LY86_MOUSE
ID LY86_MOUSE Reviewed; 162 AA.
AC O88188; Q4VAF1; Q5D046;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
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 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], AND PROTEIN SEQUENCE OF 20-44.
RC TISSUE=B-cell;
RX PubMed=9686597;
RA Miyake K., Shimazu R., Kondo J., Niki T., Akashi S., Ogata H.,
RA Yamashita Y., Miura Y., Kimoto M.;
RT "Mouse MD-1, a molecule that is physically associated with RP105 and
RT positively regulates its expression.";
RL J. Immunol. 161:1348-1353(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [5]
RP FUNCTION.
RX PubMed=10925274; DOI=10.4049/jimmunol.165.4.1925;
RA Gorczynski R.M., Chen Z., Clark D.A., Hu J., Yu G., Li X., Tsang W.,
RA Hadidi S.;
RT "Regulation of gene expression of murine MD-1 regulates subsequent T cell
RT activation and cytokine production.";
RL J. Immunol. 165:1925-1932(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH PHOSPHOLIPID,
RP SUBUNIT, GLYCOSYLATION AT ASN-96 AND ASN-156, AND DISULFIDE BONDS.
RX PubMed=20595044; DOI=10.1016/j.jmb.2010.05.063;
RA Harada H., Ohto U., Satow Y.;
RT "Crystal structure of mouse MD-1 with endogenous phospholipid bound in its
RT cavity.";
RL J. Mol. Biol. 400:838-846(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 20-162 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.
CC {ECO:0000269|PubMed:10925274}.
CC -!- SUBUNIT: M-shaped tetramer of two CD180-LY86 heterodimers.
CC {ECO:0000269|PubMed:20595044, ECO:0000269|PubMed:21959264}.
CC -!- INTERACTION:
CC O88188; Q62192: Cd180; NbExp=5; IntAct=EBI-79494, EBI-79487;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. Note=Associated
CC with CD180 at the cell surface.
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen, liver, brain and
CC thymus, and at lower levels in kidney.
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DR EMBL; AB007599; BAA32399.1; -; mRNA.
DR EMBL; AK027929; BAC25670.1; -; mRNA.
DR EMBL; CH466546; EDL40921.1; -; Genomic_DNA.
DR EMBL; BC065783; AAH65783.1; -; mRNA.
DR EMBL; BC096414; AAH96414.1; -; mRNA.
DR CCDS; CCDS26457.1; -.
DR RefSeq; NP_034875.1; NM_010745.2.
DR PDB; 3M7O; X-ray; 1.65 A; A/B/C/D=1-162.
DR PDB; 3T6Q; X-ray; 1.90 A; C/D=20-162.
DR PDBsum; 3M7O; -.
DR PDBsum; 3T6Q; -.
DR AlphaFoldDB; O88188; -.
DR SMR; O88188; -.
DR DIP; DIP-30960N; -.
DR IntAct; O88188; 1.
DR STRING; 10090.ENSMUSP00000021860; -.
DR GlyGen; O88188; 2 sites.
DR iPTMnet; O88188; -.
DR PhosphoSitePlus; O88188; -.
DR MaxQB; O88188; -.
DR PaxDb; O88188; -.
DR PeptideAtlas; O88188; -.
DR PRIDE; O88188; -.
DR ProteomicsDB; 295734; -.
DR Antibodypedia; 9679; 402 antibodies from 33 providers.
DR DNASU; 17084; -.
DR Ensembl; ENSMUST00000021860; ENSMUSP00000021860; ENSMUSG00000021423.
DR GeneID; 17084; -.
DR KEGG; mmu:17084; -.
DR UCSC; uc007qcr.2; mouse.
DR CTD; 9450; -.
DR MGI; MGI:1321404; Ly86.
DR VEuPathDB; HostDB:ENSMUSG00000021423; -.
DR eggNOG; ENOG502S63U; Eukaryota.
DR GeneTree; ENSGT00390000018605; -.
DR HOGENOM; CLU_145135_0_0_1; -.
DR InParanoid; O88188; -.
DR OMA; QPKFSFC; -.
DR OrthoDB; 1548356at2759; -.
DR PhylomeDB; O88188; -.
DR TreeFam; TF335876; -.
DR Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR BioGRID-ORCS; 17084; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Ly86; mouse.
DR EvolutionaryTrace; O88188; -.
DR PRO; PR:O88188; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; O88188; protein.
DR Bgee; ENSMUSG00000021423; Expressed in mesenteric lymph node and 180 other tissues.
DR Genevisible; O88188; MM.
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; IDA:MGI.
DR GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IDA: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..19
FT /evidence="ECO:0000269|PubMed:9686597"
FT CHAIN 20..162
FT /note="Lymphocyte antigen 86"
FT /id="PRO_0000018615"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20595044"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20595044"
FT DISULFID 33..58
FT DISULFID 45..154
FT DISULFID 102..112
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3M7O"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:3M7O"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:3M7O"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3M7O"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:3M7O"
FT STRAND 79..89
FT /evidence="ECO:0007829|PDB:3M7O"
FT STRAND 92..103
FT /evidence="ECO:0007829|PDB:3M7O"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:3M7O"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3M7O"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:3M7O"
FT STRAND 135..146
FT /evidence="ECO:0007829|PDB:3M7O"
FT STRAND 151..161
FT /evidence="ECO:0007829|PDB:3M7O"
SQ SEQUENCE 162 AA; 17811 MW; EED25DEA64A9372E CRC64;
MNGVAAALLV WILTSPSSSD HGSENGWPKH TACNSGGLEV VYQSCDPLQD FGLSIDQCSK
QIQSNLNIRF GIILRQDIRK LFLDITLMAK GSSILNYSYP LCEEDQPKFS FCGRRKGEQI
YYAGPVNNPG LDVPQGEYQL LLELYNENRA TVACANATVT SS
