LIME1_MOUSE
ID LIME1_MOUSE Reviewed; 269 AA.
AC Q9EQR5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Lck-interacting transmembrane adapter 1;
DE AltName: Full=Lck-interacting molecule;
GN Name=Lime1; Synonyms=Lime;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH LCK; PTPN11; GRB2; PIK3R1 AND
RP GRAP2, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF CYS-28; CYS-31;
RP TYR-242 AND TYR-261, PALMITOYLATION AT CYS-28 AND CYS-31, PHOSPHORYLATION
RP AT TYR-242 AND TYR-261, SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Lung;
RX PubMed=14610044; DOI=10.1084/jem.20030232;
RA Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.;
RT "LIME, a novel transmembrane adaptor protein, associates with p56lck and
RT mediates T cell activation.";
RL J. Exp. Med. 198:1463-1473(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY, PHOSPHORYLATION AT TYR-137, INTERACTION WITH PIK3R1;
RP LYN; PLCG2 AND GRB2, MUTAGENESIS OF TYR-137; TYR-242 AND TYR-261, AND
RP FUNCTION.
RX PubMed=16249387; DOI=10.1182/blood-2005-05-1859;
RA Ahn E., Lee H., Yun Y.;
RT "LIME acts as a transmembrane adapter mediating BCR-dependent B-cell
RT activation.";
RL Blood 107:1521-1527(2006).
CC -!- FUNCTION: Involved in BCR (B-cell antigen receptor)-mediated signaling
CC in B-cells and TCR (T-cell antigen receptor)-mediated T-cell signaling
CC in T-cells. In absence of TCR signaling, may be involved in CD4-
CC mediated inhibition of T-cell activation. Couples activation of these
CC receptors and their associated kinases with distal intracellular events
CC such as calcium mobilization or MAPK activation through the recruitment
CC of PLCG2, GRB2, GRAP2, and other signaling molecules.
CC {ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:16249387}.
CC -!- SUBUNIT: When phosphorylated in response to TCR stimulation and/or CD4
CC costimulation, interacts with LCK, CSK, FYN, PTPN11/SHP2, GRB2, PIK3R1
CC and GRAP2 (By similarity). When phosphorylated in response to BCR
CC activation, interacts with LYN, PIK3R1, PLCG2 and GRB2. {ECO:0000250,
CC ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:16249387}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14610044};
CC Single-pass type III membrane protein {ECO:0000269|PubMed:14610044}.
CC Note=Present in lipid rafts. Recruited to the immunological synapse
CC upon conjugation of T-cell with antigen-presenting cell.
CC -!- TISSUE SPECIFICITY: Expressed in spleen and lung. Present in primary B-
CC cells and peripheral T-cells (at protein level).
CC {ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:16249387}.
CC -!- INDUCTION: Up-regulated in T-cells following TCR engagement.
CC {ECO:0000269|PubMed:14610044}.
CC -!- PTM: Palmitoylation of Cys-28 and Cys-31 is required for raft
CC targeting. {ECO:0000269|PubMed:14610044}.
CC -!- PTM: Phosphorylated on tyrosines upon TCR activation and/or CD4
CC coreceptor stimulation, or upon BCR stimulation; which leads to the
CC recruitment of SH2-containing proteins. {ECO:0000269|PubMed:14610044,
CC ECO:0000269|PubMed:16249387}.
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DR EMBL; AF115339; AAG35210.1; -; mRNA.
DR EMBL; BC023065; AAH23065.1; -; mRNA.
DR CCDS; CCDS17211.1; -.
DR RefSeq; NP_076173.1; NM_023684.2.
DR AlphaFoldDB; Q9EQR5; -.
DR STRING; 10090.ENSMUSP00000045010; -.
DR iPTMnet; Q9EQR5; -.
DR PhosphoSitePlus; Q9EQR5; -.
DR SwissPalm; Q9EQR5; -.
DR EPD; Q9EQR5; -.
DR jPOST; Q9EQR5; -.
DR PaxDb; Q9EQR5; -.
DR PRIDE; Q9EQR5; -.
DR ProteomicsDB; 292258; -.
DR DNASU; 72699; -.
DR Ensembl; ENSMUST00000048077; ENSMUSP00000045010; ENSMUSG00000090077.
DR GeneID; 72699; -.
DR KEGG; mmu:72699; -.
DR UCSC; uc008omd.1; mouse.
DR CTD; 54923; -.
DR MGI; MGI:1919949; Lime1.
DR VEuPathDB; HostDB:ENSMUSG00000090077; -.
DR eggNOG; ENOG502RGRF; Eukaryota.
DR GeneTree; ENSGT00510000050080; -.
DR HOGENOM; CLU_094813_0_0_1; -.
DR InParanoid; Q9EQR5; -.
DR OMA; HQELPWA; -.
DR OrthoDB; 1143036at2759; -.
DR PhylomeDB; Q9EQR5; -.
DR TreeFam; TF337416; -.
DR BioGRID-ORCS; 72699; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Lime1; mouse.
DR PRO; PR:Q9EQR5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9EQR5; protein.
DR Bgee; ENSMUSG00000090077; Expressed in granulocyte and 67 other tissues.
DR ExpressionAtlas; Q9EQR5; baseline and differential.
DR Genevisible; Q9EQR5; MM.
DR GO; GO:0019815; C:B cell receptor complex; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IDA:MGI.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0043405; P:regulation of MAP kinase activity; IMP:MGI.
DR GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; IMP:MGI.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:InterPro.
DR InterPro; IPR026072; Lime1.
DR PANTHER; PTHR47740; PTHR47740; 1.
DR Pfam; PF15332; LIME1; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Immunity; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..269
FT /note="Lck-interacting transmembrane adapter 1"
FT /id="PRO_0000083333"
FT TOPO_DOM 1..7
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 102..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..140
FT /note="Interaction with GRB2"
FT REGION 175..178
FT /note="Interaction with CSK"
FT /evidence="ECO:0000250"
FT REGION 207..210
FT /note="Interaction with CSK"
FT /evidence="ECO:0000250"
FT REGION 242..245
FT /note="Interaction with LCK and PIK3R1"
FT /evidence="ECO:0000269|PubMed:14610044"
FT REGION 261..264
FT /note="Interaction with LCK, PLCG2 and PIK3R1"
FT /evidence="ECO:0000269|PubMed:14610044,
FT ECO:0000269|PubMed:16249387"
FT MOD_RES 137
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:16249387"
FT MOD_RES 175
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9H400"
FT MOD_RES 207
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9H400"
FT MOD_RES 242
FT /note="Phosphotyrosine; by LYN or LCK"
FT /evidence="ECO:0000305|PubMed:14610044"
FT MOD_RES 261
FT /note="Phosphotyrosine; by LYN or LCK"
FT /evidence="ECO:0000305|PubMed:14610044"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H400"
FT LIPID 28
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:14610044"
FT LIPID 31
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:14610044"
FT MUTAGEN 28
FT /note="C->S: Abolishes palmitoylation and lipid raft
FT localization; when associated with S-31."
FT /evidence="ECO:0000269|PubMed:14610044"
FT MUTAGEN 31
FT /note="C->S: Abolishes palmitoylation and lipid raft
FT localization; when associated with S-28."
FT /evidence="ECO:0000269|PubMed:14610044"
FT MUTAGEN 137
FT /note="Y->F: Reduces GRB2 binding."
FT /evidence="ECO:0000269|PubMed:16249387"
FT MUTAGEN 242
FT /note="Y->F: Abolishes LCK, PIK3R1 and LYN binding; when
FT associated with F-261."
FT /evidence="ECO:0000269|PubMed:14610044,
FT ECO:0000269|PubMed:16249387"
FT MUTAGEN 261
FT /note="Y->F: Strongly reduces PLCG2 binding. Abolishes LCK,
FT PIK3R1 and LYN binding; when associated with F-242."
FT /evidence="ECO:0000269|PubMed:14610044,
FT ECO:0000269|PubMed:16249387"
SQ 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
