LAIR1_MOUSE
ID LAIR1_MOUSE Reviewed; 263 AA.
AC Q8BG84; Q80UN5; Q8BHB6; Q8BRR6; Q8C6N8; Q8CEP5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Leukocyte-associated immunoglobulin-like receptor 1;
DE Short=LAIR-1;
DE Short=mLAIR1;
DE AltName: CD_antigen=CD305;
DE Flags: Precursor;
GN Name=Lair1;
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] (ISOFORMS 1; 2; 5 AND 6), TISSUE SPECIFICITY,
RP FUNCTION, DOMAIN ITIM MOTIF, AND INTERACTION WITH PTPN11.
RX PubMed=15100296; DOI=10.4049/jimmunol.172.9.5535;
RA Lebbink R.J., de Ruiter T., Verbrugge A., Bril W.S., Meyaard L.;
RT "The mouse homologue of the leukocyte-associated Ig-like receptor-1 is an
RT inhibitory receptor that recruits Src homology region 2-containing protein
RT tyrosine phosphatase (SHP)-2, but not SHP-1.";
RL J. Immunol. 172:5535-5543(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Brain cortex, Colon, Hypothalamus, Intestine, Liver, Oviduct, and
RC Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary gland;
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 [4]
RP INTERACTION WITH CSK.
RX PubMed=16380958; DOI=10.1002/eji.200535226;
RA Verbrugge A., Rijkers E.S.K., de Ruiter T., Meyaard L.;
RT "Leukocyte-associated Ig-like receptor-1 has SH2 domain-containing
RT phosphatase-independent function and recruits C-terminal Src kinase.";
RL Eur. J. Immunol. 36:190-198(2006).
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, ECO:0000269|PubMed:15100296}.
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: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=mLair-1a;
CC IsoId=Q8BG84-1; Sequence=Displayed;
CC Name=2; Synonyms=mLair-1b;
CC IsoId=Q8BG84-2; Sequence=VSP_020716;
CC Name=3;
CC IsoId=Q8BG84-3; Sequence=VSP_020714, VSP_020719;
CC Name=5; Synonyms=mLair-1d;
CC IsoId=Q8BG84-5; Sequence=VSP_020715;
CC Name=6; Synonyms=mLair-1e;
CC IsoId=Q8BG84-6; Sequence=VSP_020718;
CC -!- TISSUE SPECIFICITY: Expressed in lymphoid organs and in cell lines of
CC hemopoietic origin. {ECO:0000269|PubMed:15100296}.
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:15100296}.
CC -!- PTM: Phosphorylation at Tyr-228 and Tyr-257 activates it. May be
CC phosphorylated by LCK (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25505.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC31610.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=BAC35674.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AY392763; AAR32125.1; -; mRNA.
DR EMBL; AY392764; AAR32126.1; -; mRNA.
DR EMBL; AY392765; AAR32127.1; -; mRNA.
DR EMBL; AY392766; AAR32128.1; -; mRNA.
DR EMBL; AK017222; BAC25505.1; ALT_FRAME; mRNA.
DR EMBL; AK033472; BAC28306.1; -; mRNA.
DR EMBL; AK038574; BAC30051.1; -; mRNA.
DR EMBL; AK043664; BAC31610.1; ALT_SEQ; mRNA.
DR EMBL; AK044465; BAC31936.1; -; mRNA.
DR EMBL; AK050281; BAC34164.1; -; mRNA.
DR EMBL; AK054158; BAC35674.1; ALT_SEQ; mRNA.
DR EMBL; BC025901; AAH25901.1; -; mRNA.
DR CCDS; CCDS20729.1; -. [Q8BG84-2]
DR CCDS; CCDS51969.1; -. [Q8BG84-1]
DR CCDS; CCDS80654.1; -. [Q8BG84-6]
DR CCDS; CCDS85202.1; -. [Q8BG84-5]
DR RefSeq; NP_001106945.1; NM_001113474.1. [Q8BG84-1]
DR RefSeq; NP_001289604.1; NM_001302675.1. [Q8BG84-6]
DR RefSeq; NP_001289605.1; NM_001302676.1.
DR RefSeq; NP_001289606.1; NM_001302677.1. [Q8BG84-5]
DR RefSeq; NP_001289610.1; NM_001302681.1.
DR RefSeq; NP_001289611.1; NM_001302682.1.
DR RefSeq; NP_001289612.1; NM_001302683.1.
DR RefSeq; NP_848726.1; NM_178611.6. [Q8BG84-2]
DR RefSeq; XP_006540238.1; XM_006540175.3. [Q8BG84-1]
DR RefSeq; XP_006540239.1; XM_006540176.3. [Q8BG84-1]
DR RefSeq; XP_017177847.1; XM_017322358.1. [Q8BG84-2]
DR RefSeq; XP_017177848.1; XM_017322359.1.
DR PDB; 4ESK; X-ray; 1.76 A; A/B/C/D=22-121.
DR PDB; 4ETY; X-ray; 1.90 A; A/B/C/D=22-133.
DR PDBsum; 4ESK; -.
DR PDBsum; 4ETY; -.
DR AlphaFoldDB; Q8BG84; -.
DR SMR; Q8BG84; -.
DR DIP; DIP-61634N; -.
DR IntAct; Q8BG84; 1.
DR STRING; 10090.ENSMUSP00000083589; -.
DR GlyGen; Q8BG84; 2 sites.
DR PhosphoSitePlus; Q8BG84; -.
DR EPD; Q8BG84; -.
DR MaxQB; Q8BG84; -.
DR PaxDb; Q8BG84; -.
DR PRIDE; Q8BG84; -.
DR ProteomicsDB; 264825; -. [Q8BG84-1]
DR ProteomicsDB; 264826; -. [Q8BG84-2]
DR ProteomicsDB; 264828; -. [Q8BG84-5]
DR ProteomicsDB; 264829; -. [Q8BG84-6]
DR Antibodypedia; 2596; 804 antibodies from 37 providers.
DR DNASU; 52855; -.
DR Ensembl; ENSMUST00000068865; ENSMUSP00000070712; ENSMUSG00000055541. [Q8BG84-2]
DR Ensembl; ENSMUST00000086401; ENSMUSP00000083589; ENSMUSG00000055541. [Q8BG84-1]
DR Ensembl; ENSMUST00000108600; ENSMUSP00000104241; ENSMUSG00000055541. [Q8BG84-6]
DR Ensembl; ENSMUST00000131126; ENSMUSP00000121738; ENSMUSG00000055541. [Q8BG84-3]
DR Ensembl; ENSMUST00000136616; ENSMUSP00000122037; ENSMUSG00000055541. [Q8BG84-3]
DR Ensembl; ENSMUST00000149395; ENSMUSP00000116800; ENSMUSG00000055541. [Q8BG84-3]
DR Ensembl; ENSMUST00000205296; ENSMUSP00000145940; ENSMUSG00000055541. [Q8BG84-5]
DR GeneID; 52855; -.
DR KEGG; mmu:52855; -.
DR UCSC; uc009ews.2; mouse. [Q8BG84-2]
DR UCSC; uc009ewt.2; mouse. [Q8BG84-1]
DR UCSC; uc012ewk.1; mouse. [Q8BG84-5]
DR UCSC; uc012ewl.1; mouse. [Q8BG84-6]
DR CTD; 3903; -.
DR MGI; MGI:105492; Lair1.
DR VEuPathDB; HostDB:ENSMUSG00000055541; -.
DR eggNOG; ENOG502TBGD; Eukaryota.
DR GeneTree; ENSGT00940000162693; -.
DR HOGENOM; CLU_1712690_0_0_1; -.
DR InParanoid; Q8BG84; -.
DR OMA; CIYQIES; -.
DR OrthoDB; 1481318at2759; -.
DR PhylomeDB; Q8BG84; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 52855; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Lair1; mouse.
DR PRO; PR:Q8BG84; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BG84; protein.
DR Bgee; ENSMUSG00000055541; Expressed in granulocyte and 110 other tissues.
DR ExpressionAtlas; Q8BG84; baseline and differential.
DR Genevisible; Q8BG84; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; 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_0000250683"
FT TOPO_DOM 22..144
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..115
FT /note="Ig-like C2-type"
FT MOTIF 226..231
FT /note="ITIM motif 1"
FT MOTIF 255..260
FT /note="ITIM motif 2"
FT MOD_RES 228
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6GTX8"
FT MOD_RES 257
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6GTX8"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 24..172
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15100296"
FT /id="VSP_020715"
FT VAR_SEQ 24..133
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15100296,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_020716"
FT VAR_SEQ 25..56
FT /note="SLPDITIFPNSSLMISQGTFVTVVCSYSDKHD -> ELCLWFLLYPWATLEL
FT IMCTWDAWKETLEYFL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020714"
FT VAR_SEQ 57..263
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020719"
FT VAR_SEQ 134..172
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15100296"
FT /id="VSP_020718"
FT CONFLICT 143..145
FT /note="IYI -> MYM (in Ref. 2; BAC25505)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="V -> G (in Ref. 2; BAC25505)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="L -> P (in Ref. 2; BAC25505)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="H -> R (in Ref. 3; AAH25901)"
FT /evidence="ECO:0000305"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:4ESK"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:4ESK"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:4ESK"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:4ESK"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:4ESK"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4ESK"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:4ESK"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:4ESK"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4ESK"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:4ESK"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:4ESK"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:4ESK"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:4ESK"
SQ SEQUENCE 263 AA; 29793 MW; B72D1E170DEF3404 CRC64;
MSLHPVILLV LVLCLGWKIN TQEGSLPDIT IFPNSSLMIS QGTFVTVVCS YSDKHDLYNM
VRLEKDGSTF MEKSTEPYKT EDEFEIGPVN ETITGHYSCI YSKGITWSER SKTLELKVIK
ENVIQTPAPG PTSDTSWLKT YSIYIFTVVS VIFLLCLSAL LFCFLRHRQK KQGLPNNKRQ
QQRPEERLNL ATNGLEMTPD IVADDRLPED RWTETWTPVA GDLQEVTYIQ LDHHSLTQRA
VGAVTSQSTD MAESSTYAAI IRH
