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Monocyte differentiation antigen CD14 (Myeloid cell-specific leucine-rich glycoprotein) (CD antigen CD14) [Cleaved into: Monocyte differentiation antigen CD14, urinary form; Monocyte differentiation antigen CD14, membrane-bound form]

 CD14_HUMAN              Reviewed;         375 AA.
P08571; Q53XT5; Q96FR6; Q96L99; Q9UNS3;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
27-MAR-2002, sequence version 2.
25-OCT-2017, entry version 186.
RecName: Full=Monocyte differentiation antigen CD14 {ECO:0000303|PubMed:3385210};
AltName: Full=Myeloid cell-specific leucine-rich glycoprotein;
AltName: CD_antigen=CD14;
Contains:
RecName: Full=Monocyte differentiation antigen CD14, urinary form;
Contains:
RecName: Full=Monocyte differentiation antigen CD14, membrane-bound form;
Flags: Precursor;
Name=CD14;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=3385210;
Haziot A., Chen S., Ferrero E., Low M.G., Silber R., Goyert S.M.;
"The monocyte differentiation antigen, CD14, is anchored to the cell
membrane by a phosphatidylinositol linkage.";
J. Immunol. 141:547-552(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lymphocyte;
PubMed=2453848; DOI=10.1093/nar/16.9.4173;
Ferrero E., Goyert S.M.;
"Nucleotide sequence of the gene encoding the monocyte differentiation
antigen, CD14.";
Nucleic Acids Res. 16:4173-4173(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=2462937;
Simmons D.L., Tan S., Tenen D.G., Nicholson-Weller A., Seed B.;
"Monocyte antigen CD14 is a phospholipid anchored membrane protein.";
Blood 73:284-289(1989).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Promyelocytic leukemia;
Long J.Y., Xue Y.N., Sun L., Wang H.X.;
"Cloning and sequencing of human CD14 gene.";
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 25:377-378(1998).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=18810425; DOI=10.1007/s00251-008-0332-0;
Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T.,
Kimura A.;
"Natural selection in the TLR-related genes in the course of primate
evolution.";
Immunogenetics 60:727-735(2008).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-125.
TISSUE=Glioblastoma;
Deininger M.H., Meyermann R., Schluesener H.J.;
"Expression and secretion of CD14 in glial neoplasms of the brain.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[11]
PROTEIN SEQUENCE OF 362-367, AND SUBCELLULAR LOCATION.
PubMed=2779588; DOI=10.1016/0161-5890(89)90048-5;
Bazil V., Baudys M., Hilgert I., Stefanova I., Low M.G., Zbrozek J.,
Horejsi V.;
"Structural relationship between the soluble and membrane-bound forms
of human monocyte surface glycoprotein CD14.";
Mol. Immunol. 26:657-662(1989).
[12]
FUNCTION, INTERACTION WITH LBP, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=1698311; DOI=10.1126/science.1698311;
Wright S.D., Ramos R.A., Tobias P.S., Ulevitch R.J., Mathison J.C.;
"CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS
binding protein.";
Science 249:1431-1433(1990).
[13]
FUNCTION.
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).
[14]
SUBUNIT.
PubMed=11274165; DOI=10.1074/jbc.M009164200;
da Silva Correia J., Soldau K., Christen U., Tobias P.S.,
Ulevitch R.J.;
"Lipopolysaccharide is in close proximity to each of the proteins in
its membrane receptor complex. transfer from CD14 to TLR4 and MD-2.";
J. Biol. Chem. 276:21129-21135(2001).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151 AND ASN-282.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TLR1; TLR2 AND
TLR6.
PubMed=16880211; DOI=10.1074/jbc.M602794200;
Triantafilou M., Gamper F.G., Haston R.M., Mouratis M.A., Morath S.,
Hartung T., Triantafilou K.;
"Membrane sorting of toll-like receptor (TLR)-2/6 and TLR2/1
heterodimers at the cell surface determines heterotypic associations
with CD36 and intracellular targeting.";
J. Biol. Chem. 281:31002-31011(2006).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-336, AND STRUCTURE OF
CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[19]
FUNCTION.
PubMed=20133493; DOI=10.1093/intimm/dxq005;
Tsukamoto H., Fukudome K., Takao S., Tsuneyoshi N., Kimoto M.;
"Lipopolysaccharide-binding protein-mediated Toll-like receptor 4
dimerization enables rapid signal transduction against
lipopolysaccharide stimulation on membrane-associated CD14-expressing
cells.";
Int. Immunol. 22:271-280(2010).
[20]
FUNCTION.
PubMed=23880187; DOI=10.1016/j.atherosclerosis.2013.05.011;
Estruch M., Bancells C., Beloki L., Sanchez-Quesada J.L.,
Ordonez-Llanos J., Benitez S.;
"CD14 and TLR4 mediate cytokine release promoted by electronegative
LDL in monocytes.";
Atherosclerosis 229:356-362(2013).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
SUBCELLULAR LOCATION, INDUCTION BY 27-HYDROXYCHOLESTEROL, AND TISSUE
SPECIFICITY.
PubMed=25497142; DOI=10.1016/j.bbadis.2014.12.003;
Kim S.M., Kim B.Y., Eo S.K., Kim C.D., Kim K.;
"27-Hydroxycholesterol up-regulates CD14 and predisposes monocytic
cells to superproduction of CCL2 in response to lipopolysaccharide.";
Biochim. Biophys. Acta 1852:442-450(2015).
[23]
INTERACTION WITH MYO18A.
PubMed=25965346; DOI=10.1371/journal.pone.0126576;
Yang L., Carrillo M., Wu Y.M., DiAngelo S.L., Silveyra P.,
Umstead T.M., Halstead E.S., Davies M.L., Hu S., Floros J.,
McCormack F.X., Christensen N.D., Chroneos Z.C.;
"SP-R210 (Myo18A) isoforms as intrinsic modulators of macrophage
priming and activation.";
PLoS ONE 10:E0126576-E0126576(2015).
[24]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 26-335, DISULFIDE BONDS,
FUNCTION, AND SUBUNIT.
PubMed=23264655; DOI=10.4049/jimmunol.1202446;
Kelley S.L., Lukk T., Nair S.K., Tapping R.I.;
"The crystal structure of human soluble CD14 reveals a bent solenoid
with a hydrophobic amino-terminal pocket.";
J. Immunol. 190:1304-1311(2013).
-!- FUNCTION: Coreceptor for bacterial lipopolysaccharide
(PubMed:1698311, PubMed:23264655). 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:20133493, PubMed:23264655). Acts
via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation,
cytokine secretion and the inflammatory response (PubMed:8612135).
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 (PubMed:16880211). Binds
electronegative LDL (LDL(-)) and mediates the cytokine release
induced by LDL(-) (PubMed:23880187). {ECO:0000269|PubMed:16880211,
ECO:0000269|PubMed:1698311, ECO:0000269|PubMed:20133493,
ECO:0000269|PubMed:23264655, ECO:0000269|PubMed:23880187,
ECO:0000269|PubMed:8612135}.
-!- SUBUNIT: Interacts with LPS-bound LPB (PubMed:1698311,
PubMed:23264655). Belongs to the lipopolysaccharide (LPS)
receptor, a multi-protein complex containing at least CD14, LY96
and TLR4 (PubMed:11274165). Interacts with LPAR1 (By similarity).
Interacts with the TLR2:TLR6 or TLR2:TLR1 heterodimers; upon
interaction with ligands such as diacylated lipopeptides and
triacylated lipopeptides, respectively (PubMed:16880211).
Interacts with MYO18A (PubMed:25965346).
{ECO:0000250|UniProtKB:P10810, ECO:0000269|PubMed:11274165,
ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:1698311,
ECO:0000269|PubMed:23264655, ECO:0000269|PubMed:25965346}.
-!- INTERACTION:
Q12841:FSTL1; NbExp=3; IntAct=EBI-3905196, EBI-2349801;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1698311,
ECO:0000269|PubMed:2462937, ECO:0000269|PubMed:3385210}; Lipid-
anchor, GPI-anchor {ECO:0000269|PubMed:1698311,
ECO:0000269|PubMed:2462937, ECO:0000269|PubMed:3385210}. Secreted
{ECO:0000269|PubMed:25497142, ECO:0000269|PubMed:2779588}.
Membrane raft {ECO:0000269|PubMed:16880211}. Golgi apparatus
{ECO:0000269|PubMed:16880211}. Note=Secreted forms may arise by
cleavage of the GPI anchor. {ECO:0000269|PubMed:2462937,
ECO:0000269|PubMed:2779588, ECO:0000269|PubMed:3385210}.
-!- TISSUE SPECIFICITY: Detected on macrophages (at protein level)
(PubMed:1698311). Expressed strongly on the surface of monocytes
and weakly on the surface of granulocytes; also expressed by most
tissue macrophages. {ECO:0000269|PubMed:1698311,
ECO:0000269|PubMed:25497142}.
-!- INDUCTION: The expression in monocytes is highly induced by 27-
hydroxycholesterol, priming monocytes/macrophages such that LPS-
mediated inflammatory reaction is accelerated. Secretion of
soluble CD14 is also enhanced. {ECO:0000269|PubMed:25497142}.
-!- DOMAIN: The C-terminal leucine-rich repeat (LRR) region is
required for responses to smooth LPS.
{ECO:0000250|UniProtKB:P10810}.
-!- PTM: N- and O- glycosylated. O-glycosylated with a core 1 or
possibly core 8 glycan. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169}.
-!- WEB RESOURCE: Name=Wikipedia; Note=CD14 entry;
URL="https://en.wikipedia.org/wiki/CD14";
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EMBL; X06882; CAA29999.1; -; Genomic_DNA.
EMBL; X13334; CAA31711.1; -; mRNA.
EMBL; M86511; AAA51930.1; -; mRNA.
EMBL; AF097942; AAC83816.1; -; mRNA.
EMBL; AB446505; BAG55282.1; -; mRNA.
EMBL; BT007331; AAP35995.1; -; mRNA.
EMBL; CH471062; EAW62037.1; -; Genomic_DNA.
EMBL; BC010507; AAH10507.1; -; mRNA.
EMBL; AY044269; AAL02401.1; -; mRNA.
CCDS; CCDS4232.1; -.
PIR; A27637; TDHUM4.
RefSeq; NP_000582.1; NM_000591.3.
RefSeq; NP_001035110.1; NM_001040021.2.
RefSeq; NP_001167575.1; NM_001174104.1.
RefSeq; NP_001167576.1; NM_001174105.1.
UniGene; Hs.163867; -.
PDB; 4GLP; X-ray; 4.00 A; A=26-335.
PDBsum; 4GLP; -.
ProteinModelPortal; P08571; -.
SMR; P08571; -.
BioGrid; 107367; 35.
DIP; DIP-1030N; -.
IntAct; P08571; 27.
MINT; MINT-7990664; -.
STRING; 9606.ENSP00000304236; -.
ChEMBL; CHEMBL2384897; -.
iPTMnet; P08571; -.
PhosphoSitePlus; P08571; -.
BioMuta; CD14; -.
DMDM; 20141203; -.
MaxQB; P08571; -.
PaxDb; P08571; -.
PeptideAtlas; P08571; -.
PRIDE; P08571; -.
DNASU; 929; -.
Ensembl; ENST00000302014; ENSP00000304236; ENSG00000170458.
Ensembl; ENST00000401743; ENSP00000385519; ENSG00000170458.
GeneID; 929; -.
KEGG; hsa:929; -.
UCSC; uc003lgi.3; human.
CTD; 929; -.
DisGeNET; 929; -.
EuPathDB; HostDB:ENSG00000170458.13; -.
GeneCards; CD14; -.
HGNC; HGNC:1628; CD14.
HPA; CAB033631; -.
HPA; CAB072865; -.
HPA; CAB072866; -.
HPA; HPA001887; -.
HPA; HPA002127; -.
MIM; 158120; gene.
neXtProt; NX_P08571; -.
OpenTargets; ENSG00000170458; -.
PharmGKB; PA26188; -.
eggNOG; ENOG410IXG9; Eukaryota.
eggNOG; ENOG41118N2; LUCA.
GeneTree; ENSGT00390000005689; -.
HOGENOM; HOG000237268; -.
HOVERGEN; HBG005269; -.
InParanoid; P08571; -.
KO; K04391; -.
OMA; LCPHKFP; -.
OrthoDB; EOG091G0DA3; -.
PhylomeDB; P08571; -.
TreeFam; TF338550; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-140534; Ligand-dependent caspase activation.
Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
Reactome; R-HSA-166020; Transfer of LPS from LBP carrier to CD14.
Reactome; R-HSA-166058; MyD88:Mal cascade initiated on plasma membrane.
Reactome; R-HSA-166166; MyD88-independent TLR3/TLR4 cascade.
Reactome; R-HSA-168179; Toll Like Receptor TLR1:TLR2 Cascade.
Reactome; R-HSA-168188; Toll Like Receptor TLR6:TLR2 Cascade.
Reactome; R-HSA-2562578; TRIF-mediated programmed cell death.
Reactome; R-HSA-5602498; MyD88 deficiency (TLR2/4).
Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4).
Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
Reactome; R-HSA-937072; TRAF6 mediated induction of TAK1 complex.
Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
ChiTaRS; CD14; human.
GeneWiki; CD14; -.
GenomeRNAi; 929; -.
PMAP-CutDB; P08571; -.
PRO; PR:P08571; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000170458; -.
CleanEx; HS_CD14; -.
ExpressionAtlas; P08571; baseline and differential.
Genevisible; P08571; HS.
GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0046696; C:lipopolysaccharide receptor complex; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0071723; F:lipopeptide binding; IDA:AgBase.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:MGI.
GO; GO:0070891; F:lipoteichoic acid binding; IDA:MGI.
GO; GO:0001847; F:opsonin receptor activity; TAS:BHF-UCL.
GO; GO:0016019; F:peptidoglycan receptor activity; TAS:ProtInc.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
GO; GO:0071223; P:cellular response to lipoteichoic acid; IDA:MGI.
GO; GO:0071219; P:cellular response to molecule of bacterial origin; IDA:CAFA.
GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; IDA:UniProtKB.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
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; IEA:Ensembl.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0070266; P:necroptotic process; TAS:Reactome.
GO; GO:0034128; P:negative regulation of MyD88-independent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006909; P:phagocytosis; TAS:ProtInc.
GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; IMP:CAFA.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:AgBase.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:AgBase.
GO; GO:0032481; P:positive regulation of type I interferon production; IEA:Ensembl.
GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
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:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISS:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome.
GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
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; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Golgi apparatus; GPI-anchor; Immunity; Inflammatory response;
Innate immunity; Leucine-rich repeat; Lipoprotein; Membrane;
Polymorphism; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 19
CHAIN 20 367 Monocyte differentiation antigen CD14,
urinary form.
/FTId=PRO_0000020884.
CHAIN 20 345 Monocyte differentiation antigen CD14,
membrane-bound form.
/FTId=PRO_0000020885.
PROPEP 346 375 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000020886.
REPEAT 54 82 LRR 1.
REPEAT 83 118 LRR 2.
REPEAT 119 144 LRR 3.
REPEAT 145 172 LRR 4.
REPEAT 173 196 LRR 5.
REPEAT 197 224 LRR 6.
REPEAT 225 251 LRR 7.
REPEAT 252 278 LRR 8.
REPEAT 279 299 LRR 9.
REPEAT 300 321 LRR 10.
REPEAT 322 349 LRR 11.
REGION 290 375 Required for response to bacterial
lipopolysaccharide (LPS).
{ECO:0000250|UniProtKB:P10810}.
LIPID 345 345 GPI-anchor amidated asparagine.
{ECO:0000255}.
CARBOHYD 37 37 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 282 282 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 336 336 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:19838169}.
DISULFID 25 36 {ECO:0000269|PubMed:23264655}.
DISULFID 34 51 {ECO:0000269|PubMed:23264655}.
DISULFID 187 217 {ECO:0000269|PubMed:23264655}.
DISULFID 241 272 {ECO:0000269|PubMed:23264655}.
VARIANT 204 204 N -> D (in dbSNP:rs2228049).
/FTId=VAR_024302.
VARIANT 341 341 E -> K (in dbSNP:rs11556179).
/FTId=VAR_050771.
CONFLICT 187 187 C -> Y (in Ref. 2; CAA29999).
{ECO:0000305}.
CONFLICT 303 303 D -> E (in Ref. 5; AAC83816).
{ECO:0000305}.
SEQUENCE 375 AA; 40076 MW; 1746CDB41F394F8D CRC64;
MERASCLLLL LLPLVHVSAT TPEPCELDDE DFRCVCNFSE PQPDWSEAFQ CVSAVEVEIH
AGGLNLEPFL KRVDADADPR QYADTVKALR VRRLTVGAAQ VPAQLLVGAL RVLAYSRLKE
LTLEDLKITG TMPPLPLEAT GLALSSLRLR NVSWATGRSW LAELQQWLKP GLKVLSIAQA
HSPAFSCEQV RAFPALTSLD LSDNPGLGER GLMAALCPHK FPAIQNLALR NTGMETPTGV
CAALAAAGVQ PHSLDLSHNS LRATVNPSAP RCMWSSALNS LNLSFAGLEQ VPKGLPAKLR
VLDLSCNRLN RAPQPDELPE VDNLTLDGNP FLVPGTALPH EGSMNSGVVP ACARSTLSVG
VSGTLVLLQG ARGFA


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