LY86_HUMAN
ID LY86_HUMAN Reviewed; 162 AA.
AC O95711; Q9UQC4;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Lymphocyte antigen 86;
DE Short=Ly-86;
DE AltName: Full=Protein MD-1;
DE Flags: Precursor;
GN Name=LY86; Synonyms=MD1;
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].
RC TISSUE=Fetal liver, and Spleen;
RX PubMed=9763566;
RA Miura Y., Shimazu R., Miyake K., Akashi S., Ogata H., Yamashita Y.,
RA Narisawa Y., Kimoto M.;
RT "RP105 is associated with MD-1 and transmits an activation signal in human
RT B cells.";
RL Blood 92:2815-2822(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-162.
RC TISSUE=Monocyte;
RX PubMed=10079183; DOI=10.1006/bbrc.1999.0329;
RA Begum N.A., Tsuji S., Nomura M., Shida K., Azuma I., Hayashi A.,
RA Matsumoto M., Seya T., Toyoshima K.;
RT "Human MD-1 homologue is a BCG-regulated gene product in monocytes: Its
RT identification by differential display.";
RL Biochem. Biophys. Res. Commun. 256:325-329(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [5]
RP PROTEIN SEQUENCE OF 21-35.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 21-162 IN COMPLEX WITH CD180,
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=21959264; DOI=10.1016/j.jmb.2011.09.020;
RA Ohto U., Miyake K., Shimizu T.;
RT "Crystal structures of mouse and human RP105/MD-1 complexes reveal unique
RT dimer organization of the toll-like receptor family.";
RL J. Mol. Biol. 413:815-825(2011).
CC -!- FUNCTION: May cooperate with CD180 and TLR4 to mediate the innate
CC immune response to bacterial lipopolysaccharide (LPS) and cytokine
CC production. Important for efficient CD180 cell surface expression (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: M-shaped tetramer of two CD180-LY86 heterodimers.
CC {ECO:0000269|PubMed:21959264}.
CC -!- INTERACTION:
CC O95711; Q99467: CD180; NbExp=3; IntAct=EBI-12203791, EBI-15940363;
CC O95711; P57678: GEMIN4; NbExp=3; IntAct=EBI-12203791, EBI-356700;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. Note=Associated
CC with CD180 at the cell surface.
CC -!- TISSUE SPECIFICITY: Highly expressed in B-cells, monocytes and tonsil.
CC -!- INDUCTION: In monocytes, down-regulated by the cell-wall fraction of
CC Mycobacterium bovis (BCG-CWS).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76410.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF057178; AAC98152.2; -; mRNA.
DR EMBL; AB020499; BAA76410.1; ALT_INIT; mRNA.
DR EMBL; AL031123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038846; AAH38846.1; -; mRNA.
DR CCDS; CCDS4498.1; -.
DR RefSeq; NP_004262.1; NM_004271.3.
DR PDB; 3B2D; X-ray; 2.80 A; C/D=21-162.
DR PDBsum; 3B2D; -.
DR AlphaFoldDB; O95711; -.
DR SMR; O95711; -.
DR BioGRID; 114839; 245.
DR DIP; DIP-59105N; -.
DR IntAct; O95711; 3.
DR STRING; 9606.ENSP00000369286; -.
DR GlyConnect; 1473; 1 N-Linked glycan (1 site).
DR GlyGen; O95711; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; O95711; -.
DR PhosphoSitePlus; O95711; -.
DR BioMuta; LY86; -.
DR MassIVE; O95711; -.
DR PaxDb; O95711; -.
DR PeptideAtlas; O95711; -.
DR PRIDE; O95711; -.
DR ProteomicsDB; 51007; -.
DR Antibodypedia; 9679; 402 antibodies from 33 providers.
DR DNASU; 9450; -.
DR Ensembl; ENST00000230568.5; ENSP00000230568.3; ENSG00000112799.9.
DR Ensembl; ENST00000379953.6; ENSP00000369286.1; ENSG00000112799.9.
DR GeneID; 9450; -.
DR KEGG; hsa:9450; -.
DR MANE-Select; ENST00000230568.5; ENSP00000230568.3; NM_004271.4; NP_004262.1.
DR UCSC; uc003mwy.2; human.
DR CTD; 9450; -.
DR DisGeNET; 9450; -.
DR GeneCards; LY86; -.
DR HGNC; HGNC:16837; LY86.
DR HPA; ENSG00000112799; Tissue enhanced (lymphoid).
DR MIM; 605241; gene.
DR neXtProt; NX_O95711; -.
DR OpenTargets; ENSG00000112799; -.
DR PharmGKB; PA128394549; -.
DR VEuPathDB; HostDB:ENSG00000112799; -.
DR eggNOG; ENOG502S63U; Eukaryota.
DR GeneTree; ENSGT00390000018605; -.
DR HOGENOM; CLU_145135_0_0_1; -.
DR InParanoid; O95711; -.
DR OMA; QPKFSFC; -.
DR OrthoDB; 1548356at2759; -.
DR PhylomeDB; O95711; -.
DR TreeFam; TF335876; -.
DR PathwayCommons; O95711; -.
DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR SignaLink; O95711; -.
DR BioGRID-ORCS; 9450; 10 hits in 1065 CRISPR screens.
DR ChiTaRS; LY86; human.
DR GenomeRNAi; 9450; -.
DR Pharos; O95711; Tbio.
DR PRO; PR:O95711; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O95711; protein.
DR Bgee; ENSG00000112799; Expressed in monocyte and 156 other tissues.
DR Genevisible; O95711; HS.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IGI:MGI.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR039945; LY86.
DR InterPro; IPR003172; ML_dom.
DR PANTHER; PTHR20838; PTHR20838; 1.
DR SMART; SM00737; ML; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunity; Inflammatory response; Innate immunity; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 21..162
FT /note="Lymphocyte antigen 86"
FT /id="PRO_0000018614"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..58
FT /evidence="ECO:0000269|PubMed:21959264"
FT DISULFID 45..154
FT /evidence="ECO:0000269|PubMed:21959264"
FT DISULFID 102..112
FT /evidence="ECO:0000269|PubMed:21959264"
FT VARIANT 93
FT /note="S -> P (in dbSNP:rs5743649)"
FT /id="VAR_024531"
FT VARIANT 121
FT /note="Y -> C (in dbSNP:rs5743651)"
FT /id="VAR_050029"
FT VARIANT 160
FT /note="M -> V (in dbSNP:rs1802323)"
FT /id="VAR_014539"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 79..89
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 92..102
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 135..145
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 151..161
FT /evidence="ECO:0007829|PDB:3B2D"
SQ SEQUENCE 162 AA; 17906 MW; 3E6497E2DB4C6F27 CRC64;
MKGFTATLFL WTLIFPSCSG GGGGKAWPTH VVCSDSGLEV LYQSCDPLQD FGFSVEKCSK
QLKSNINIRF GIILREDIKE LFLDLALMSQ GSSVLNFSYP ICEAALPKFS FCGRRKGEQI
YYAGPVNNPE FTIPQGEYQV LLELYTEKRS TVACANATIM CS
