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Proto-oncogene tyrosine-protein kinase LCK (EC 2.7.10.2) (Lymphocyte cell-specific protein-tyrosine kinase) (p56-LCK)

 LCK_SAISC               Reviewed;         509 AA.
Q95KR7;
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 105.
RecName: Full=Proto-oncogene tyrosine-protein kinase LCK;
EC=2.7.10.2;
AltName: Full=Lymphocyte cell-specific protein-tyrosine kinase;
AltName: Full=p56-LCK;
Name=LCK;
Saimiri sciureus (Common squirrel monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Platyrrhini; Cebidae; Saimiriinae; Saimiri.
NCBI_TaxID=9521;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, AND INTERACTION WITH
SAIMIRIINE HERPESVIRUS 2 TIP.
TISSUE=T-cell;
PubMed=11533187; DOI=10.1128/JVI.75.19.9252-9261.2001;
Greve T., Tamgueney G., Fleischer B., Fickenscher H., Broeker B.M.;
"Downregulation of p56Lck tyrosine kinase activity in T cells of
squirrel monkeys (Saimiri sciureus) correlates with the non-
transforming and apathogenic properties of herpesvirus saimiri in its
natural host.";
J. Virol. 75:9252-9261(2001).
-!- FUNCTION: Non-receptor tyrosine-protein kinase that plays an
essential role in the selection and maturation of developing T-
cells in the thymus and in the function of mature T-cells. Plays a
key role in T-cell antigen receptor (TCR)-linked signal
transduction pathways. Constitutively associated with the
cytoplasmic portions of the CD4 and CD8 surface receptors.
Association of the TCR with a peptide antigen-bound MHC complex
facilitates the interaction of CD4 and CD8 with MHC class II and
class I molecules, respectively, thereby recruiting the associated
LCK protein to the vicinity of the TCR/CD3 complex. LCK then
phosphorylates tyrosine residues within the immunoreceptor
tyrosine-based activation motifs (ITAM) of the cytoplasmic tails
of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3
signaling pathway. Once stimulated, the TCR recruits the tyrosine
kinase ZAP70, that becomes phosphorylated and activated by LCK.
Following this, a large number of signaling molecules are
recruited, ultimately leading to lymphokine production. LCK also
contributes to signaling by other receptor molecules. Associates
directly with the cytoplasmic tail of CD2, which leads to
hyperphosphorylation and activation of LCK. Also plays a role in
the IL2 receptor-linked signaling pathway that controls the T-cell
proliferative response. Binding of IL2 to its receptor results in
increased activity of LCK. Is expressed at all stages of thymocyte
development and is required for the regulation of maturation
events that are governed by both pre-TCR and mature alpha beta
TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2,
the microtubule-associated protein MAPT, RHOH or TYROBP (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: The relative activities of the inhibitory
tyrosine-protein kinase CSK and the activating tyrosine-protein
phosphatase PTPRC/CD45 determine the level of LCK activity. These
interactions allow rapid and efficient activation of LCK in
response to TCR stimulation (By similarity). {ECO:0000250}.
-!- SUBUNIT: Binds to the cytoplasmic domain of cell surface
receptors, such as AXL, CD2, CD4, CD5, CD8, CD44, CD45 and CD122.
Also binds to effector molecules, such as PI4K, VAV1, RASA1, FYB1
and to other protein kinases including CDK1, RAF1, ZAP70 and SYK.
Binds to phosphatidylinositol 3'-kinase (PI3K) from T-lymphocytes
through its SH3 domain and to the tyrosine phosphorylated form of
KHDRBS1/p70 through its SH2 domain. Interacts with SQSTM1.
Interacts with phosphorylated LIME1. Interacts with CBLB and
PTPRH. Interacts with RUNX3. Forms a signaling complex with EPHA1,
PTK2B AND PI3-KINASE; upon activation by EFNA1 which may regulate
T-lymphocytes migration. Associates with ZAP70 and RHOH; these
interactions allow LCK-mediated RHOH and CD3 subunit
phosphorylations in the presence of functional ZAP70 (By
similarity). Interacts with Saimiriine herpesvirus 2 TIP.
Interacts with UNC119; this interaction plays a crucial role in
activation of LCK. Interacts with CEACAM1 (via cytoplasmic
domain); mediates CEACAM1 phosphorylation resulting in PTPN6
recruitment that dephosphorylates TCR stimulation-induced CD247
and ZAP70. {ECO:0000250|UniProtKB:P06239}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Note=Present in lipid rafts in an inactive form.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed specifically in lymphoid cells.
-!- DEVELOPMENTAL STAGE: Levels remain relatively constant throughout
T-cell ontogeny.
-!- DOMAIN: The SH2 domain mediates interaction with SQSTM1.
Interaction is regulated by Ser-59 phosphorylation (By
similarity). {ECO:0000250}.
-!- PTM: Autophosphorylated on Tyr-394, increasing enzymatic activity,
this site is dephosphorylated by PTN22. Phosphorylated on Tyr-505
by CSK, decreasing activity. Dephosphorylated by PTPRC/CD45.
Dephosphorylation at Tyr-394 by PTPN2 negatively regulates T-cells
differentiation (By similarity). {ECO:0000250}.
-!- PTM: Myristoylation is required prior to palmitoylation.
{ECO:0000250}.
-!- PTM: Palmitoylation regulates subcellular location. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- CAUTION: LCK seems to be active in all vertebrates, except in
squirrel monkey T-cells, in which it is inactivated. The reason
seems to be that squirrel monkeys are the natural host for
Saimiriine herpesvirus 2, which is able to efficiently transform
T-cells through a mechanism involving viral Tip/ host LCK
interaction. Its inactivation may a mechanism that specifically
counteracts the transformation effects of viral Tip.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ277921; CAC38871.1; -; mRNA.
ProteinModelPortal; Q95KR7; -.
SMR; Q95KR7; -.
HOVERGEN; HBG008761; -.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0000242; C:pericentriolar material; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0006882; P:cellular zinc ion homeostasis; ISS:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0050870; P:positive regulation of T cell activation; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; ISS:UniProtKB.
GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
CDD; cd10362; SH2_Src_Lck; 1.
CDD; cd12005; SH3_Lck; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR035850; Lck_SH2.
InterPro; IPR035749; Lck_SH3.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Cytoplasm; Kinase; Lipoprotein; Membrane;
Myristate; Nucleotide-binding; Palmitate; Phosphoprotein;
Proto-oncogene; SH2 domain; SH3 domain; Transferase;
Tyrosine-protein kinase.
INIT_MET 1 1 Removed.
CHAIN 2 509 Proto-oncogene tyrosine-protein kinase
LCK.
/FTId=PRO_0000088127.
DOMAIN 61 121 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 127 224 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 245 498 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 251 259 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 2 72 Interactions with CD4 and CD8.
{ECO:0000250}.
REGION 154 242 Interaction with PTPRH. {ECO:0000250}.
ACT_SITE 364 364 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 273 273 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000250|UniProtKB:P06239}.
MOD_RES 159 159 Phosphothreonine.
{ECO:0000250|UniProtKB:P06239}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000250|UniProtKB:P06239}.
MOD_RES 192 192 Phosphotyrosine.
{ECO:0000250|UniProtKB:P06240}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000250|UniProtKB:P06239}.
MOD_RES 394 394 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P06239}.
MOD_RES 505 505 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P06239}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
LIPID 3 3 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 5 5 S-palmitoyl cysteine. {ECO:0000250}.
SEQUENCE 509 AA; 58253 MW; 5088C6407D109519 CRC64;
MGCGCSSHLE DDWMENIDVC ENCHYPIVPL DGKATLLFRN GSEVRDPLVR YEGSNPPASP
LQDNLVIALH SYEPSHDGDL GFEKGEHLRI LEQNGEWWKA QSLTTGQEGF VPFNFVAKAN
SLEPEPWFFK NLSRKDAERQ LLAPGNTHGS FLIRESESTA GSFSLSVRDF DQNQGEVVKH
YKIRNLDNGG FYISPRITFS GLHELVRHYT NASDGLCTRL SRPCQTQKPQ KPWWEDEWEV
PRETLKLVER LGAGQFGEVW MGYYNEHTKV AVKSLKQGSM SPDAFLAEAN LMKQLQHKRL
VRLYAVVTEE PIYIITEYME NGSLVDFLKT PSGIKLTINK LLDMAAQIVE GMAFLEERNY
IHRDLRAANI LVSDTLSCKI ADFGLARLIE DNEYTAREGA KFPIKWTAPE AINYGTFTIK
SDVWSFGILM TEIVTHGRIP YPGMTNPEVI QNLERGYRMP RPDNCPEELY KLMMQCWRER
PDDRPTFDYL RSVLEDFFTA TEGQYQPQP


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