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Monocyte differentiation antigen CD14 (Myeloid cell-specific leucine-rich glycoprotein) (CD antigen CD14)

 CD14_MOUSE              Reviewed;         366 AA.
P10810;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
07-JUN-2017, entry version 166.
RecName: Full=Monocyte differentiation antigen CD14;
AltName: Full=Myeloid cell-specific leucine-rich glycoprotein;
AltName: CD_antigen=CD14;
Flags: Precursor;
Name=Cd14;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=2467257; DOI=10.1093/nar/17.5.2132;
Miyazaki Y., Setoguchi M., Yoshida S., Higuchi Y., Akizuki S.,
Yamamoto S.;
"Nucleotide and amino acid sequences of the mouse CD14 gene.";
Nucleic Acids Res. 17:2132-2132(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ICR; TISSUE=Macrophage;
PubMed=2472171; DOI=10.1016/0167-4781(80)90012-3;
Setoguchi M., Nasu N., Yoshida S., Higuchi Y., Akizuki S.,
Yamamoto S.;
"Mouse and human CD14 (myeloid cell-specific leucine-rich
glycoprotein) primary structure deduced from cDNA clones.";
Biochim. Biophys. Acta 1008:213-222(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1694207;
Ferrero E., Hsieh C.L., Francke U., Goyert S.M.;
"CD14 is a member of the family of leucine-rich proteins and is
encoded by a gene syntenic with multiple receptor genes.";
J. Immunol. 145:331-336(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NMRI; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8612135; DOI=10.1016/S1074-7613(00)80254-X;
Haziot A., Ferrero E., Kontgen F., Hijiya N., Yamamoto S., Silver J.,
Stewart C.L., Goyert S.M.;
"Resistance to endotoxin shock and reduced dissemination of gram-
negative bacteria in CD14-deficient mice.";
Immunity 4:407-414(1996).
[6]
FUNCTION.
PubMed=16148141; DOI=10.4049/jimmunol.175.6.3940;
Gangloff S.C., Zahringer U., Blondin C., Guenounou M., Silver J.,
Goyert S.M.;
"Influence of CD14 on ligand interactions between lipopolysaccharide
and its receptor complex.";
J. Immunol. 175:3940-3945(2005).
[7]
FUNCTION, AND DOMAIN.
PubMed=15895089; DOI=10.1038/ni1207;
Jiang Z., Georgel P., Du X., Shamel L., Sovath S., Mudd S., Huber M.,
Kalis C., Keck S., Galanos C., Freudenberg M., Beutler B.;
"CD14 is required for MyD88-independent LPS signaling.";
Nat. Immunol. 6:565-570(2005).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Macrophage;
PubMed=19362712; DOI=10.1016/j.cellimm.2009.03.008;
Drage M.G., Pecora N.D., Hise A.G., Febbraio M., Silverstein R.L.,
Golenbock D.T., Boom W.H., Harding C.V.;
"TLR2 and its co-receptors determine responses of macrophages and
dendritic cells to lipoproteins of Mycobacterium tuberculosis.";
Cell. Immunol. 258:29-37(2009).
[9]
FUNCTION, INTERACTION WITH LPAR1, AND SUBCELLULAR LOCATION.
PubMed=21821728; DOI=10.1152/ajplung.00058.2011;
Zhao J., He D., Su Y., Berdyshev E., Chun J., Natarajan V., Zhao Y.;
"Lysophosphatidic acid receptor 1 modulates lipopolysaccharide-induced
inflammation in alveolar epithelial cells and murine lungs.";
Am. J. Physiol. 301:L547-L556(2011).
[10]
FUNCTION.
PubMed=24380872; DOI=10.1093/intimm/dxt071;
Tanimura N., Saitoh S., Ohto U., Akashi-Takamura S., Fujimoto Y.,
Fukase K., Shimizu T., Miyake K.;
"The attenuated inflammation of MPL is due to the lack of CD14-
dependent tight dimerization of the TLR4/MD2 complex at the plasma
membrane.";
Int. Immunol. 26:307-314(2014).
[11]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-329, DISULFIDE BONDS,
GLYCOSYLATION AT ASN-147; ASN-180 AND ASN-276, AND DOMAINS
LEUCINE-RICH REPEATS.
PubMed=15644310; DOI=10.1074/jbc.M414607200;
Kim J.I., Lee C.J., Jin M.S., Lee C.H., Paik S.G., Lee H., Lee J.O.;
"Crystal structure of CD14 and its implications for lipopolysaccharide
signaling.";
J. Biol. Chem. 280:11347-11351(2005).
-!- FUNCTION: Coreceptor for bacterial lipopolysaccharide. In concert
with LBP, binds to monomeric lipopolysaccharide and delivers it to
the LY96/TLR4 complex, thereby mediating the innate immune
response to bacterial lipopolysaccharide (LPS) (PubMed:16148141).
Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation,
cytokine secretion and the inflammatory response (PubMed:8612135,
PubMed:15895089). Acts as a coreceptor for TLR2:TLR6 heterodimer
in response to diacylated lipopeptides and for TLR2:TLR1
heterodimer in response to triacylated lipopeptides, these
clusters trigger signaling from the cell surface and subsequently
are targeted to the Golgi in a lipid-raft dependent pathway (By
similarity). Acts as an accessory receptor for M.tuberculosis
lipoproteins LprA, LprG and LpqH, in conjunction with coreceptors
TLR2 and TLR1. The lipoproteins act as agonists to modulate
antigen presenting cell functions in response to the pathogen
(PubMed:19362712). Binds electronegative LDL (LDL(-)) and mediates
the cytokine release induced by LDL(-) (By similarity).
{ECO:0000250|UniProtKB:P08571, ECO:0000269|PubMed:15895089,
ECO:0000269|PubMed:16148141, ECO:0000269|PubMed:19362712,
ECO:0000269|PubMed:21821728, ECO:0000269|PubMed:8612135}.
-!- SUBUNIT: Belongs to the lipopolysaccharide (LPS) receptor, a
multi-protein complex containing at least CD14, LY96 and TLR4 (By
similarity). Interacts with LPS-bound LPB. Interacts with LPAR1
(PubMed:21821728). Interacts with the TLR2:TLR6 or TLR2:TLR1
heterodimers; upon interaction with ligands such as diacylated
lipopeptides and triacylated lipopeptides, respectively. Interacts
with MYO18A (By similarity). {ECO:0000250|UniProtKB:P08571,
ECO:0000269|PubMed:21821728}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21821728,
ECO:0000269|PubMed:8612135}; Lipid-anchor, GPI-anchor
{ECO:0000250|UniProtKB:P08571}. Secreted
{ECO:0000250|UniProtKB:P08571}. Membrane raft
{ECO:0000250|UniProtKB:P08571}. Golgi apparatus
{ECO:0000250|UniProtKB:P08571}. Note=Soluble, secreted forms seem
to exist. They may arise by cleavage of the GPI anchor.
{ECO:0000250|UniProtKB:P08571}.
-!- TISSUE SPECIFICITY: Detected on peritoneal macrophages (at protein
level) (PubMed:8612135). Cell surface expression detected in lung
alveolar macrophages, dendritic macrophages and lung macrophages
(at protein level) (PubMed:19362712).
{ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:8612135}.
-!- DOMAIN: The C-terminal leucine-rich repeat (LRR) region is
required for responses to smooth LPS.
{ECO:0000269|PubMed:15895089}.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are fertile and
appear healthy when kept in a clean, microbe-free environment.
Mice do not respond to bacterial smooth lipopolysaccharide (LPS).
Contrary to wild-type, they do not develop toxic shock or secrete
TNF in response to LPS. Surprisingly, they have fewer live
bacteria in their lungs and bloodstream after inoculation with
bacteria and are not killed by an inoculum that is lethal to wild-
type; they are killed when the inoculum is further increased.
{ECO:0000269|PubMed:8612135}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X13987; CAA32166.1; -; Genomic_DNA.
EMBL; X13333; CAA31710.1; -; mRNA.
EMBL; M34510; AAA37387.1; -; Genomic_DNA.
EMBL; BC057889; AAH57889.1; -; mRNA.
CCDS; CCDS29159.1; -.
PIR; S03605; TDMSM4.
RefSeq; NP_033971.1; NM_009841.4.
UniGene; Mm.3460; -.
PDB; 1WWL; X-ray; 2.50 A; A/B=20-329.
PDBsum; 1WWL; -.
ProteinModelPortal; P10810; -.
SMR; P10810; -.
BioGrid; 198573; 1.
STRING; 10090.ENSMUSP00000056669; -.
ChEMBL; CHEMBL2384896; -.
iPTMnet; P10810; -.
PhosphoSitePlus; P10810; -.
SwissPalm; P10810; -.
PaxDb; P10810; -.
PeptideAtlas; P10810; -.
PRIDE; P10810; -.
Ensembl; ENSMUST00000061829; ENSMUSP00000056669; ENSMUSG00000051439.
GeneID; 12475; -.
KEGG; mmu:12475; -.
UCSC; uc008eof.2; mouse.
CTD; 929; -.
MGI; MGI:88318; Cd14.
eggNOG; ENOG410IXG9; Eukaryota.
eggNOG; ENOG41118N2; LUCA.
GeneTree; ENSGT00390000005689; -.
HOGENOM; HOG000237268; -.
HOVERGEN; HBG005269; -.
InParanoid; P10810; -.
KO; K04391; -.
OMA; LCPHKFP; -.
OrthoDB; EOG091G0DA3; -.
PhylomeDB; P10810; -.
TreeFam; TF338550; -.
Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
Reactome; R-MMU-166020; Transfer of LPS from LBP carrier to CD14.
Reactome; R-MMU-166166; MyD88-independent TLR3/TLR4 cascade.
Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-MMU-6798695; Neutrophil degranulation.
EvolutionaryTrace; P10810; -.
PMAP-CutDB; P10810; -.
PRO; PR:P10810; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000051439; -.
CleanEx; MM_CD14; -.
ExpressionAtlas; P10810; baseline and differential.
Genevisible; P10810; MM.
GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0046696; C:lipopolysaccharide receptor complex; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0071723; F:lipopeptide binding; ISO:MGI.
GO; GO:0001530; F:lipopolysaccharide binding; ISO:MGI.
GO; GO:0070891; F:lipoteichoic acid binding; ISO:MGI.
GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; ISS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0071223; P:cellular response to lipoteichoic acid; ISO:MGI.
GO; GO:0071219; P:cellular response to molecule of bacterial origin; ISO:MGI.
GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0045807; P:positive regulation of endocytosis; IMP:UniProtKB.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; ISO:MGI.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; IMP:CACAO.
GO; GO:0006898; P:receptor-mediated endocytosis; IMP:CACAO.
GO; GO:0009617; P:response to bacterium; IMP:UniProtKB.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0009408; P:response to heat; IEA:Ensembl.
GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
GO; GO:0002237; P:response to molecule of bacterial origin; IDA:UniProtKB.
GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IMP:UniProtKB.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR016337; Monocyte_diff_Ag_CD14.
PIRSF; PIRSF002017; CD14; 1.
SUPFAM; SSF52058; SSF52058; 1.
PROSITE; PS51450; LRR; 3.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Golgi apparatus; GPI-anchor; Immunity;
Inflammatory response; Innate immunity; Leucine-rich repeat;
Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 15
CHAIN 16 336 Monocyte differentiation antigen CD14.
/FTId=PRO_0000020887.
PROPEP 337 366 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000020888.
REPEAT 50 78 LRR 1.
REPEAT 79 114 LRR 2.
REPEAT 115 140 LRR 3.
REPEAT 141 168 LRR 4.
REPEAT 169 192 LRR 5.
REPEAT 193 220 LRR 6.
REPEAT 221 247 LRR 7.
REPEAT 248 272 LRR 8.
REPEAT 273 293 LRR 9.
REPEAT 294 315 LRR 10.
REPEAT 316 340 LRR 11.
REGION 284 366 Required for response to bacterial
lipopolysaccharide (LPS).
{ECO:0000269|PubMed:15895089}.
LIPID 336 336 GPI-anchor amidated asparagine.
{ECO:0000255}.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15644310}.
CARBOHYD 180 180 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15644310}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15644310}.
CARBOHYD 317 317 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 23 32 {ECO:0000269|PubMed:15644310}.
DISULFID 30 47 {ECO:0000269|PubMed:15644310}.
DISULFID 183 213 {ECO:0000269|PubMed:15644310}.
DISULFID 237 266 {ECO:0000269|PubMed:15644310}.
STRAND 36 38 {ECO:0000244|PDB:1WWL}.
HELIX 41 46 {ECO:0000244|PDB:1WWL}.
STRAND 47 49 {ECO:0000244|PDB:1WWL}.
STRAND 51 61 {ECO:0000244|PDB:1WWL}.
HELIX 65 68 {ECO:0000244|PDB:1WWL}.
HELIX 76 84 {ECO:0000244|PDB:1WWL}.
STRAND 89 96 {ECO:0000244|PDB:1WWL}.
HELIX 99 109 {ECO:0000244|PDB:1WWL}.
STRAND 116 123 {ECO:0000244|PDB:1WWL}.
STRAND 132 134 {ECO:0000244|PDB:1WWL}.
STRAND 141 147 {ECO:0000244|PDB:1WWL}.
STRAND 151 155 {ECO:0000244|PDB:1WWL}.
HELIX 156 161 {ECO:0000244|PDB:1WWL}.
STRAND 170 175 {ECO:0000244|PDB:1WWL}.
TURN 183 185 {ECO:0000244|PDB:1WWL}.
STRAND 194 196 {ECO:0000244|PDB:1WWL}.
HELIX 204 211 {ECO:0000244|PDB:1WWL}.
STRAND 222 224 {ECO:0000244|PDB:1WWL}.
HELIX 233 242 {ECO:0000244|PDB:1WWL}.
STRAND 248 251 {ECO:0000244|PDB:1WWL}.
STRAND 274 276 {ECO:0000244|PDB:1WWL}.
STRAND 291 297 {ECO:0000244|PDB:1WWL}.
TURN 309 311 {ECO:0000244|PDB:1WWL}.
STRAND 314 319 {ECO:0000244|PDB:1WWL}.
TURN 324 326 {ECO:0000244|PDB:1WWL}.
SEQUENCE 366 AA; 39204 MW; 57C4492EC7EA3AA1 CRC64;
MERVLGLLLL LLVHASPAPP EPCELDEESC SCNFSDPKPD WSSAFNCLGA ADVELYGGGR
SLEYLLKRVD TEADLGQFTD IIKSLSLKRL TVRAARIPSR ILFGALRVLG ISGLQELTLE
NLEVTGTAPP PLLEATGPDL NILNLRNVSW ATRDAWLAEL QQWLKPGLKV LSIAQAHSLN
FSCEQVRVFP ALSTLDLSDN PELGERGLIS ALCPLKFPTL QVLALRNAGM ETPSGVCSAL
AAARVQLQGL DLSHNSLRDA AGAPSCDWPS QLNSLNLSFT GLKQVPKGLP AKLSVLDLSY
NRLDRNPSPD ELPQVGNLSL KGNPFLDSES HSEKFNSGVV TAGAPSSQAV ALSGTLALLL
GDRLFV


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