ID LCK_CHICK STANDARD; PRT; 507 AA. AC P42683; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE PROTO-ONCOGENE TYROSINE-PROTEIN KINASE LCK (EC 2.7.1.112) (PROTEIN- DE TYROSINE KINASE C-TKL). GN LCK. OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP SEQUENCE OF 1-88 FROM N.A. RX MEDLINE=92186854; PubMed=1545804; RA Chow L., Ratcliffe M., Veillette A.; RT "tkl is the avian homolog of the mammalian lck tyrosine protein kinase RT gene."; RL Mol. Cell. Biol. 12:1226-1233(1992). RN [2] RP SEQUENCE OF 46-507 FROM N.A. RX MEDLINE=88097370; PubMed=3321053; RA Strebhardt K., Mullins J.I., Bruck C., Ruebsamen-Waigmann H.; RT "Additional member of the protein-tyrosine kinase family: the src-and RT lck-related protooncogene c-tkl."; RL Proc. Natl. Acad. Sci. U.S.A. 84:8778-8782(1987). CC -!- FUNCTION: MAY PARTICIPATE IN ANTIGEN-INDUCED T-CELL ACTIVATION. 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 -!- 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; M85043; AAA49003.1; -. DR EMBL; J03579; AAA49081.1; ALT_INIT. DR HSSP; P06239; 3LCK. 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 (BY SIMILARITY). FT LIPID 4 4 PALMITATE (BY SIMILARITY). FT DOMAIN 59 119 SH3. FT DOMAIN 125 222 SH2. FT DOMAIN 243 496 PROTEIN KINASE. FT NP_BIND 249 257 ATP (BY SIMILARITY). FT BINDING 271 271 ATP (BY SIMILARITY). FT ACT_SITE 362 362 BY SIMILARITY. FT MOD_RES 392 392 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT MOD_RES 503 503 PHOSPHORYLATION (NEGATIVE REGULATION) (BY FT SIMILARITY). SQ SEQUENCE 507 AA; 58008 MW; BC83C4FA891B6170 CRC64; GCCCSSDYDE DWIENIDICE HCNYPIDPDS KRQQLIRNVS EVRDPLVSYE AMSPPCSPLQ DKLVVALYDY EPTHDGDLGL KQGEKLRVLE ESGEWWRAQS LTTGQEGLIP HNFVAMVNSL EPEPWFFKNL SRKNAEARLL ASGNTHGSFL IRESETSKGS YSLSVRDFDQ NQGETVKHYK IRNMDNGGYY ISPRVTFSSL HELVEYYSSS SDGLCTRLGK PCRTQKPQKP WWQDEWEVPR ESLKLVEKLG AGQFGEVWMG FYNGHTKVAI KNLKQGSMSP SAFLAEANLM KNLQHPRLVR LYAVVTKEPI YIITEYMEKG SLVDFLKTSE GIKLSINKLL DMAAQIAEGM AFIEAKNYIH RDLRAANILV SEALCCKIAD FGLARLIEDN EYTAREGAKF PIKWTAPEAI NYGTFTIKSD VWSFGILLTE IVTYGRIPYP GMTNPEVIQN LERGYRMPQP DNCPQELYEL MMQCWKEQPE ERPTFEYMKS VLEDFFTATE GQYQQQP //