ID   LY86_CHICK              Reviewed;         160 AA.
AC   Q90890;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
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   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=1718743; DOI=10.1002/j.1460-2075.1991.tb04939.x;
RA   Burk O., Klempnauer K.-H.;
RT   "Estrogen-dependent alterations in differentiation state of myeloid cells
RT   caused by a v-myb/estrogen receptor fusion protein.";
RL   EMBO J. 10:3713-3719(1991).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-160 IN COMPLEX WITH LPS
RP   PRECURSOR, AND DISULFIDE BONDS.
RX   PubMed=20534476; DOI=10.1073/pnas.1004153107;
RA   Yoon S.I., Hong M., Han G.W., Wilson I.A.;
RT   "Crystal structure of soluble MD-1 and its interaction with lipid IVa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:10990-10995(2010).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC       Note=Associated with CD180 at the cell surface. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in the macrophage-like 10.4 cells.
CC   -!- INDUCTION: By myb.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X60450; CAA42980.1; -; mRNA.
DR   PIR; S18633; S18633.
DR   RefSeq; NP_001004399.1; NM_001004399.1.
DR   PDB; 3MTX; X-ray; 2.00 A; A/B=21-160.
DR   PDB; 3MU3; X-ray; 2.40 A; A/B=21-160.
DR   PDBsum; 3MTX; -.
DR   PDBsum; 3MU3; -.
DR   AlphaFoldDB; Q90890; -.
DR   SMR; Q90890; -.
DR   STRING; 9031.ENSGALP00000020856; -.
DR   PaxDb; Q90890; -.
DR   GeneID; 420872; -.
DR   KEGG; gga:420872; -.
DR   CTD; 9450; -.
DR   VEuPathDB; HostDB:geneid_420872; -.
DR   eggNOG; ENOG502S63U; Eukaryota.
DR   InParanoid; Q90890; -.
DR   OrthoDB; 1548356at2759; -.
DR   PhylomeDB; Q90890; -.
DR   EvolutionaryTrace; Q90890; -.
DR   PRO; PR:Q90890; -.
DR   Proteomes; UP000000539; Unplaced.
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:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IBA:GO_Central.
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; Disulfide bond; Immunity; Inflammatory response;
KW   Innate immunity; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..160
FT                   /note="Lymphocyte antigen 86"
FT                   /id="PRO_0000018616"
FT   DISULFID        28..53
FT                   /evidence="ECO:0000269|PubMed:20534476"
FT   DISULFID        40..149
FT                   /evidence="ECO:0000269|PubMed:20534476"
FT   DISULFID        97..107
FT                   /evidence="ECO:0000269|PubMed:20534476"
FT   STRAND          25..30
FT                   /evidence="ECO:0007829|PDB:3MTX"
FT   STRAND          33..39
FT                   /evidence="ECO:0007829|PDB:3MTX"
FT   STRAND          47..51
FT                   /evidence="ECO:0007829|PDB:3MTX"
FT   HELIX           53..58
FT                   /evidence="ECO:0007829|PDB:3MTX"
FT   STRAND          60..68
FT                   /evidence="ECO:0007829|PDB:3MTX"
FT   STRAND          74..84
FT                   /evidence="ECO:0007829|PDB:3MTX"
FT   STRAND          87..98
FT                   /evidence="ECO:0007829|PDB:3MTX"
FT   TURN            105..108
FT                   /evidence="ECO:0007829|PDB:3MTX"
FT   STRAND          114..122
FT                   /evidence="ECO:0007829|PDB:3MTX"
FT   STRAND          124..127
FT                   /evidence="ECO:0007829|PDB:3MU3"
FT   STRAND          131..141
FT                   /evidence="ECO:0007829|PDB:3MTX"
FT   STRAND          146..156
FT                   /evidence="ECO:0007829|PDB:3MTX"
SQ   SEQUENCE   160 AA;  18114 MW;  6E3345141E33C007 CRC64;
     MKTLNVLALV LVLLCINAST EWPTHTVCKE ENLEIYYKSC DPQQDFAFSI DRCSDVTTHT
     FDIRAAMVLR QSIKELYAKV DLIINGKTVL SYSETLCGPG LSKLIFCGKK KGEHLYYEGP
     ITLGIKEIPQ RDYTITARLT NEDRATVACA DFTVKNYLDY