIN. BELONGS TO THE SRC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03533; CAA27234.1; -. DR EMBL; M12056; AAB59674.1; -. DR EMBL; X03533; CAA27235.1; ALT_SEQ. DR EMBL; X03533; CAA27236.1; ALT_SEQ. DR EMBL; M21511; AAA39422.1; ALT_SEQ. DR EMBL; M18098; AAA39421.1; -. DR PIR; A23639; A23639. DR HSSP; P06239; 1LCK. DR MGD; MGI:96756; Lck. DR INTERPRO; IPR000719; -. DR INTERPRO; IPR000980; -. DR INTERPRO; IPR001245; -. DR INTERPRO; IPR001452; -. DR PFAM; PF00017; SH2; 1. DR PFAM; PF00018; SH3; 1. DR PFAM; PF00069; pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00452; SH3DOMAIN. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. KW Proto-oncogene; Tyrosine-protein kinase; Phosphorylation; Transferase; KW ATP-binding; Myristate; SH2 domain; SH3 domain; Palmitate; KW Lipoprotein. FT INIT_MET 0 0 PROBABLE. FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT LIPID 2 2 PALMITATE. FT LIPID 4 4 PALMITATE. FT DOMAIN 60 120 SH3. FT DOMAIN 126 223 SH2. FT DOMAIN 244 497 PROTEIN KINASE. FT NP_BIND 250 258 ATP (BY SIMILARITY). FT BINDING 272 272 ATP (BY SIMILARITY). FT ACT_SITE 363 363 BY SIMILARITY. FT MOD_RES 393 393 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT MOD_RES 504 504 PHOSPHORYLATION (NEGATIVE REGULATION) (BY FT SIMILARITY). FT MUTAGEN 268 268 K->N: REDUCED ACTIVITY. FT MUTAGEN 269 269 V->L: REDUCED ACTIVITY. FT MUTAGEN 270 270 A->S: REDUCED ACTIVITY. FT MUTAGEN 271 271 V->A: REDUCED ACTIVITY. FT MUTAGEN 272 272 K->R: LOSS OF ACTIVITY. FT MUTAGEN 273 273 S->N: REDUCED ACTIVITY. FT MUTAGEN 274 274 L->M: REDUCED ACTIVITY. FT MUTAGEN 275 275 K->V: REDUCED ACTIVITY. FT MUTAGEN 504 504 Y->F: CAUSES THYMIC TUMORS. FT CONFLICT 282 283 VP -> DA (IN REF. 2). SQ SEQUENCE 508 AA; 57821 MW; E92562498CAF6878 CRC64; GCVCSSNPED DWMENIDVCE NCHYPIVPLD SKISLPIRNG SEVRDPLVTY EGSLPPASPL QDNLVIALHS YEPSHDGDLG FEKGEQLRIL EQSGEWWKAQ SLTTGQEGFI PFNFVAKANS LEPEPWFFKN LSRKDAERQL LAPGNTHGSF LIRESESTAG SFSLSVRDFD QNQGEVVKHY KIRNLDNGGF YISPRITFPG LHDLVRHYTN ASDGLCTKLS RPCQTQKPQK PWWEDEWEVP RETLKLVERL GAGQFGEVWM GYYNGHTKVA VKSLKQGSMS PVPFLAEANL MKQLQHPRLV RLYAVVTQEP IYIITEYMEN GSLVDFLKTP SGIKLNVNKL LDMAAQIAEG MAFIEEQNYI HRDLRAANIL VSDTLSCKIA DFGLARLIED NEYTAREGAK FPIKWTAPEA INYGTFTIKS DVWSFGILLT EIVTHGRIPY PGMTNPEVIQ NLERGYRMVR PDNCPEELYH LMMLCWKERP EDRPTFDYLR SVLDDFFTAT EGQYQPQP //