CD14_BOVIN
ID CD14_BOVIN Reviewed; 373 AA.
AC Q95122; A8DBS7; Q9TVA7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Monocyte differentiation antigen CD14;
DE AltName: Full=Myeloid cell-specific leucine-rich glycoprotein;
DE AltName: CD_antigen=CD14;
DE Flags: Precursor;
GN Name=CD14;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION BY
RP BACTERIAL LIPOPOLYSACCHARIDE.
RC STRAIN=Holstein;
RX PubMed=9300371; DOI=10.1292/jvms.59.715;
RA Ikeda A., Takata M., Taniguchi T., Sekikawa K.;
RT "Molecular cloning of bovine CD14 gene.";
RL J. Vet. Med. Sci. 59:715-719(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein-Friesian;
RA Filipp D., Julius M.J.;
RT "Cloning of cDNA for bovine CD14.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ibeagha-Awemu E.M., Lee J.-W., Ibeagha A.E., Zhao X.;
RT "Genetic mutations in the CD14 gene of cattle and relationship with the
RT percentage of surface CD14-bound monocytes and neutrophils in healthy dairy
RT cows.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 179-278, AND TISSUE SPECIFICITY.
RX PubMed=8643545; DOI=10.1073/pnas.93.10.5156;
RA Diamond G., Russell J.P., Bevins C.L.;
RT "Inducible expression of an antibiotic peptide gene in lipopolysaccharide-
RT challenged tracheal epithelial cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5156-5160(1996).
CC -!- FUNCTION: Coreceptor for bacterial lipopolysaccharide. In concert with
CC LBP, binds to monomeric lipopolysaccharide and delivers it to the
CC LY96/TLR4 complex, thereby mediating the innate immune response to
CC bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6,
CC leading to NF-kappa-B activation, cytokine secretion and the
CC inflammatory response. Acts as a coreceptor for TLR2:TLR6 heterodimer
CC in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in
CC response to triacylated lipopeptides, these clusters trigger signaling
CC from the cell surface and subsequently are targeted to the Golgi in a
CC lipid-raft dependent pathway. Binds electronegative LDL (LDL(-)) and
CC mediates the cytokine release induced by LDL(-) (By similarity).
CC {ECO:0000250|UniProtKB:P08571, ECO:0000250|UniProtKB:P10810}.
CC -!- SUBUNIT: Belongs to the lipopolysaccharide (LPS) receptor, a multi-
CC protein complex containing at least CD14, LY96 and TLR4. Interacts with
CC LPS-bound LPB. Interacts with LPAR1. Interacts with the TLR2:TLR6 or
CC TLR2:TLR1 heterodimers; upon interaction with ligands such as
CC diacylated lipopeptides and triacylated lipopeptides, respectively.
CC Interacts with MYO18A. Interacts with FSTL1.
CC {ECO:0000250|UniProtKB:P08571, ECO:0000250|UniProtKB:P10810}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08571};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P08571}. Secreted
CC {ECO:0000250|UniProtKB:P08571}. Membrane raft
CC {ECO:0000250|UniProtKB:P08571}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P08571}. Note=Soluble, secreted forms seem to
CC exist. They may arise by cleavage of the GPI anchor.
CC {ECO:0000250|UniProtKB:P08571}.
CC -!- TISSUE SPECIFICITY: Detected in lung (PubMed:9300371, PubMed:8643545).
CC Detected in brain and kidney (PubMed:9300371). Detected in trachea and
CC bone marrow (PubMed:8643545). {ECO:0000269|PubMed:8643545,
CC ECO:0000269|PubMed:9300371}.
CC -!- INDUCTION: Up-regulated in peripheral blood monocytes exposed to
CC bacterial lipopolysaccharide (LPS). {ECO:0000269|PubMed:9300371}.
CC -!- DOMAIN: The C-terminal leucine-rich repeat (LRR) region is required for
CC responses to smooth LPS. {ECO:0000250|UniProtKB:P10810}.
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; D84509; BAA21517.1; -; Genomic_DNA.
DR EMBL; AF141313; AAD32215.1; -; mRNA.
DR EMBL; EU148609; ABV68569.1; -; Genomic_DNA.
DR EMBL; EU148610; ABV68570.1; -; Genomic_DNA.
DR EMBL; U48356; AAB07861.1; -; mRNA.
DR RefSeq; NP_776433.1; NM_174008.1.
DR AlphaFoldDB; Q95122; -.
DR SMR; Q95122; -.
DR STRING; 9913.ENSBTAP00000020009; -.
DR PaxDb; Q95122; -.
DR PeptideAtlas; Q95122; -.
DR PRIDE; Q95122; -.
DR GeneID; 281048; -.
DR KEGG; bta:281048; -.
DR CTD; 929; -.
DR eggNOG; ENOG502SNYQ; Eukaryota.
DR InParanoid; Q95122; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0046696; C:lipopolysaccharide receptor complex; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0001530; F:lipopolysaccharide binding; IBA:GO_Central.
DR GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; ISS:UniProtKB.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR016337; Monocyte_diff_Ag_CD14.
DR PANTHER; PTHR10630; PTHR10630; 1.
DR Pfam; PF13516; LRR_6; 1.
DR PIRSF; PIRSF002017; CD14; 1.
DR PROSITE; PS51450; LRR; 3.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Golgi apparatus; GPI-anchor;
KW Immunity; Inflammatory response; Innate immunity; Leucine-rich repeat;
KW Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..373
FT /note="Monocyte differentiation antigen CD14"
FT /id="PRO_0000020883"
FT REPEAT 55..81
FT /note="LRR 1"
FT REPEAT 82..117
FT /note="LRR 2"
FT REPEAT 118..143
FT /note="LRR 3"
FT REPEAT 144..171
FT /note="LRR 4"
FT REPEAT 172..195
FT /note="LRR 5"
FT REPEAT 196..223
FT /note="LRR 6"
FT REPEAT 224..250
FT /note="LRR 7"
FT REPEAT 251..276
FT /note="LRR 8"
FT REPEAT 277..297
FT /note="LRR 9"
FT REPEAT 298..319
FT /note="LRR 10"
FT REPEAT 320..347
FT /note="LRR 11"
FT REGION 288..373
FT /note="Required for response to bacterial
FT lipopolysaccharide (LPS)"
FT /evidence="ECO:0000250|UniProtKB:P10810"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..37
FT /evidence="ECO:0000250|UniProtKB:P08571"
FT DISULFID 35..52
FT /evidence="ECO:0000250|UniProtKB:P08571"
FT DISULFID 186..216
FT /evidence="ECO:0000250|UniProtKB:P08571"
FT DISULFID 240..270
FT /evidence="ECO:0000250|UniProtKB:P08571"
FT CONFLICT 209
FT /note="S -> T (in Ref. 2; AAD32215)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 39667 MW; B9E9C2C51BE82227 CRC64;
MVCVPYLLLL LLPSLLRVSA DTTEPCELDD DDFRCVCNFT DPKPDWSSAV QCMVAVEVEI
SAGGRSLEQF LKGADTNPKQ YADTIKALRV RRLKLGAAQV PAQLLVAVLR ALGYSRLKEL
TLEDLEVTGP TPPTPLEAAG PALTTLSLRN VSWTTGGAWL GELQQWLKPG LRVLNIAQAH
SLAFPCAGLS TFEALTTLDL SDNPSLGDSG LMAALCPNKF PALQYLALRN AGMETPSGVC
AALAAARVQP QSLDLSHNSL RVTAPGATRC VWPSALRSLN LSFAGLEQVP KGLPPKLSVL
DLSCNKLSRE PRRDELPEVN DLTLDGNPFL DPGALQHQND PMISGVVPAC ARSALTMGVS
GALALLQGAR GFA
