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Lck-interacting transmembrane adapter 1 (Lck-interacting molecule)

 LIME1_MOUSE             Reviewed;         269 AA.
Q9EQR5;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
23-MAY-2018, entry version 105.
RecName: Full=Lck-interacting transmembrane adapter 1;
AltName: Full=Lck-interacting molecule;
Name=Lime1; Synonyms=Lime;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH LCK; PTPN11; GRB2; PIK3R1
AND GRAP2, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF CYS-28;
CYS-31; TYR-242 AND TYR-261, PALMITOYLATION AT CYS-28 AND CYS-31,
PHOSPHORYLATION AT TYR-242 AND TYR-261, SUBCELLULAR LOCATION, AND
FUNCTION.
TISSUE=Lung;
PubMed=14610044; DOI=10.1084/jem.20030232;
Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.;
"LIME, a novel transmembrane adaptor protein, associates with p56lck
and mediates T cell activation.";
J. Exp. Med. 198:1463-1473(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
TISSUE SPECIFICITY, PHOSPHORYLATION AT TYR-137, INTERACTION WITH
PIK3R1; LYN; PLCG2 AND GRB2, MUTAGENESIS OF TYR-137; TYR-242 AND
TYR-261, AND FUNCTION.
PubMed=16249387; DOI=10.1182/blood-2005-05-1859;
Ahn E., Lee H., Yun Y.;
"LIME acts as a transmembrane adapter mediating BCR-dependent B-cell
activation.";
Blood 107:1521-1527(2006).
-!- FUNCTION: Involved in BCR (B-cell antigen receptor)-mediated
signaling in B-cells and TCR (T-cell antigen receptor)-mediated T-
cell signaling in T-cells. In absence of TCR signaling, may be
involved in CD4-mediated inhibition of T-cell activation. Couples
activation of these receptors and their associated kinases with
distal intracellular events such as calcium mobilization or MAPK
activation through the recruitment of PLCG2, GRB2, GRAP2, and
other signaling molecules. {ECO:0000269|PubMed:14610044,
ECO:0000269|PubMed:16249387}.
-!- SUBUNIT: When phosphorylated in response to TCR stimulation and/or
CD4 costimulation, interacts with LCK, CSK, FYN, PTPN11/SHP2,
GRB2, PIK3R1 and GRAP2 (By similarity). When phosphorylated in
response to BCR activation, interacts with LYN, PIK3R1, PLCG2 and
GRB2. {ECO:0000250, ECO:0000269|PubMed:14610044,
ECO:0000269|PubMed:16249387}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14610044};
Single-pass type III membrane protein
{ECO:0000269|PubMed:14610044}. Note=Present in lipid rafts.
Recruited to the immunological synapse upon conjugation of T-cell
with antigen-presenting cell.
-!- TISSUE SPECIFICITY: Expressed in spleen and lung. Present in
primary B-cells and peripheral T-cells (at protein level).
{ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:16249387}.
-!- INDUCTION: Up-regulated in T-cells following TCR engagement.
{ECO:0000269|PubMed:14610044}.
-!- PTM: Palmitoylation of Cys-28 and Cys-31 is required for raft
targeting. {ECO:0000269|PubMed:14610044}.
-!- PTM: Phosphorylated on tyrosines upon TCR activation and/or CD4
coreceptor stimulation, or upon BCR stimulation; which leads to
the recruitment of SH2-containing proteins.
{ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:16249387}.
-----------------------------------------------------------------------
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EMBL; AF115339; AAG35210.1; -; mRNA.
EMBL; BC023065; AAH23065.1; -; mRNA.
CCDS; CCDS17211.1; -.
RefSeq; NP_076173.1; NM_023684.2.
UniGene; Mm.440138; -.
ProteinModelPortal; Q9EQR5; -.
IntAct; Q9EQR5; 1.
STRING; 10090.ENSMUSP00000045010; -.
iPTMnet; Q9EQR5; -.
PhosphoSitePlus; Q9EQR5; -.
SwissPalm; Q9EQR5; -.
EPD; Q9EQR5; -.
PaxDb; Q9EQR5; -.
PRIDE; Q9EQR5; -.
Ensembl; ENSMUST00000048077; ENSMUSP00000045010; ENSMUSG00000090077.
GeneID; 72699; -.
KEGG; mmu:72699; -.
UCSC; uc008omd.1; mouse.
CTD; 54923; -.
MGI; MGI:1919949; Lime1.
eggNOG; ENOG410J9JT; Eukaryota.
eggNOG; ENOG41114H9; LUCA.
GeneTree; ENSGT00510000050080; -.
HOGENOM; HOG000231956; -.
HOVERGEN; HBG080499; -.
InParanoid; Q9EQR5; -.
OMA; LYSRVCK; -.
OrthoDB; EOG091G0IKW; -.
PhylomeDB; Q9EQR5; -.
TreeFam; TF337416; -.
PRO; PR:Q9EQR5; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000090077; -.
CleanEx; MM_LIME1; -.
ExpressionAtlas; Q9EQR5; baseline and differential.
Genevisible; Q9EQR5; MM.
GO; GO:0019815; C:B cell receptor complex; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0071008; C:U2-type post-mRNA release spliceosomal complex; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; IPI:MGI.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0050853; P:B cell receptor signaling pathway; IDA:MGI.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
GO; GO:0043405; P:regulation of MAP kinase activity; IMP:MGI.
GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IMP:MGI.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; IMP:MGI.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IMP:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0000390; P:spliceosomal complex disassembly; IBA:GO_Central.
GO; GO:0050852; P:T cell receptor signaling pathway; IEA:InterPro.
InterPro; IPR026072; Lime1.
Pfam; PF15332; LIME1; 1.
1: Evidence at protein level;
Adaptive immunity; Cell membrane; Complete proteome; Immunity;
Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 269 Lck-interacting transmembrane adapter 1.
/FTId=PRO_0000083333.
TOPO_DOM 1 7 Extracellular. {ECO:0000255}.
TRANSMEM 8 28 Helical; Signal-anchor for type III
membrane protein. {ECO:0000255}.
TOPO_DOM 29 269 Cytoplasmic. {ECO:0000255}.
REGION 137 140 Interaction with GRB2.
REGION 175 178 Interaction with CSK. {ECO:0000250}.
REGION 207 210 Interaction with CSK. {ECO:0000250}.
REGION 242 245 Interaction with LCK and PIK3R1.
{ECO:0000269|PubMed:14610044}.
REGION 261 264 Interaction with LCK, PLCG2 and PIK3R1.
{ECO:0000269|PubMed:14610044,
ECO:0000269|PubMed:16249387}.
MOD_RES 137 137 Phosphotyrosine.
{ECO:0000305|PubMed:16249387}.
MOD_RES 175 175 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9H400}.
MOD_RES 207 207 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9H400}.
MOD_RES 242 242 Phosphotyrosine; by LYN or LCK.
{ECO:0000305|PubMed:14610044}.
MOD_RES 261 261 Phosphotyrosine; by LYN or LCK.
{ECO:0000305|PubMed:14610044}.
MOD_RES 263 263 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H400}.
LIPID 28 28 S-palmitoyl cysteine.
{ECO:0000305|PubMed:14610044}.
LIPID 31 31 S-palmitoyl cysteine.
{ECO:0000305|PubMed:14610044}.
MUTAGEN 28 28 C->S: Abolishes palmitoylation and lipid
raft localization; when associated with
S-31. {ECO:0000269|PubMed:14610044}.
MUTAGEN 31 31 C->S: Abolishes palmitoylation and lipid
raft localization; when associated with
S-28. {ECO:0000269|PubMed:14610044}.
MUTAGEN 137 137 Y->F: Reduces GRB2 binding.
{ECO:0000269|PubMed:16249387}.
MUTAGEN 242 242 Y->F: Abolishes LCK, PIK3R1 and LYN
binding; when associated with F-261.
{ECO:0000269|PubMed:14610044,
ECO:0000269|PubMed:16249387}.
MUTAGEN 261 261 Y->F: Strongly reduces PLCG2 binding.
Abolishes LCK, PIK3R1 and LYN binding;
when associated with F-242.
{ECO:0000269|PubMed:14610044,
ECO:0000269|PubMed:16249387}.
SEQUENCE 269 AA; 29551 MW; B37A1059EB723FBF CRC64;
MRPPVPSAPL ALWVLGCFSL LLWLWALCTA CHRKRAQRQQ TGLQDSLVPV EMPLLRQTHL
CSLSKSDTRL HELHRGPRSS IAPRPASMDL LHPRWLEMSR GSTRSQVPNS AFPPRQLPRA
PPAAPATAPS TSSEATYSNV GLAAIPRASL AASPVVWAGT QLTISCARLG PGAEYACIQK
HKGTEQGCQE LQQKAKVIPA TQMDVLYSRV CKPKRRDPRP VTDQLNLQDG RTSLPLGSDV
EYEAINLRGQ DMKQGPLENV YESIKEMGL


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