CD14_RAT
ID CD14_RAT Reviewed; 372 AA.
AC Q63691; Q6GT04;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Monocyte differentiation antigen CD14;
DE AltName: Full=Myeloid cell-specific leucine-rich glycoprotein;
DE AltName: CD_antigen=CD14;
DE Flags: Precursor;
GN Name=Cd14;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY BACTERIAL
RP LIPOPOLYSACCHARIDE.
RC TISSUE=Spleen;
RX PubMed=8598386; DOI=10.1016/0165-5728(95)00143-3;
RA Galea E., Reis D.J., Fox E.S., Xu H., Feinstein D.L.;
RT "CD14 mediate endotoxin induction of nitric oxide synthase in cultured
RT brain glial cells.";
RL J. Neuroimmunol. 64:19-28(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9201265; DOI=10.1002/jlb.61.6.736;
RA Takai N., Kataoka M., Higuchi Y., Matsuura K., Yamamoto S.;
RT "Primary structure of rat CD14 and characteristics of rat CD14, cytokine,
RT and NO synthase mRNA expression in mononuclear phagocyte system cells in
RT response to LPS.";
RL J. Leukoc. Biol. 61:736-744(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9784508; DOI=10.1128/iai.66.11.5089-5098.1998;
RA Liu S., Khemlani L.S., Shapiro R.A., Johnson M.L., Liu K., Geller D.A.,
RA Watkins S.C., Goyert S.M., Billiar T.R.;
RT "Expression of CD14 by hepatocytes: upregulation by cytokines during
RT endotoxemia.";
RL Infect. Immun. 66:5089-5098(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
CC -!- FUNCTION: Coreceptor for bacterial lipopolysaccharide. In concert with
CC LBP, binds to monomeric lipopolysaccharide and delivers it to the
CC LY96/TLR4 complex, thereby mediating the innate immune response to
CC bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6,
CC leading to NF-kappa-B activation, cytokine secretion and the
CC inflammatory response. Acts as a coreceptor for TLR2:TLR6 heterodimer
CC in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in
CC response to triacylated lipopeptides, these clusters trigger signaling
CC from the cell surface and subsequently are targeted to the Golgi in a
CC lipid-raft dependent pathway. Binds electronegative LDL (LDL(-)) and
CC mediates the cytokine release induced by LDL(-) (By similarity).
CC {ECO:0000250|UniProtKB:P08571, ECO:0000250|UniProtKB:P10810}.
CC -!- SUBUNIT: Belongs to the lipopolysaccharide (LPS) receptor, a multi-
CC protein complex containing at least CD14, LY96 and TLR4. Interacts with
CC LPS-bound LPB. Interacts with LPAR1. Interacts with the TLR2:TLR6 or
CC TLR2:TLR1 heterodimers; upon interaction with ligands such as
CC diacylated lipopeptides and triacylated lipopeptides, respectively.
CC Interacts with MYO18A. Interacts with FSTL1.
CC {ECO:0000250|UniProtKB:P08571, ECO:0000250|UniProtKB:P10810}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08571};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P08571}. Secreted
CC {ECO:0000250|UniProtKB:P08571}. Membrane raft
CC {ECO:0000250|UniProtKB:P08571}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P08571}. Note=Soluble, secreted forms seem to
CC exist. They may arise by cleavage of the GPI anchor.
CC {ECO:0000250|UniProtKB:P08571}.
CC -!- TISSUE SPECIFICITY: Detected in macrophages and peripheral blood
CC monocytes. {ECO:0000269|PubMed:8598386}.
CC -!- INDUCTION: Up-regulated in Kuppfer cells exposed to bacterial
CC lipopolysaccharide (LPS). {ECO:0000269|PubMed:8598386}.
CC -!- DOMAIN: The C-terminal leucine-rich repeat (LRR) region is required for
CC responses to smooth LPS. {ECO:0000250|UniProtKB:P10810}.
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DR EMBL; U51804; AAB01154.1; -; mRNA.
DR EMBL; AF087943; AAC35371.1; -; mRNA.
DR EMBL; BC061733; AAH61733.1; -; mRNA.
DR RefSeq; NP_068512.1; NM_021744.1.
DR AlphaFoldDB; Q63691; -.
DR SMR; Q63691; -.
DR IntAct; Q63691; 2.
DR STRING; 10116.ENSRNOP00000023977; -.
DR GlyGen; Q63691; 5 sites.
DR SwissPalm; Q63691; -.
DR PaxDb; Q63691; -.
DR PRIDE; Q63691; -.
DR Ensembl; ENSRNOT00000023977; ENSRNOP00000023977; ENSRNOG00000017819.
DR GeneID; 60350; -.
DR KEGG; rno:60350; -.
DR UCSC; RGD:620588; rat.
DR CTD; 929; -.
DR RGD; 620588; Cd14.
DR eggNOG; ENOG502SNYQ; Eukaryota.
DR GeneTree; ENSGT00390000005689; -.
DR HOGENOM; CLU_062152_0_0_1; -.
DR InParanoid; Q63691; -.
DR OMA; PSSSCQW; -.
DR OrthoDB; 1097023at2759; -.
DR PhylomeDB; Q63691; -.
DR TreeFam; TF338550; -.
DR Reactome; R-RNO-166020; Transfer of LPS from LBP carrier to CD14.
DR Reactome; R-RNO-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q63691; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000017819; Expressed in liver and 19 other tissues.
DR Genevisible; Q63691; RN.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0046696; C:lipopolysaccharide receptor complex; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0071723; F:lipopeptide binding; ISO:RGD.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:RGD.
DR GO; GO:0070891; F:lipoteichoic acid binding; ISO:RGD.
DR GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071223; P:cellular response to lipoteichoic acid; ISO:RGD.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; ISO:RGD.
DR GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IDA:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:RGD.
DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:RGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:RGD.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:RGD.
DR GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; ISO:RGD.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISS:UniProtKB.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0032026; P:response to magnesium ion; IEP:RGD.
DR GO; GO:0002237; P:response to molecule of bacterial origin; ISO:RGD.
DR GO; GO:0034612; P:response to tumor necrosis factor; IMP:RGD.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISO:RGD.
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; 4.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Golgi apparatus; GPI-anchor;
KW Immunity; Inflammatory response; Innate immunity; Leucine-rich repeat;
KW Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..342
FT /note="Monocyte differentiation antigen CD14"
FT /id="PRO_0000020891"
FT PROPEP 343..372
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000020892"
FT REPEAT 57..84
FT /note="LRR 1"
FT REPEAT 85..120
FT /note="LRR 2"
FT REPEAT 121..146
FT /note="LRR 3"
FT REPEAT 147..174
FT /note="LRR 4"
FT REPEAT 175..198
FT /note="LRR 5"
FT REPEAT 199..226
FT /note="LRR 6"
FT REPEAT 227..253
FT /note="LRR 7"
FT REPEAT 254..278
FT /note="LRR 8"
FT REPEAT 279..299
FT /note="LRR 9"
FT REPEAT 300..321
FT /note="LRR 10"
FT REPEAT 322..346
FT /note="LRR 11"
FT REGION 290..372
FT /note="Required for response to bacterial
FT lipopolysaccharide (LPS)"
FT /evidence="ECO:0000250|UniProtKB:P10810"
FT LIPID 342
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..38
FT /evidence="ECO:0000250|UniProtKB:P08571"
FT DISULFID 36..53
FT /evidence="ECO:0000250|UniProtKB:P08571"
FT DISULFID 189..219
FT /evidence="ECO:0000250|UniProtKB:P08571"
FT DISULFID 243..272
FT /evidence="ECO:0000250|UniProtKB:P08571"
FT CONFLICT 56
FT /note="Missing (in Ref. 1; AAB01154)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="P -> S (in Ref. 1; AAB01154)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="T -> A (in Ref. 1; AAB01154)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 40054 MW; E99DD2C551DBBE69 CRC64;
MKLMLGLLLL PLTLVHASPA TPEPCELDQD EESVRCYCNF SDPQPNWSSA FLCAGAEDVE
FYGGGRSLEY LLKRVDTEAN LGQYTDIIRS LPLKRLTVRS ARVPTQILFG TLRVLGYSGL
RELTLENLEV TGTALSPLLD ATGPDLNTLS LRNVSWATTD TWLAELQQWL KPGLKVLSIA
QAHSLNFSCK QVGVFPALAT LDLSDNPELG EKGLISALCP HKFPTLQVLA LRNAGMETTS
GVCSALAAAR VPLQALDLSH NSLRDTAGTP SCDWPSQLNS LNLSFTGLEH VPKGLPAKLS
VLDLSYNRLD RKPRPEELPE VGSLSLTGNP FLHSESQSEA YNSGVVIATA LSPGSAGLSG
TLALLLGHRL FV
