LAIR1_HUMAN
ID LAIR1_HUMAN Reviewed; 287 AA.
AC Q6GTX8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Leukocyte-associated immunoglobulin-like receptor 1;
DE Short=LAIR-1;
DE Short=hLAIR1;
DE AltName: CD_antigen=CD305;
DE Flags: Precursor;
GN Name=LAIR1; Synonyms=CD305;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, GLYCOSYLATION,
RP SUBCELLULAR LOCATION, DOMAIN ITIM MOTIF, INTERACTION WITH PTPN6 AND PTPN11,
RP AND VARIANTS GLU-63; SER-92; PRO-98 AND THR-123.
RX PubMed=9285412; DOI=10.1016/s1074-7613(00)80530-0;
RA Meyaard L., Adema G.J., Chang C., Woollatt E., Sutherland G.R.,
RA Lanier L.L., Phillips J.H.;
RT "LAIR-1, a novel inhibitory receptor expressed on human mononuclear
RT leukocytes.";
RL Immunity 7:283-290(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP VARIANTS GLU-63; SER-92 AND PRO-98.
RX PubMed=10229813;
RA Meyaard L., Hurenkamp J., Clevers H., Lanier L.L., Phillips J.H.;
RT "Leukocyte-associated Ig-like receptor-1 functions as an inhibitory
RT receptor on cytotoxic T cells.";
RL J. Immunol. 162:5800-5804(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, PHOSPHORYLATION AT
RP TYR-251 AND TYR-281, MUTAGENESIS OF TYR-251 AND TYR-281, INTERACTION WITH
RP PTPN6, AND VARIANTS GLU-63; SER-92; PRO-98 AND THR-123.
RX PubMed=10764762; DOI=10.1074/jbc.m001313200;
RA Xu M.-J., Zhao R., Zhao Z.J.;
RT "Identification and characterization of leukocyte-associated Ig-like
RT receptor-1 as a major anchor protein of tyrosine phosphatase SHP-1 in
RT hematopoietic cells.";
RL J. Biol. Chem. 275:17440-17446(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-63;
RP SER-92; PRO-98 AND THR-123.
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-63;
RP SER-92; PRO-98 AND THR-123.
RC TISSUE=Pancreas;
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 [6]
RP FUNCTION.
RX PubMed=9692876;
RX DOI=10.1002/(sici)1521-4141(199807)28:07<2086::aid-immu2086>3.0.co;2-t;
RA Poggi A., Tomasello E., Ferrero E., Zocchi M.R., Moretta L.;
RT "p40/LAIR-1 regulates the differentiation of peripheral blood precursors to
RT dendritic cells induced by granulocyte-monocyte colony-stimulating
RT factor.";
RL Eur. J. Immunol. 28:2086-2091(1998).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10540327;
RX DOI=10.1002/(sici)1521-4141(199910)29:10<3160::aid-immu3160>3.0.co;2-s;
RA van der Vuurst de Vries A.-R., Clevers H., Logtenberg T., Meyaard L.;
RT "Leukocyte-associated immunoglobulin-like receptor-1 (LAIR-1) is
RT differentially expressed during human B cell differentiation and inhibits B
RT cell receptor-mediated signaling.";
RL Eur. J. Immunol. 29:3160-3167(1999).
RN [8]
RP FUNCTION.
RX PubMed=11069054;
RX DOI=10.1002/1521-4141(200010)30:10<2751::aid-immu2751>3.0.co;2-l;
RA Poggi A., Pellegatta F., Leone B.E., Moretta L., Zocchi M.R.;
RT "Engagement of the leukocyte-associated Ig-like receptor-1 induces
RT programmed cell death and prevents NF-kappaB nuclear translocation in human
RT myeloid leukemias.";
RL Eur. J. Immunol. 30:2751-2758(2000).
RN [9]
RP SUBCELLULAR LOCATION, INTERACTION WITH PTPN6, AND FUNCTION.
RX PubMed=11160222; DOI=10.4049/jimmunol.166.3.1763;
RA Sathish J.G., Johnson K.G., Fuller K.J., LeRoy F.G., Meyaard L., Sims M.J.,
RA Matthews R.J.;
RT "Constitutive association of SHP-1 with leukocyte-associated Ig-like
RT receptor-1 in human T cells.";
RL J. Immunol. 166:1763-1770(2001).
RN [10]
RP FUNCTION.
RX PubMed=12072189; DOI=10.1016/s0198-8859(02)00409-3;
RA Saverino D., Fabbi M., Merlo A., Ravera G., Grossi C.E., Ciccone E.;
RT "Surface density expression of the leukocyte-associated Ig-like receptor-1
RT is directly related to inhibition of human T-cell functions.";
RL Hum. Immunol. 63:534-546(2002).
RN [11]
RP MUTAGENESIS OF TYR-251 AND TYR-281.
RX PubMed=14565933; DOI=10.1093/intimm/dxg134;
RA Verbrugge A., de Ruiter T., Clevers H., Meyaard L.;
RT "Differential contribution of the immunoreceptor tyrosine-based inhibitory
RT motifs of human leukocyte-associated Ig-like receptor-1 to inhibitory
RT function and phosphatase recruitment.";
RL Int. Immunol. 15:1349-1358(2003).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=12757266; DOI=10.1023/a:1022580929226;
RA Aoukaty A., Lee I.-F., Wu J., Tan R.;
RT "Chronic active Epstein-Barr virus infection associated with low expression
RT of leukocyte-associated immunoglobulin-like receptor-1 (LAIR-1) on natural
RT killer cells.";
RL J. Clin. Immunol. 23:141-145(2003).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=14604962; DOI=10.1182/blood-2003-07-2375;
RA De Milito A., Nilsson A., Titanji K., Thorstensson R., Reizenstein E.,
RA Narita M., Grutzmeier S., Sonnerborg A., Chiodi F.;
RT "Mechanisms of hypergammaglobulinemia and impaired antigen-specific humoral
RT immunity in HIV-1 infection.";
RL Blood 103:2180-2186(2004).
RN [14]
RP FUNCTION.
RX PubMed=15939744; DOI=10.1128/cdli.12.6.705-712.2005;
RA Merlo A., Tenca C., Fais F., Battini L., Ciccone E., Grossi C.E.,
RA Saverino D.;
RT "Inhibitory receptors CD85j, LAIR-1, and CD152 down-regulate immunoglobulin
RT and cytokine production by human B lymphocytes.";
RL Clin. Diagn. Lab. Immunol. 12:705-712(2005).
RN [15]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15950745; DOI=10.1016/j.molimm.2005.01.004;
RA Maasho K., Masilamani M., Valas R., Basu S., Coligan J.E., Borrego F.;
RT "The inhibitory leukocyte-associated Ig-like receptor-1 (LAIR-1) is
RT expressed at high levels by human naive T cells and inhibits TCR mediated
RT activation.";
RL Mol. Immunol. 42:1521-1530(2005).
RN [16]
RP INTERACTION WITH CSK, MUTAGENESIS OF TYR-251 AND TYR-281, AND FUNCTION.
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).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-122, INTERACTION WITH
RP COLLAGENS, AND DISULFIDE BOND.
RX PubMed=20007810; DOI=10.1182/blood-2009-10-246322;
RA Brondijk T.H., de Ruiter T., Ballering J., Wienk H., Lebbink R.J.,
RA van Ingen H., Boelens R., Farndale R.W., Meyaard L., Huizinga E.G.;
RT "Crystal structure and collagen-binding site of immune inhibitory receptor
RT LAIR-1: unexpected implications for collagen binding by platelet receptor
RT GPVI.";
RL Blood 115:1364-1373(2010).
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. {ECO:0000269|PubMed:10229813, ECO:0000269|PubMed:10764762,
CC ECO:0000269|PubMed:11069054, ECO:0000269|PubMed:11160222,
CC ECO:0000269|PubMed:12072189, ECO:0000269|PubMed:15939744,
CC ECO:0000269|PubMed:15950745, ECO:0000269|PubMed:16380958,
CC ECO:0000269|PubMed:9285412, ECO:0000269|PubMed:9692876}.
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.
CC {ECO:0000269|PubMed:10764762, ECO:0000269|PubMed:11160222,
CC ECO:0000269|PubMed:16380958, ECO:0000269|PubMed:20007810,
CC ECO:0000269|PubMed:9285412}.
CC -!- INTERACTION:
CC Q6GTX8; P29350: PTPN6; NbExp=5; IntAct=EBI-965864, EBI-78260;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10229813,
CC ECO:0000269|PubMed:11160222, ECO:0000269|PubMed:9285412}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:10229813,
CC ECO:0000269|PubMed:11160222, ECO:0000269|PubMed:9285412}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=LAIR-1a;
CC IsoId=Q6GTX8-1; Sequence=Displayed;
CC Name=2; Synonyms=LAIR-1b;
CC IsoId=Q6GTX8-2; Sequence=VSP_020711;
CC Name=3; Synonyms=LAIR-1c;
CC IsoId=Q6GTX8-3; Sequence=VSP_020710, VSP_020711;
CC Name=4; Synonyms=LAIR-1d;
CC IsoId=Q6GTX8-4; Sequence=VSP_020712;
CC -!- TISSUE SPECIFICITY: Expressed on the majority of peripheral mononuclear
CC cells, including natural killer (NK) cells, T-cells, B-cells,
CC monocytes, and dendritic cells. Highly expressed in naive T-cells and
CC B-cells but no expression on germinal center B-cells. Abnormally low
CC expression in naive B-cells from HIV-1 infected patients. Very low
CC expression in NK cells from a patient with chronic active Epstein-Barr
CC virus infection. {ECO:0000269|PubMed:10540327,
CC ECO:0000269|PubMed:12757266, ECO:0000269|PubMed:14604962,
CC ECO:0000269|PubMed:15950745}.
CC -!- DEVELOPMENTAL STAGE: Complete loss of expression when naive B-cells
CC proliferates and differentiates into Ig-producing plasma cells under in
CC vitro stimulation. {ECO:0000269|PubMed:10540327}.
CC -!- INDUCTION: By T-cell receptor stimulation in a process that requires
CC p38 MAP kinase and ERK signaling. {ECO:0000269|PubMed:15950745}.
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:9285412}.
CC -!- PTM: Phosphorylation at Tyr-251 and Tyr-281 activates it. May be
CC phosphorylated by LCK. {ECO:0000269|PubMed:10764762}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19349973,
CC ECO:0000269|PubMed:9285412}.
CC -!- MISCELLANEOUS: [Isoform 2]: Functions as an inhibitory receptor in NK
CC cells and T-cells. {ECO:0000305}.
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DR EMBL; AF013249; AAB69324.1; -; mRNA.
DR EMBL; AF109683; AAF17107.1; -; mRNA.
DR EMBL; AF251509; AAF71274.2; -; mRNA.
DR EMBL; AF251510; AAF71275.2; -; mRNA.
DR EMBL; CR542051; CAG46848.1; -; mRNA.
DR EMBL; BC027899; AAH27899.1; -; mRNA.
DR CCDS; CCDS12891.1; -. [Q6GTX8-1]
DR CCDS; CCDS12892.1; -. [Q6GTX8-2]
DR CCDS; CCDS74448.1; -. [Q6GTX8-3]
DR RefSeq; NP_001275952.2; NM_001289023.2.
DR RefSeq; NP_001275954.2; NM_001289025.2.
DR RefSeq; NP_002278.2; NM_002287.5.
DR RefSeq; NP_068352.2; NM_021706.4.
DR PDB; 3KGR; X-ray; 1.80 A; A/B/C=22-122.
DR PDB; 3RP1; X-ray; 2.60 A; A/B/C/D=22-123.
DR PDB; 7F9L; X-ray; 2.70 A; G/H/I/J/K/L=22-122.
DR PDB; 7F9M; X-ray; 2.90 A; C/D=22-122.
DR PDB; 7F9N; X-ray; 3.00 A; C/D=22-122.
DR PDBsum; 3KGR; -.
DR PDBsum; 3RP1; -.
DR PDBsum; 7F9L; -.
DR PDBsum; 7F9M; -.
DR PDBsum; 7F9N; -.
DR AlphaFoldDB; Q6GTX8; -.
DR SMR; Q6GTX8; -.
DR BioGRID; 110098; 7.
DR IntAct; Q6GTX8; 3.
DR MINT; Q6GTX8; -.
DR STRING; 9606.ENSP00000375622; -.
DR GlyConnect; 1998; 10 N-Linked glycans (1 site).
DR GlyGen; Q6GTX8; 2 sites, 10 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q6GTX8; -.
DR PhosphoSitePlus; Q6GTX8; -.
DR SwissPalm; Q6GTX8; -.
DR BioMuta; LAIR1; -.
DR DMDM; 74736490; -.
DR EPD; Q6GTX8; -.
DR jPOST; Q6GTX8; -.
DR MassIVE; Q6GTX8; -.
DR MaxQB; Q6GTX8; -.
DR PaxDb; Q6GTX8; -.
DR PeptideAtlas; Q6GTX8; -.
DR PRIDE; Q6GTX8; -.
DR ProteomicsDB; 66322; -. [Q6GTX8-1]
DR ProteomicsDB; 66323; -. [Q6GTX8-2]
DR ProteomicsDB; 66324; -. [Q6GTX8-3]
DR ProteomicsDB; 66325; -. [Q6GTX8-4]
DR ABCD; Q6GTX8; 22 sequenced antibodies.
DR Antibodypedia; 2596; 804 antibodies from 37 providers.
DR DNASU; 3903; -.
DR Ensembl; ENST00000348231.8; ENSP00000301193.4; ENSG00000167613.16. [Q6GTX8-2]
DR Ensembl; ENST00000391742.7; ENSP00000375622.2; ENSG00000167613.16. [Q6GTX8-1]
DR Ensembl; ENST00000474878.5; ENSP00000418998.1; ENSG00000167613.16. [Q6GTX8-3]
DR Ensembl; ENST00000610549.4; ENSP00000481204.1; ENSG00000276053.4.
DR Ensembl; ENST00000614937.4; ENSP00000479006.1; ENSG00000278154.4.
DR Ensembl; ENST00000614946.1; ENSP00000478853.1; ENSG00000274110.4.
DR Ensembl; ENST00000616612.4; ENSP00000479682.1; ENSG00000278154.4.
DR Ensembl; ENST00000618434.4; ENSP00000479133.1; ENSG00000274110.4.
DR Ensembl; ENST00000619717.4; ENSP00000479707.1; ENSG00000276053.4.
DR Ensembl; ENST00000619817.4; ENSP00000480619.1; ENSG00000276163.4.
DR Ensembl; ENST00000620077.4; ENSP00000482922.1; ENSG00000276053.4.
DR Ensembl; ENST00000620357.4; ENSP00000479649.1; ENSG00000278154.4.
DR Ensembl; ENST00000620726.1; ENSP00000478405.1; ENSG00000276163.4.
DR Ensembl; ENST00000622097.4; ENSP00000480659.1; ENSG00000274110.4.
DR GeneID; 3903; -.
DR KEGG; hsa:3903; -.
DR MANE-Select; ENST00000391742.7; ENSP00000375622.2; NM_002287.6; NP_002278.2.
DR UCSC; uc032idt.2; human. [Q6GTX8-1]
DR CTD; 3903; -.
DR DisGeNET; 3903; -.
DR GeneCards; LAIR1; -.
DR HGNC; HGNC:6477; LAIR1.
DR HPA; ENSG00000167613; Tissue enhanced (lung, lymphoid tissue).
DR MIM; 602992; gene.
DR neXtProt; NX_Q6GTX8; -.
DR OpenTargets; ENSG00000167613; -.
DR PharmGKB; PA30266; -.
DR VEuPathDB; HostDB:ENSG00000167613; -.
DR eggNOG; ENOG502TBGD; Eukaryota.
DR GeneTree; ENSGT00940000162693; -.
DR HOGENOM; CLU_021100_3_1_1; -.
DR InParanoid; Q6GTX8; -.
DR OrthoDB; 1481318at2759; -.
DR PhylomeDB; Q6GTX8; -.
DR TreeFam; TF336644; -.
DR PathwayCommons; Q6GTX8; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q6GTX8; -.
DR BioGRID-ORCS; 3903; 25 hits in 1067 CRISPR screens.
DR ChiTaRS; LAIR1; human.
DR EvolutionaryTrace; Q6GTX8; -.
DR GeneWiki; LAIR1; -.
DR GenomeRNAi; 3903; -.
DR Pharos; Q6GTX8; Tbio.
DR PRO; PR:Q6GTX8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6GTX8; protein.
DR Bgee; ENSG00000167613; Expressed in granulocyte and 99 other tissues.
DR ExpressionAtlas; Q6GTX8; baseline and differential.
DR Genevisible; Q6GTX8; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
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 InterPro; IPR003599; Ig_sub.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..287
FT /note="Leukocyte-associated immunoglobulin-like receptor 1"
FT /id="PRO_0000250682"
FT TOPO_DOM 22..165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..117
FT /note="Ig-like C2-type"
FT REGION 121..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 249..254
FT /note="ITIM motif 1"
FT MOTIF 279..284
FT /note="ITIM motif 2"
FT COMPBIAS 129..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 251
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10764762"
FT MOD_RES 281
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10764762"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 49..101
FT /evidence="ECO:0000269|PubMed:20007810"
FT VAR_SEQ 23
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10764762"
FT /id="VSP_020710"
FT VAR_SEQ 122..138
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10229813,
FT ECO:0000303|PubMed:10764762"
FT /id="VSP_020711"
FT VAR_SEQ 210..287
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10764762"
FT /id="VSP_020712"
FT VARIANT 63
FT /note="D -> E (in dbSNP:rs3745442)"
FT /evidence="ECO:0000269|PubMed:10229813,
FT ECO:0000269|PubMed:10764762, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9285412"
FT /id="VAR_027598"
FT VARIANT 92
FT /note="R -> S (in dbSNP:rs118056835)"
FT /evidence="ECO:0000269|PubMed:10229813,
FT ECO:0000269|PubMed:10764762, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9285412"
FT /id="VAR_085777"
FT VARIANT 98
FT /note="L -> P (in dbSNP:rs79046875)"
FT /evidence="ECO:0000269|PubMed:10229813,
FT ECO:0000269|PubMed:10764762, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9285412"
FT /id="VAR_085778"
FT VARIANT 123
FT /note="S -> T (in dbSNP:rs190462445)"
FT /evidence="ECO:0000269|PubMed:10764762,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9285412"
FT /id="VAR_085779"
FT MUTAGEN 251
FT /note="Y->F: Reduced tyrosine phosphorylation and loss of
FT binding to PTPN6 and CSK as well as complete loss of
FT inhibitory activity. Loss of phosphorylation and of
FT inhibition of calcium mobilization; when associated with F-
FT 281."
FT /evidence="ECO:0000269|PubMed:10764762,
FT ECO:0000269|PubMed:14565933, ECO:0000269|PubMed:16380958"
FT MUTAGEN 281
FT /note="Y->F: Reduced tyrosine phosphorylation and loss of
FT binding to PTPN6. Partial inhibition of cytotoxic
FT activity."
FT /evidence="ECO:0000269|PubMed:10764762,
FT ECO:0000269|PubMed:14565933, ECO:0000269|PubMed:16380958"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3KGR"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:3KGR"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:3KGR"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:3KGR"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3KGR"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:3KGR"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3KGR"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:3KGR"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3KGR"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:3KGR"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:3KGR"
SQ SEQUENCE 287 AA; 31469 MW; E2A921D84F426B35 CRC64;
MSPHPTALLG LVLCLAQTIH TQEEDLPRPS ISAEPGTVIP LGSHVTFVCR GPVGVQTFRL
ERDSRSTYND TEDVSQASPS ESEARFRIDS VREGNAGLYR CIYYKPPKWS EQSDYLELLV
KESSGGPDSP DTEPGSSAGP TQRPSDNSHN EHAPASQGLK AEHLYILIGV SVVFLFCLLL
LVLFCLHRQN QIKQGPPRSK DEEQKPQQRP DLAVDVLERT ADKATVNGLP EKDRETDTSA
LAAGSSQEVT YAQLDHWALT QRTARAVSPQ STKPMAESIT YAAVARH
