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   13-FEB-2019, entry version 130.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   human 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:
RT   Its 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.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   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.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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
RT   project: 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
RT   verified 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
RT   unique 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
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: M-shaped tetramer of two CD180-LY86 heterodimers.
CC       {ECO:0000269|PubMed:21959264}.
CC   -!- INTERACTION:
CC       Q99467:CD180; NbExp=3; IntAct=EBI-12203791, EBI-15940363;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC       Note=Associated with CD180 at the cell surface.
CC   -!- TISSUE SPECIFICITY: Highly expressed in B-cells, monocytes and
CC       tonsil.
CC   -!- INDUCTION: In monocytes, down-regulated by the cell-wall fraction
CC       of 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   UniGene; Hs.653138; -.
DR   PDB; 3B2D; X-ray; 2.80 A; C/D=21-162.
DR   PDBsum; 3B2D; -.
DR   ProteinModelPortal; O95711; -.
DR   SMR; O95711; -.
DR   BioGrid; 114839; 63.
DR   DIP; DIP-59105N; -.
DR   IntAct; O95711; 3.
DR   STRING; 9606.ENSP00000230568; -.
DR   GlyConnect; 1473; -.
DR   iPTMnet; O95711; -.
DR   PhosphoSitePlus; O95711; -.
DR   BioMuta; LY86; -.
DR   PaxDb; O95711; -.
DR   PeptideAtlas; O95711; -.
DR   PRIDE; O95711; -.
DR   ProteomicsDB; 51007; -.
DR   DNASU; 9450; -.
DR   Ensembl; ENST00000230568; ENSP00000230568; ENSG00000112799.
DR   Ensembl; ENST00000379953; ENSP00000369286; ENSG00000112799.
DR   GeneID; 9450; -.
DR   KEGG; hsa:9450; -.
DR   UCSC; uc003mwy.2; human.
DR   CTD; 9450; -.
DR   DisGeNET; 9450; -.
DR   EuPathDB; HostDB:ENSG00000112799.8; -.
DR   GeneCards; LY86; -.
DR   HGNC; HGNC:16837; LY86.
DR   HPA; CAB025000; -.
DR   HPA; HPA044895; -.
DR   MIM; 605241; gene.
DR   neXtProt; NX_O95711; -.
DR   OpenTargets; ENSG00000112799; -.
DR   PharmGKB; PA128394549; -.
DR   eggNOG; ENOG410IWHW; Eukaryota.
DR   eggNOG; ENOG410YWD5; LUCA.
DR   GeneTree; ENSGT00390000018605; -.
DR   HOGENOM; HOG000261640; -.
DR   HOVERGEN; HBG019056; -.
DR   InParanoid; O95711; -.
DR   OMA; WPTHTAC; -.
DR   OrthoDB; 1548356at2759; -.
DR   PhylomeDB; O95711; -.
DR   TreeFam; TF335876; -.
DR   Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR   GenomeRNAi; 9450; -.
DR   PRO; PR:O95711; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000112799; Expressed in 182 organ(s), highest expression level in leukocyte.
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; IEA:UniProtKB-KW.
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   Pfam; PF02221; E1_DerP2_DerF2; 1.
DR   SMART; SM00737; ML; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Immunity; Inflammatory response;
KW   Innate immunity; Polymorphism; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     20       {ECO:0000269|PubMed:15340161}.
FT   CHAIN        21    162       Lymphocyte antigen 86.
FT                                /FTId=PRO_0000018614.
FT   CARBOHYD     96     96       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    156    156       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     33     58       {ECO:0000269|PubMed:21959264}.
FT   DISULFID     45    154       {ECO:0000269|PubMed:21959264}.
FT   DISULFID    102    112       {ECO:0000269|PubMed:21959264}.
FT   VARIANT      93     93       S -> P (in dbSNP:rs5743649).
FT                                /FTId=VAR_024531.
FT   VARIANT     121    121       Y -> C (in dbSNP:rs5743651).
FT                                /FTId=VAR_050029.
FT   VARIANT     160    160       M -> V (in dbSNP:rs1802323).
FT                                /FTId=VAR_014539.
FT   STRAND       30     33       {ECO:0000244|PDB:3B2D}.
FT   STRAND       35     37       {ECO:0000244|PDB:3B2D}.
FT   STRAND       39     44       {ECO:0000244|PDB:3B2D}.
FT   STRAND       52     57       {ECO:0000244|PDB:3B2D}.
FT   STRAND       67     73       {ECO:0000244|PDB:3B2D}.
FT   STRAND       79     89       {ECO:0000244|PDB:3B2D}.
FT   STRAND       92    102       {ECO:0000244|PDB:3B2D}.
FT   TURN        110    113       {ECO:0000244|PDB:3B2D}.
FT   STRAND      119    125       {ECO:0000244|PDB:3B2D}.
FT   STRAND      135    145       {ECO:0000244|PDB:3B2D}.
FT   STRAND      151    161       {ECO:0000244|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
//