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P08571 (CD14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Names and origin

Protein namesRecommended name:
Monocyte differentiation antigen CD14
Alternative name(s):
Myeloid cell-specific leucine-rich glycoprotein
CD_antigen=CD14

Cleaved into the following 2 chains:

  1. Monocyte differentiation antigen CD14, urinary form
  2. Monocyte differentiation antigen CD14, membrane-bound form
Gene names
Name:CD14
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (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 structure

Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, MD-2 and TLR4.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor.

Tissue specificity

Expressed strongly on the surface of monocytes and weakly on the surface of granulocytes; also expressed by most tissue macrophages.

Post-translational modification

N- and O- glycosylated. O-glycosylated with a core 1 or possibly core 8 glycan. Ref.12 Ref.13 Ref.14

Sequence similarities

Contains 11 LRR (leucine-rich) repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Chain20 – 367348Monocyte differentiation antigen CD14, urinary form
PRO_0000020884
Chain20 – 345326Monocyte differentiation antigen CD14, membrane-bound form
PRO_0000020885
Propeptide346 – 37530Removed in mature form Potential
PRO_0000020886

Regions

Repeat54 – 8229LRR 1
Repeat83 – 11836LRR 2
Repeat119 – 14426LRR 3
Repeat145 – 17228LRR 4
Repeat173 – 19624LRR 5
Repeat197 – 22428LRR 6
Repeat225 – 25127LRR 7
Repeat252 – 27827LRR 8
Repeat279 – 29921LRR 9
Repeat300 – 32122LRR 10
Repeat322 – 34928LRR 11

Amino acid modifications

Lipidation3451GPI-anchor amidated asparagine Potential
Glycosylation371N-linked (GlcNAc...) Potential
Glycosylation1511N-linked (GlcNAc...) Ref.12
Glycosylation2821N-linked (GlcNAc...) Ref.12
Glycosylation3231N-linked (GlcNAc...) Ref.13
Glycosylation3361O-linked (GalNAc...) Ref.14
Disulfide bond25 ↔ 36 By similarity
Disulfide bond34 ↔ 51 By similarity
Disulfide bond187 ↔ 217 By similarity
Disulfide bond241 ↔ 272 By similarity

Natural variations

Natural variant2041N → D. [dbSNP:rs2228049]
VAR_024302
Natural variant3411E → K. [dbSNP:rs11556179]
VAR_050771

Experimental info

Sequence conflict1871C → Y in CAA29999. Ref.2
Sequence conflict3031D → E in AAC83816. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P08571-1 [UniParc].

Last modified March 27, 2002. Version 2.
Checksum: 1746CDB41F394F8D

FASTA37540,076
        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 

« Hide

References

« Hide 'large scale' references
[1]"The monocyte differentiation antigen, CD14, is anchored to the cell membrane by a phosphatidylinositol linkage."
Haziot A., Chen S., Ferrero E., Low M.G., Silber R., Goyert S.M.
J. Immunol. 141:547-552(1988) [PubMed: 3385210] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence of the gene encoding the monocyte differentiation antigen, CD14."
Ferrero E., Goyert S.M.
Nucleic Acids Res. 16:4173-4173(1988) [PubMed: 2453848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Lymphocyte.
[3]"Mouse and human CD14 (myeloid cell-specific leucine-rich glycoprotein) primary structure deduced from cDNA clones."
Setoguchi M., Nasu N., Yoshida S., Higuchi Y., Akizuki S., Yamamoto S.
Biochim. Biophys. Acta 1008:213-222(1989) [PubMed: 2472171] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Macrophage.
[4]"Monocyte antigen CD14 is a phospholipid anchored membrane protein."
Simmons D.L., Tan S., Tenen D.G., Nicholson-Weller A., Seed B.
Blood 73:284-289(1989) [PubMed: 2462937] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Cloning and sequencing of human CD14 gene."
Long J.Y., Xue Y.N., Sun L., Wang H.X.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 25:377-378(1998)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Promyelocytic leukemia.
[6]"Natural selection in the TLR-related genes in the course of primate evolution."
Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T., Kimura A.
Immunogenetics 60:727-735(2008) [PubMed: 18810425] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[10]"Expression and secretion of CD14 in glial neoplasms of the brain."
Deininger M.H., Meyermann R., Schluesener H.J.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-125.
Tissue: Glioblastoma.
[11]"Structural relationship between the soluble and membrane-bound forms of human monocyte surface glycoprotein CD14."
Bazil V., Baudys M., Hilgert I., Stefanova I., Low M.G., Zbrozek J., Horejsi V.
Mol. Immunol. 26:657-662(1989) [PubMed: 2779588] [Abstract]
Cited for: PROTEIN SEQUENCE OF 362-367.
[12]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151 AND ASN-282, MASS SPECTROMETRY.
Tissue: Plasma.
[13]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323, MASS SPECTROMETRY.
Tissue: Liver.
[14]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed: 19838169] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-336, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY.
Tissue: Cerebrospinal fluid.
+Additional computationally mapped references.

Web resources

Wikipedia

CD14 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06882 Genomic DNA. Translation: CAA29999.1.
X13334 mRNA. Translation: CAA31711.1.
M86511 mRNA. Translation: AAA51930.1.
AF097942 mRNA. Translation: AAC83816.1.
AB446505 mRNA. Translation: BAG55282.1.
BT007331 mRNA. Translation: AAP35995.1.
CH471062 Genomic DNA. Translation: EAW62037.1.
BC010507 mRNA. Translation: AAH10507.1.
AY044269 mRNA. Translation: AAL02401.1.
IPIIPI00029260.
PIRTDHUM4. A27637.
RefSeqNP_000582.1.
NP_001035110.1.
NP_001167575.1.
NP_001167576.1.
UniGeneHs.163867.
Hs.638333.

3D structure databases

ProteinModelPortalP08571.
SMRP08571. Positions 22-332.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1030N.
STRINGP08571.

Proteomic databases

PeptideAtlasP08571.
PRIDEP08571.

Genome annotation databases

EnsemblENST00000302014; ENSP00000304236; ENSG00000170458; Homo sapiens. [Genome view]
ENST00000401743; ENSP00000385519; ENSG00000170458; Homo sapiens. [Genome view]
GeneID929.
KEGGhsa:929.
UCSCuc003lgi.1. human.

Organism-specific databases

CTD929.
GeneCardsGC05M139991.
H-InvDBHIX0005234.
HGNCHGNC:1628. CD14.
HPAHPA001887.
HPA002127.
MIM158120. gene.
PharmGKBPA26188.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG18529.
HOGENOMHBG125703.
HOVERGENHBG005269.
InParanoidP08571.
OMAALCPHKF.
OrthoDBEOG94N1C5.
PhylomeDBP08571.

Enzyme and pathway databases

ReactomeREACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressP08571.
BgeeP08571.
CleanExHS_CD14.
GenevestigatorP08571.
GermOnlineENSG00000170458. Homo sapiens.

Family and domain databases

InterProIPR001611. Leu-rich_rpt.
IPR016337. Monocyte_diff_Ag_CD14.
[Graphical view]
PfamPF00560. LRR_1. 1 hit.
[Graphical view]
PIRSFPIRSF002017. CD14. 1 hit.
PROSITEPS51450. LRR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio3850.
PMAP-CutDBP08571.
SOURCESearch...

Entry information

Entry nameCD14_HUMAN
AccessionPrimary (citable) accession number: P08571
Secondary accession number(s): Q53XT5 expand/collapse secondary AC list , Q96FR6, Q96L99, Q9UNS3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: March 27, 2002
Last modified: August 10, 2010
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families