CD14_HUMAN
ID CD14_HUMAN Reviewed; 375 AA.
AC P08571; Q53XT5; Q96FR6; Q96L99; Q9UNS3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Monocyte differentiation antigen CD14 {ECO:0000303|PubMed:3385210};
DE AltName: Full=Myeloid cell-specific leucine-rich glycoprotein;
DE AltName: CD_antigen=CD14;
DE Contains:
DE RecName: Full=Monocyte differentiation antigen CD14, urinary form;
DE Contains:
DE RecName: Full=Monocyte differentiation antigen CD14, membrane-bound form;
DE Flags: Precursor;
GN Name=CD14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=3385210;
RA Haziot A., Chen S., Ferrero E., Low M.G., Silber R., Goyert S.M.;
RT "The monocyte differentiation antigen, CD14, is anchored to the cell
RT membrane by a phosphatidylinositol linkage.";
RL J. Immunol. 141:547-552(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lymphocyte;
RX PubMed=2453848; DOI=10.1093/nar/16.9.4173;
RA Ferrero E., Goyert S.M.;
RT "Nucleotide sequence of the gene encoding the monocyte differentiation
RT antigen, CD14.";
RL Nucleic Acids Res. 16:4173-4173(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Macrophage;
RX PubMed=2472171; DOI=10.1016/0167-4781(80)90012-3;
RA Setoguchi M., Nasu N., Yoshida S., Higuchi Y., Akizuki S., Yamamoto S.;
RT "Mouse and human CD14 (myeloid cell-specific leucine-rich glycoprotein)
RT primary structure deduced from cDNA clones.";
RL Biochim. Biophys. Acta 1008:213-222(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=2462937;
RA Simmons D.L., Tan S., Tenen D.G., Nicholson-Weller A., Seed B.;
RT "Monocyte antigen CD14 is a phospholipid anchored membrane protein.";
RL Blood 73:284-289(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Promyelocytic leukemia;
RA Long J.Y., Xue Y.N., Sun L., Wang H.X.;
RT "Cloning and sequencing of human CD14 gene.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 25:377-378(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=18810425; DOI=10.1007/s00251-008-0332-0;
RA Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T., Kimura A.;
RT "Natural selection in the TLR-related genes in the course of primate
RT evolution.";
RL Immunogenetics 60:727-735(2008).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-125.
RC TISSUE=Glioblastoma;
RA Deininger M.H., Meyermann R., Schluesener H.J.;
RT "Expression and secretion of CD14 in glial neoplasms of the brain.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP PROTEIN SEQUENCE OF 362-367, AND SUBCELLULAR LOCATION.
RX PubMed=2779588; DOI=10.1016/0161-5890(89)90048-5;
RA Bazil V., Baudys M., Hilgert I., Stefanova I., Low M.G., Zbrozek J.,
RA Horejsi V.;
RT "Structural relationship between the soluble and membrane-bound forms of
RT human monocyte surface glycoprotein CD14.";
RL Mol. Immunol. 26:657-662(1989).
RN [12]
RP FUNCTION, INTERACTION WITH LBP, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=1698311; DOI=10.1126/science.1698311;
RA Wright S.D., Ramos R.A., Tobias P.S., Ulevitch R.J., Mathison J.C.;
RT "CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding
RT protein.";
RL Science 249:1431-1433(1990).
RN [13]
RP FUNCTION.
RX PubMed=8612135; DOI=10.1016/s1074-7613(00)80254-x;
RA Haziot A., Ferrero E., Kontgen F., Hijiya N., Yamamoto S., Silver J.,
RA Stewart C.L., Goyert S.M.;
RT "Resistance to endotoxin shock and reduced dissemination of gram-negative
RT bacteria in CD14-deficient mice.";
RL Immunity 4:407-414(1996).
RN [14]
RP SUBUNIT.
RX PubMed=11274165; DOI=10.1074/jbc.m009164200;
RA da Silva Correia J., Soldau K., Christen U., Tobias P.S., Ulevitch R.J.;
RT "Lipopolysaccharide is in close proximity to each of the proteins in its
RT membrane receptor complex. transfer from CD14 to TLR4 and MD-2.";
RL J. Biol. Chem. 276:21129-21135(2001).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151 AND ASN-282.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TLR1; TLR2 AND TLR6.
RX PubMed=16880211; DOI=10.1074/jbc.m602794200;
RA Triantafilou M., Gamper F.G., Haston R.M., Mouratis M.A., Morath S.,
RA Hartung T., Triantafilou K.;
RT "Membrane sorting of toll-like receptor (TLR)-2/6 and TLR2/1 heterodimers
RT at the cell surface determines heterotypic associations with CD36 and
RT intracellular targeting.";
RL J. Biol. Chem. 281:31002-31011(2006).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [18]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-336, AND STRUCTURE OF
RP CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [19]
RP FUNCTION.
RX PubMed=20133493; DOI=10.1093/intimm/dxq005;
RA Tsukamoto H., Fukudome K., Takao S., Tsuneyoshi N., Kimoto M.;
RT "Lipopolysaccharide-binding protein-mediated Toll-like receptor 4
RT dimerization enables rapid signal transduction against lipopolysaccharide
RT stimulation on membrane-associated CD14-expressing cells.";
RL Int. Immunol. 22:271-280(2010).
RN [20]
RP FUNCTION, AND INTERACTION WITH FSTL1.
RX PubMed=22265692; DOI=10.1016/j.febslet.2012.01.010;
RA Murakami K., Tanaka M., Usui T., Kawabata D., Shiomi A.,
RA Iguchi-Hashimoto M., Shimizu M., Yukawa N., Yoshifuji H., Nojima T.,
RA Ohmura K., Fujii T., Umehara H., Mimori T.;
RT "Follistatin-related protein/follistatin-like 1 evokes an innate immune
RT response via CD14 and toll-like receptor 4.";
RL FEBS Lett. 586:319-324(2012).
RN [21]
RP FUNCTION.
RX PubMed=23880187; DOI=10.1016/j.atherosclerosis.2013.05.011;
RA Estruch M., Bancells C., Beloki L., Sanchez-Quesada J.L.,
RA Ordonez-Llanos J., Benitez S.;
RT "CD14 and TLR4 mediate cytokine release promoted by electronegative LDL in
RT monocytes.";
RL Atherosclerosis 229:356-362(2013).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP SUBCELLULAR LOCATION, INDUCTION BY 27-HYDROXYCHOLESTEROL, AND TISSUE
RP SPECIFICITY.
RX PubMed=25497142; DOI=10.1016/j.bbadis.2014.12.003;
RA Kim S.M., Kim B.Y., Eo S.K., Kim C.D., Kim K.;
RT "27-Hydroxycholesterol up-regulates CD14 and predisposes monocytic cells to
RT superproduction of CCL2 in response to lipopolysaccharide.";
RL Biochim. Biophys. Acta 1852:442-450(2015).
RN [24]
RP INTERACTION WITH MYO18A.
RX PubMed=25965346; DOI=10.1371/journal.pone.0126576;
RA Yang L., Carrillo M., Wu Y.M., DiAngelo S.L., Silveyra P., Umstead T.M.,
RA Halstead E.S., Davies M.L., Hu S., Floros J., McCormack F.X.,
RA Christensen N.D., Chroneos Z.C.;
RT "SP-R210 (Myo18A) isoforms as intrinsic modulators of macrophage priming
RT and activation.";
RL PLoS ONE 10:E0126576-E0126576(2015).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 26-335, DISULFIDE BONDS, FUNCTION,
RP AND SUBUNIT.
RX PubMed=23264655; DOI=10.4049/jimmunol.1202446;
RA Kelley S.L., Lukk T., Nair S.K., Tapping R.I.;
RT "The crystal structure of human soluble CD14 reveals a bent solenoid with a
RT hydrophobic amino-terminal pocket.";
RL J. Immunol. 190:1304-1311(2013).
CC -!- FUNCTION: Coreceptor for bacterial lipopolysaccharide (PubMed:1698311,
CC PubMed:23264655). In concert with LBP, binds to monomeric
CC lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby
CC mediating the innate immune response to bacterial lipopolysaccharide
CC (LPS) (PubMed:20133493, PubMed:23264655, PubMed:22265692). Acts via
CC MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine
CC secretion and the inflammatory response (PubMed:8612135). Acts as a
CC coreceptor for TLR2:TLR6 heterodimer in response to diacylated
CC lipopeptides and for TLR2:TLR1 heterodimer in response to triacylated
CC lipopeptides, these clusters trigger signaling from the cell surface
CC and subsequently are targeted to the Golgi in a lipid-raft dependent
CC pathway (PubMed:16880211). Binds electronegative LDL (LDL(-)) and
CC mediates the cytokine release induced by LDL(-) (PubMed:23880187).
CC {ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:1698311,
CC ECO:0000269|PubMed:20133493, ECO:0000269|PubMed:22265692,
CC ECO:0000269|PubMed:23264655, ECO:0000269|PubMed:23880187,
CC ECO:0000269|PubMed:8612135}.
CC -!- SUBUNIT: Interacts with LPS-bound LPB (PubMed:1698311,
CC PubMed:23264655). Belongs to the lipopolysaccharide (LPS) receptor, a
CC multi-protein complex containing at least CD14, LY96 and TLR4
CC (PubMed:11274165). Interacts with LPAR1 (By similarity). Interacts with
CC the TLR2:TLR6 or TLR2:TLR1 heterodimers; upon interaction with ligands
CC such as diacylated lipopeptides and triacylated lipopeptides,
CC respectively (PubMed:16880211). Interacts with MYO18A
CC (PubMed:25965346). Interacts with FSTL1 (PubMed:22265692).
CC {ECO:0000250|UniProtKB:P10810, ECO:0000269|PubMed:11274165,
CC ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:1698311,
CC ECO:0000269|PubMed:22265692, ECO:0000269|PubMed:23264655,
CC ECO:0000269|PubMed:25965346}.
CC -!- INTERACTION:
CC P08571; Q12841: FSTL1; NbExp=3; IntAct=EBI-3905196, EBI-2349801;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1698311,
CC ECO:0000269|PubMed:2462937, ECO:0000269|PubMed:3385210}; Lipid-anchor,
CC GPI-anchor {ECO:0000269|PubMed:1698311, ECO:0000269|PubMed:2462937,
CC ECO:0000269|PubMed:3385210}. Secreted {ECO:0000269|PubMed:25497142,
CC ECO:0000269|PubMed:2779588}. Membrane raft
CC {ECO:0000269|PubMed:16880211}. Golgi apparatus
CC {ECO:0000269|PubMed:16880211}. Note=Secreted forms may arise by
CC cleavage of the GPI anchor. {ECO:0000269|PubMed:2462937,
CC ECO:0000269|PubMed:2779588, ECO:0000269|PubMed:3385210}.
CC -!- TISSUE SPECIFICITY: Detected on macrophages (at protein level)
CC (PubMed:1698311). Expressed strongly on the surface of monocytes and
CC weakly on the surface of granulocytes; also expressed by most tissue
CC macrophages. {ECO:0000269|PubMed:1698311, ECO:0000269|PubMed:25497142}.
CC -!- INDUCTION: The expression in monocytes is highly induced by 27-
CC hydroxycholesterol, priming monocytes/macrophages such that LPS-
CC mediated inflammatory reaction is accelerated. Secretion of soluble
CC CD14 is also enhanced. {ECO:0000269|PubMed:25497142}.
CC -!- DOMAIN: The C-terminal leucine-rich repeat (LRR) region is required for
CC responses to smooth LPS. {ECO:0000250|UniProtKB:P10810}.
CC -!- PTM: N- and O- glycosylated. O-glycosylated with a core 1 or possibly
CC core 8 glycan. {ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CD14 entry;
CC URL="https://en.wikipedia.org/wiki/CD14";
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DR EMBL; X06882; CAA29999.1; -; Genomic_DNA.
DR EMBL; X13334; CAA31711.1; -; mRNA.
DR EMBL; M86511; AAA51930.1; -; mRNA.
DR EMBL; AF097942; AAC83816.1; -; mRNA.
DR EMBL; AB446505; BAG55282.1; -; mRNA.
DR EMBL; BT007331; AAP35995.1; -; mRNA.
DR EMBL; CH471062; EAW62037.1; -; Genomic_DNA.
DR EMBL; BC010507; AAH10507.1; -; mRNA.
DR EMBL; AY044269; AAL02401.1; -; mRNA.
DR CCDS; CCDS4232.1; -.
DR PIR; A27637; TDHUM4.
DR RefSeq; NP_000582.1; NM_000591.3.
DR RefSeq; NP_001035110.1; NM_001040021.2.
DR RefSeq; NP_001167575.1; NM_001174104.1.
DR RefSeq; NP_001167576.1; NM_001174105.1.
DR PDB; 4GLP; X-ray; 4.00 A; A=26-335.
DR PDBsum; 4GLP; -.
DR AlphaFoldDB; P08571; -.
DR SMR; P08571; -.
DR BioGRID; 107367; 44.
DR DIP; DIP-1030N; -.
DR IntAct; P08571; 33.
DR MINT; P08571; -.
DR STRING; 9606.ENSP00000304236; -.
DR ChEMBL; CHEMBL2384897; -.
DR DrugBank; DB06546; Atibuclimab.
DR TCDB; 8.A.43.1.17; the neat-domain containing methaemoglobin heme sequestration (n-mhs) family.
DR GlyConnect; 774; 24 N-Linked glycans (2 sites), 1 O-Linked glycan (1 site).
DR GlyGen; P08571; 7 sites, 26 N-linked glycans (2 sites), 4 O-linked glycans (3 sites).
DR iPTMnet; P08571; -.
DR PhosphoSitePlus; P08571; -.
DR BioMuta; CD14; -.
DR DMDM; 20141203; -.
DR EPD; P08571; -.
DR jPOST; P08571; -.
DR MassIVE; P08571; -.
DR MaxQB; P08571; -.
DR PaxDb; P08571; -.
DR PeptideAtlas; P08571; -.
DR PRIDE; P08571; -.
DR ProteomicsDB; 52122; -.
DR ABCD; P08571; 7 sequenced antibodies.
DR Antibodypedia; 798; 3677 antibodies from 56 providers.
DR CPTC; P08571; 1 antibody.
DR DNASU; 929; -.
DR Ensembl; ENST00000302014.11; ENSP00000304236.6; ENSG00000170458.14.
DR Ensembl; ENST00000401743.6; ENSP00000385519.2; ENSG00000170458.14.
DR GeneID; 929; -.
DR KEGG; hsa:929; -.
DR MANE-Select; ENST00000302014.11; ENSP00000304236.6; NM_000591.4; NP_000582.1.
DR UCSC; uc003lgi.3; human.
DR CTD; 929; -.
DR DisGeNET; 929; -.
DR GeneCards; CD14; -.
DR HGNC; HGNC:1628; CD14.
DR HPA; ENSG00000170458; Tissue enhanced (liver).
DR MIM; 158120; gene.
DR neXtProt; NX_P08571; -.
DR OpenTargets; ENSG00000170458; -.
DR PharmGKB; PA26188; -.
DR VEuPathDB; HostDB:ENSG00000170458; -.
DR eggNOG; ENOG502SNYQ; Eukaryota.
DR GeneTree; ENSGT00390000005689; -.
DR HOGENOM; CLU_062152_0_0_1; -.
DR InParanoid; P08571; -.
DR OMA; PSSSCQW; -.
DR PhylomeDB; P08571; -.
DR TreeFam; TF338550; -.
DR PathwayCommons; P08571; -.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-140534; Caspase activation via Death Receptors in the presence of ligand.
DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-HSA-166020; Transfer of LPS from LBP carrier to CD14.
DR Reactome; R-HSA-166058; MyD88:MAL(TIRAP) cascade initiated on plasma membrane.
DR Reactome; R-HSA-166166; MyD88-independent TLR4 cascade.
DR Reactome; R-HSA-168179; Toll Like Receptor TLR1:TLR2 Cascade.
DR Reactome; R-HSA-168188; Toll Like Receptor TLR6:TLR2 Cascade.
DR Reactome; R-HSA-2562578; TRIF-mediated programmed cell death.
DR Reactome; R-HSA-5602498; MyD88 deficiency (TLR2/4).
DR Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4).
DR Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
DR Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
DR Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR SignaLink; P08571; -.
DR SIGNOR; P08571; -.
DR BioGRID-ORCS; 929; 14 hits in 1077 CRISPR screens.
DR ChiTaRS; CD14; human.
DR GeneWiki; CD14; -.
DR GenomeRNAi; 929; -.
DR Pharos; P08571; Tbio.
DR PRO; PR:P08571; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P08571; protein.
DR Bgee; ENSG00000170458; Expressed in monocyte and 184 other tissues.
DR ExpressionAtlas; P08571; baseline and differential.
DR Genevisible; P08571; HS.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0046696; C:lipopolysaccharide receptor complex; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0071723; F:lipopeptide binding; IDA:AgBase.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:MGI.
DR GO; GO:0070891; F:lipoteichoic acid binding; IDA:MGI.
DR GO; GO:0001847; F:opsonin receptor activity; TAS:BHF-UCL.
DR GO; GO:0016019; F:peptidoglycan immune receptor activity; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0071223; P:cellular response to lipoteichoic acid; IDA:MGI.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; IDA:CAFA.
DR GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; IDA: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:0006909; P:phagocytosis; TAS:ProtInc.
DR GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:CAFA.
DR GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:AgBase.
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; IDA:AgBase.
DR GO; GO:0032481; P:positive regulation of type I interferon production; IBA:GO_Central.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
DR GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
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 PIRSF; PIRSF002017; CD14; 1.
DR PROSITE; PS51450; LRR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Golgi apparatus; GPI-anchor; Immunity; Inflammatory response;
KW Innate immunity; Leucine-rich repeat; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT CHAIN 20..367
FT /note="Monocyte differentiation antigen CD14, urinary form"
FT /id="PRO_0000020884"
FT CHAIN 20..345
FT /note="Monocyte differentiation antigen CD14, membrane-
FT bound form"
FT /id="PRO_0000020885"
FT PROPEP 346..375
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000020886"
FT REPEAT 54..82
FT /note="LRR 1"
FT REPEAT 83..118
FT /note="LRR 2"
FT REPEAT 119..144
FT /note="LRR 3"
FT REPEAT 145..172
FT /note="LRR 4"
FT REPEAT 173..196
FT /note="LRR 5"
FT REPEAT 197..224
FT /note="LRR 6"
FT REPEAT 225..251
FT /note="LRR 7"
FT REPEAT 252..278
FT /note="LRR 8"
FT REPEAT 279..299
FT /note="LRR 9"
FT REPEAT 300..321
FT /note="LRR 10"
FT REPEAT 322..349
FT /note="LRR 11"
FT REGION 290..375
FT /note="Required for response to bacterial
FT lipopolysaccharide (LPS)"
FT /evidence="ECO:0000250|UniProtKB:P10810"
FT LIPID 345
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 336
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:19838169"
FT DISULFID 25..36
FT /evidence="ECO:0000269|PubMed:23264655"
FT DISULFID 34..51
FT /evidence="ECO:0000269|PubMed:23264655"
FT DISULFID 187..217
FT /evidence="ECO:0000269|PubMed:23264655"
FT DISULFID 241..272
FT /evidence="ECO:0000269|PubMed:23264655"
FT VARIANT 204
FT /note="N -> D (in dbSNP:rs2228049)"
FT /id="VAR_024302"
FT VARIANT 341
FT /note="E -> K (in dbSNP:rs11556179)"
FT /id="VAR_050771"
FT CONFLICT 187
FT /note="C -> Y (in Ref. 2; CAA29999)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="D -> E (in Ref. 5; AAC83816)"
FT /evidence="ECO:0000305"
SQ 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
