LCK_CHICK
ID LCK_CHICK Reviewed; 508 AA.
AC P42683; Q53WS8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Proto-oncogene tyrosine-protein kinase LCK;
DE EC=2.7.10.2;
DE AltName: Full=Protein-tyrosine kinase C-TKL;
DE AltName: Full=p56tk1;
GN Name=LCK;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RA Gaertner T., Khnel H., Strebhardt K., Ruebsamen-Waigmann H.;
RL Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-89.
RX PubMed=1545804; DOI=10.1128/mcb.12.3.1226-1233.1992;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 47-508.
RX PubMed=3321053; DOI=10.1073/pnas.84.24.8778;
RA Strebhardt K., Mullins J.I., Bruck C., Ruebsamen-Waigmann H.;
RT "Additional member of the protein-tyrosine kinase family: the src- and lck-
RT related protooncogene c-tkl.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8778-8782(1987).
CC -!- FUNCTION: Tyrosine kinase that plays an essential role for the
CC selection and maturation of developing T-cell in the thymus and in
CC mature T-cell function. Is constitutively associated with the
CC cytoplasmic portions of the CD4 and CD8 surface receptors and plays a
CC key role in T-cell antigen receptor(TCR)-linked signal transduction
CC pathways (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Inhibited by tyrosine phosphorylation.
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds to the cytoplasmic domain of cell surface receptors,
CC such as CD4, CD8. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P06239};
CC Lipid-anchor {ECO:0000250|UniProtKB:P06239}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P06239}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P06239}.
CC -!- PTM: Phosphorylated on Tyr-393, which increases enzymatic activity,
CC this site is dephosphorylated by PTN22. Phosphorylated on Tyr-504,
CC presumably by CSK, which decreases activity. Dephosphorylated by
CC PTPRC/CD45. Dephosphorylation at Tyr-393 by PTPN2 negatively regulates
CC T-cells differentiation (By similarity). {ECO:0000250}.
CC -!- PTM: Palmitoylation regulates association with the plasma membrane.
CC {ECO:0000250|UniProtKB:P06239}.
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=AAA49081.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X60380; CAA42930.1; -; mRNA.
DR EMBL; M85043; AAA49003.1; -; mRNA.
DR EMBL; J03579; AAA49081.1; ALT_INIT; mRNA.
DR PIR; A42126; A39939.
DR AlphaFoldDB; P42683; -.
DR SMR; P42683; -.
DR STRING; 9031.ENSGALP00000000634; -.
DR iPTMnet; P42683; -.
DR VEuPathDB; HostDB:geneid_396460; -.
DR eggNOG; KOG0197; Eukaryota.
DR InParanoid; P42683; -.
DR PhylomeDB; P42683; -.
DR BRENDA; 2.7.10.2; 1306.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0000242; C:pericentriolar material; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; ISS:UniProtKB.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0050870; P:positive regulation of T cell activation; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
DR CDD; cd10362; SH2_Src_Lck; 1.
DR CDD; cd12005; SH3_Lck; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR035850; Lck_SH2.
DR InterPro; IPR035749; Lck_SH3.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Cytoplasm; Kinase; Lipoprotein; Membrane;
KW Myristate; Nucleotide-binding; 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:0000305"
FT CHAIN 2..508
FT /note="Proto-oncogene tyrosine-protein kinase LCK"
FT /id="PRO_0000088128"
FT DOMAIN 60..120
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 126..223
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 244..497
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 250..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 393
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 504
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 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 508 AA; 58140 MW; BC83C4E61CB66170 CRC64;
MGCCCSSDYD EDWIENIDIC EHCNYPIDPD SKRQQLIRNV SEVRDPLVSY EAMSPPCSPL
QDKLVVALYD YEPTHDGDLG LKQGEKLRVL EESGEWWRAQ SLTTGQEGLI PHNFVAMVNS
LEPEPWFFKN LSRKNAEARL LASGNTHGSF LIRESETSKG SYSLSVRDFD QNQGETVKHY
KIRNMDNGGY YISPRVTFSS LHELVEYYSS SSDGLCTRLG KPCRTQKPQK PWWQDEWEVP
RESLKLVEKL GAGQFGEVWM GFYNGHTKVA IKNLKQGSMS PSAFLAEANL MKNLQHPRLV
RLYAVVTKEP IYIITEYMEK GSLVDFLKTS EGIKLSINKL LDMAAQIAEG MAFIEAKNYI
HRDLRAANIL VSEALCCKIA DFGLARLIED NEYTAREGAK FPIKWTAPEA INYGTFTIKS
DVWSFGILLT EIVTYGRIPY PGMTNPEVIQ NLERGYRMPQ PDNCPQELYE LMMQCWKEQP
EERPTFEYMK SVLEDFFTAT EGQYQQQP
