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UniProtKB/Swiss-Prot entry P08571


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CD14_HUMAN
Primary accession number P08571
Secondary accession numbers Q53XT5 Q96FR6 Q96L99 Q9UNS3
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on March 27, 2002 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 105)
Name and origin of the protein
Protein name Monocyte differentiation antigen CD14 [Precursor]
Synonyms Myeloid cell-specific leucine-rich glycoprotein
CD14 antigen
Contains Monocyte differentiation antigen CD14, urinary form
Monocyte differentiation antigen CD14, membrane-bound form
Gene name
Name: CD14
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3385210 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1093/nar/16.9.4173; PubMed=2453848 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1016/0167-4781(80)90012-3; PubMed=2472171 [NCBI, ExPASy, EBI, Israel, Japan]
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].
PubMed=2462937 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1007/s00251-008-0332-0; PubMed=18810425 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/0161-5890(89)90048-5; PubMed=2779588 [NCBI, ExPASy, EBI, Israel, Japan]
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]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151 AND ASN-282, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
  • FUNCTION: Cooperates with MD-2 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Up-regulates cell surface molecules, including adhesion molecules.
  • SUBUNIT: Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, MD-2 and TLR4.
  • SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
  • TISSUE SPECIFICITY: Expressed strongly on the surface of monocytes and weakly on the surface of granulocytes; also expressed by most tissue macrophages.
  • SIMILARITY: Contains 11 LRR (leucine-rich) repeats.
  • WEB RESOURCE: Name=Wikipedia; Note=CD14 entry; URL="http://en.wikipedia.org/wiki/CD14";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X06882; CAA29999.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13334; CAA31711.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M86511; AAA51930.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097942; AAC83816.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB446505; BAG55282.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007331; AAP35995.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471062; EAW62037.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010507; AAH10507.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY044269; AAL02401.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00029260; -.
PIR A27637; TDHUM4.
RefSeq NP_000582.1; -.
NP_001035110.1; -.
UniGene Hs.163867
3D structure databases
SMR P08571; 24-332.
ModBase P08571.
Protein-protein interaction databases
DIP DIP:1030N; -.
Enzyme and pathway databases
Reactome REACT_6900; Signaling in Immune system.
Organism-specific databases
GeneCards GC05M139991; -.
H-InvDB HIX0005234; -.
HGNC HGNC:1628; CD14.
GenAtlas CD14.
HPA HPA001887; -.
HPA002127; -.
MIM 158120; gene. [NCBI / EBI]
PharmGKB PA26188; -.
Gene expression databases
ArrayExpress P08571; -.
Bgee P08571; -.
CleanEx HS_CD14; -.
GermOnline ENSG00000170458; Homo sapiens.
Ontologies
GO
GO:0031225; Cellular component: anchored to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005576; Cellular component: extracellular region (inferred from experiment from Reactome).
GO:0005886; Cellular component: plasma membrane (inferred from experiment from Reactome).
GO:0001847; Molecular function: opsonin receptor activity (traceable author statement from UniProtKB).
GO:0016019; Molecular function: peptidoglycan receptor activity (traceable author statement from ProtInc).
GO:0006915; Biological process: apoptosis (traceable author statement from ProtInc).
GO:0007166; Biological process: cell surface receptor linked signal transduction (traceable author statement from ProtInc).
GO:0006955; Biological process: immune response (inferred from electronic annotation from UniProtKB-KW).
GO:0006954; Biological process: inflammatory response (inferred from electronic annotation from UniProtKB-KW).
GO:0006909; Biological process: phagocytosis (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001611; Leu-rich_rpt.
IPR016337; Monocyte_diff_Ag_CD14.
Graphical view of domain structure.
Pfam PF00560; LRR_1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF002017; CD14; 1.
Proteomic databases
PeptideAtlas P08571; -.
PRIDE P08571; -.
Genome annotation databases
Ensembl ENSG00000170458; Homo sapiens. [Contig view]
GeneID 929; -.
KEGG hsa:929; -.
Phylogenomic databases
HOGENOM P08571; -.
HOVERGEN P08571; -.
OMA P08571; ALCPHKF.
Other
NextBio 3850; -.
PMAP-CutDB P08571; -.
SOURCE CD14; Homo sapiens.
ProtoNet P08571.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor; Immune response; Inflammatory response; Leucine-rich repeat; Lipoprotein; Membrane; Polymorphism; Repeat; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    19  19      
CHAIN   20   367  348     Monocyte differentiation antigen CD14, urinary form. PRO_0000020884
CHAIN   20   345  326     Monocyte differentiation antigen CD14, membrane-bound form. PRO_0000020885
PROPEP   346   375  30     Removed in mature form (Potential). PRO_0000020886
REPEAT   54    82  29     LRR 1. 
REPEAT   83   118  36     LRR 2. 
REPEAT   119   144  26     LRR 3. 
REPEAT   145   172  28     LRR 4. 
REPEAT   173   196  24     LRR 5. 
REPEAT   197   224  28     LRR 6. 
REPEAT   225   251  27     LRR 7. 
REPEAT   252   278  27     LRR 8. 
REPEAT   279   299  21     LRR 9. 
REPEAT   300   321  22     LRR 10. 
REPEAT   322   349  28     LRR 11. 
LIPID   345   345        GPI-anchor amidated asparagine (Potential). 
CARBOHYD   37    37        N-linked (GlcNAc...) (Potential). 
CARBOHYD   151   151        N-linked (GlcNAc...). 
CARBOHYD   282   282        N-linked (GlcNAc...). 
CARBOHYD   323   323        N-linked (GlcNAc...). 
DISULFID   25    36        By similarity. 
DISULFID   34    51        By similarity. 
DISULFID   187   217        By similarity. 
DISULFID   241   272        By similarity. 
VARIANT   204   204  1     N -> D (in dbSNP:rs2228049 [NCBI]). VAR_024302 
VARIANT   341   341  1     E -> K (in dbSNP:rs11556179 [NCBI]). VAR_050771 
CONFLICT   187   187        C -> Y (in Ref. 2; CAA29999). 
CONFLICT   303   303        D -> E (in Ref. 5; AAC83816). 
Sequence information
Length: 375 AA [This is the length of the unprocessed precursor] Molecular weight: 40076 Da [This is the MW of the unprocessed precursor] CRC64: 1746CDB41F394F8D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MERASCLLLL LLPLVHVSAT TPEPCELDDE DFRCVCNFSE PQPDWSEAFQ CVSAVEVEIH 

        70         80         90        100        110        120 
AGGLNLEPFL KRVDADADPR QYADTVKALR VRRLTVGAAQ VPAQLLVGAL RVLAYSRLKE 

       130        140        150        160        170        180 
LTLEDLKITG TMPPLPLEAT GLALSSLRLR NVSWATGRSW LAELQQWLKP GLKVLSIAQA 

       190        200        210        220        230        240 
HSPAFSCEQV RAFPALTSLD LSDNPGLGER GLMAALCPHK FPAIQNLALR NTGMETPTGV 

       250        260        270        280        290        300 
CAALAAAGVQ PHSLDLSHNS LRATVNPSAP RCMWSSALNS LNLSFAGLEQ VPKGLPAKLR 

       310        320        330        340        350        360 
VLDLSCNRLN RAPQPDELPE VDNLTLDGNP FLVPGTALPH EGSMNSGVVP ACARSTLSVG 

       370 
VSGTLVLLQG ARGFA 

P08571 in FASTA format

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