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Q9EQR5 (LIME1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lck-interacting transmembrane adapter 1
Alternative name(s):
Lck-interacting molecule
Gene names
Name:Lime1
Synonyms:Lime
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.3

Subunit structure

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. Ref.1 Ref.3

Subcellular location

Cell membrane; Single-pass type III membrane protein. Note: Present in lipid rafts. Recruited to the immunological synapse upon conjugation of T-cell with antigen-presenting cell. Ref.1

Tissue specificity

Expressed in spleen and lung. Present in primary B-cells and peripheral T-cells (at protein level). Ref.1 Ref.3

Induction

Up-regulated in T-cells following TCR engagement. Ref.1

Post-translational modification

Palmitoylation of Cys-28 and Cys-31 is required for raft targeting. Ref.1

Phosphorylated on tyrosines upon TCR activation and/or CD4 coreceptor stimulation, or upon BCR stimulation; which leads to the recruitment of SH2-containing proteins. Ref.1 Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 269269Lck-interacting transmembrane adapter 1
PRO_0000083333

Regions

Topological domain1 – 77Extracellular Potential
Transmembrane8 – 2821Helical; Signal-anchor for type III membrane protein; Potential
Topological domain29 – 269241Cytoplasmic Potential
Region137 – 1404Interaction with GRB2
Region175 – 1784Interaction with CSK By similarity
Region207 – 2104Interaction with CSK By similarity
Region242 – 2454Interaction with LCK and PIK3R1
Region261 – 2644Interaction with LCK, PLCG2 and PIK3R1

Amino acid modifications

Modified residue1371Phosphotyrosine Probable
Modified residue2071Phosphotyrosine By similarity
Modified residue2421Phosphotyrosine; by LYN or LCK Probable
Modified residue2611Phosphotyrosine; by LYN or LCK Probable
Lipidation281S-palmitoyl cysteine Probable
Lipidation311S-palmitoyl cysteine Probable

Experimental info

Mutagenesis281C → S: Abolishes palmitoylation and lipid raft localization; when associated with S-31. Ref.1
Mutagenesis311C → S: Abolishes palmitoylation and lipid raft localization; when associated with S-28. Ref.1
Mutagenesis1371Y → F: Reduces GRB2 binding. Ref.3
Mutagenesis2421Y → F: Abolishes LCK, PIK3R1 and LYN binding; when associated with F-261. Ref.1 Ref.3
Mutagenesis2611Y → F: Strongly reduces PLCG2 binding. Abolishes LCK, PIK3R1 and LYN binding; when associated with F-242. Ref.1 Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9EQR5 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: B37A1059EB723FBF

FASTA26929,551
        10         20         30         40         50         60 
MRPPVPSAPL ALWVLGCFSL LLWLWALCTA CHRKRAQRQQ TGLQDSLVPV EMPLLRQTHL 

        70         80         90        100        110        120 
CSLSKSDTRL HELHRGPRSS IAPRPASMDL LHPRWLEMSR GSTRSQVPNS AFPPRQLPRA 

       130        140        150        160        170        180 
PPAAPATAPS TSSEATYSNV GLAAIPRASL AASPVVWAGT QLTISCARLG PGAEYACIQK 

       190        200        210        220        230        240 
HKGTEQGCQE LQQKAKVIPA TQMDVLYSRV CKPKRRDPRP VTDQLNLQDG RTSLPLGSDV 

       250        260 
EYEAINLRGQ DMKQGPLENV YESIKEMGL 

« Hide

References

« Hide 'large scale' references
[1]"LIME, a novel transmembrane adaptor protein, associates with p56lck and mediates T cell activation."
Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.
J. Exp. Med. 198:1463-1473(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, FUNCTION.
Tissue: Lung.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[3]"LIME acts as a transmembrane adapter mediating BCR-dependent B-cell activation."
Ahn E., Lee H., Yun Y.
Blood 107:1521-1527(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH PIK3R1; LYN; PLCG2 AND GRB2, MUTAGENESIS OF TYR-137; TYR-242 AND TYR-261, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF115339 mRNA. Translation: AAG35210.1.
BC023065 mRNA. Translation: AAH23065.1.
CCDSCCDS17211.1.
RefSeqNP_076173.1. NM_023684.2.
UniGeneMm.440138.

3D structure databases

ProteinModelPortalQ9EQR5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9EQR5. 1 interaction.

PTM databases

PhosphoSiteQ9EQR5.

Proteomic databases

PaxDbQ9EQR5.
PRIDEQ9EQR5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000048077; ENSMUSP00000045010; ENSMUSG00000090077.
GeneID72699.
KEGGmmu:72699.
UCSCuc008omd.1. mouse.

Organism-specific databases

CTD54923.
MGIMGI:1919949. Lime1.

Phylogenomic databases

eggNOGNOG241375.
GeneTreeENSGT00510000050080.
HOGENOMHOG000231956.
HOVERGENHBG080499.
OMAVAEYACI.
PhylomeDBQ9EQR5.
TreeFamTF337416.

Gene expression databases

BgeeQ9EQR5.
CleanExMM_LIME1.
GenevestigatorQ9EQR5.

Family and domain databases

InterProIPR026072. Lime1.
[Graphical view]
PfamPF15332. LIME1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio336761.
PROQ9EQR5.
SOURCESearch...

Entry information

Entry nameLIME1_MOUSE
AccessionPrimary (citable) accession number: Q9EQR5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot