LAIR1_RAT
ID LAIR1_RAT Reviewed; 263 AA.
AC P0C1X9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Leukocyte-associated immunoglobulin-like receptor 1;
DE Short=LAIR-1;
DE Short=rLAIR1;
DE AltName: CD_antigen=CD305;
DE Flags: Precursor;
GN Name=Lair1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DOMAIN ITIM MOTIF, AND TISSUE SPECIFICITY.
RX PubMed=15902436; DOI=10.1007/s00251-005-0804-4;
RA Lebbink R.J., de Ruiter T., Kaptijn G.J.A., Meyaard L.;
RT "Identification and characterization of the rat homologue of LAIR-1.";
RL Immunogenetics 57:344-351(2005).
CC -!- FUNCTION: Functions as an inhibitory receptor that plays a constitutive
CC negative regulatory role on cytolytic function of natural killer (NK)
CC cells, B-cells and T-cells. Activation by Tyr phosphorylation results
CC in recruitment and activation of the phosphatases PTPN6 and PTPN11. It
CC also reduces the increase of intracellular calcium evoked by B-cell
CC receptor ligation. May also play its inhibitory role independently of
CC SH2-containing phosphatases. Modulates cytokine production in CD4+ T-
CC cells, down-regulating IL2 and IFNG production while inducing secretion
CC of transforming growth factor beta. Down-regulates also IgG and IgE
CC production in B-cells as well as IL8, IL10 and TNF secretion. Inhibits
CC proliferation and induces apoptosis in myeloid leukemia cell lines as
CC well as prevents nuclear translocation of NF-kappa-B p65 subunit/RELA
CC and phosphorylation of I-kappa-B alpha/CHUK in these cells. Inhibits
CC the differentiation of peripheral blood precursors towards dendritic
CC cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SH2 domains of tyrosine-protein phosphatases
CC PTPN6 and PTPN11. The interaction with PTPN6 is constitutive. Interacts
CC with the SH2 domain of CSK. Binds with high affinity to extracellular
CC matrix collagens, the interaction is functionally important (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in lymphoid and non-lymphoid organs.
CC {ECO:0000269|PubMed:15902436}.
CC -!- DOMAIN: ITIM (immunoreceptor tyrosine-based inhibitor motif) motif is a
CC cytoplasmic motif present in 2 copies in the intracellular part of
CC LAIR1. When phosphorylated, ITIM motif can bind the SH2 domain of
CC several SH2-containing phosphatases, leading to down-regulation of cell
CC activation. {ECO:0000269|PubMed:15902436}.
CC -!- PTM: Phosphorylation at Tyr-227 and Tyr-257 activates it. May be
CC phosphorylated by LCK (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
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DR EMBL; AY863023; AAX55651.1; -; mRNA.
DR RefSeq; NP_001025099.1; NM_001029928.1.
DR RefSeq; XP_008757196.1; XM_008758974.2.
DR RefSeq; XP_017445109.1; XM_017589620.1.
DR RefSeq; XP_017445110.1; XM_017589621.1.
DR RefSeq; XP_017445111.1; XM_017589622.1.
DR RefSeq; XP_017445112.1; XM_017589623.1.
DR AlphaFoldDB; P0C1X9; -.
DR SMR; P0C1X9; -.
DR STRING; 10116.ENSRNOP00000037815; -.
DR GlyGen; P0C1X9; 1 site.
DR PaxDb; P0C1X9; -.
DR Ensembl; ENSRNOT00000036413; ENSRNOP00000037815; ENSRNOG00000027733.
DR GeneID; 574531; -.
DR KEGG; rno:574531; -.
DR UCSC; RGD:1560048; rat.
DR CTD; 3903; -.
DR RGD; 1560048; Lair1.
DR eggNOG; ENOG502TBGD; Eukaryota.
DR GeneTree; ENSGT00940000162693; -.
DR HOGENOM; CLU_021100_3_1_1; -.
DR InParanoid; P0C1X9; -.
DR OMA; CIYQIES; -.
DR OrthoDB; 1481318at2759; -.
DR PhylomeDB; P0C1X9; -.
DR TreeFam; TF336644; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P0C1X9; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000027733; Expressed in spleen and 6 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..263
FT /note="Leukocyte-associated immunoglobulin-like receptor 1"
FT /id="PRO_0000250684"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 27..112
FT /note="Ig-like C2-type"
FT MOTIF 225..230
FT /note="ITIM motif 1"
FT MOTIF 255..260
FT /note="ITIM motif 2"
FT MOD_RES 227
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6GTX8"
FT MOD_RES 257
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6GTX8"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..96
FT /evidence="ECO:0000250"
SQ SEQUENCE 263 AA; 29724 MW; 7385B80F2A7AA52B CRC64;
MPLHSVIVLV LVLCLGWKSN TQEESLSDFT ICAEPGPVIP QGNFITIVCS TSGEYDTVRL
EKEGSTFMEK KTEPHGKQHR FRIGPVNETI TGYYNCIFEK NYVWSQRSND LQLKVIKENV
TQGLAPGPSM TSDTSWLKTY SIHILTVVSV IFLLCLSLFL FCFLSHRQKK QGLPNNKSQH
QRSQERLNLA TNGLEKTSDI VMDDSLSEDR QTETWTPVAG DLQEVTYAQL DHDSLTQRTV
KDVTPQNRVI MAESSTYAAI MRC
