CD14_RABIT
ID CD14_RABIT Reviewed; 372 AA.
AC Q28680;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1375269; DOI=10.1084/jem.175.6.1697;
RA Lee J.D., Kato K., Tobias P.S., Kirkland T.N., Ulevitch R.J.;
RT "Transfection of CD14 into 70Z/3 cells dramatically enhances the
RT sensitivity to complexes of lipopolysaccharide (LPS) and LPS binding
RT protein.";
RL J. Exp. Med. 175:1697-1705(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Myeloid;
RA Ishida T., Setoguchi M., Matsuura K., Yasunori H., Akizuki S., Yamamoto S.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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) (PubMed:1375269). Acts via MyD88,
CC TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion
CC and the inflammatory response. Acts as a coreceptor for TLR2:TLR6
CC heterodimer in response to diacylated lipopeptides and for TLR2:TLR1
CC heterodimer in response to triacylated lipopeptides, these clusters
CC trigger signaling from the cell surface and subsequently are targeted
CC to the Golgi in a lipid-raft dependent pathway (By similarity). Binds
CC electronegative LDL (LDL(-)) and mediates the cytokine release induced
CC by LDL(-) (By similarity). {ECO:0000250|UniProtKB:P08571,
CC ECO:0000250|UniProtKB:P10810, ECO:0000269|PubMed:1375269}.
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:0000269|PubMed:1375269};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1375269}. 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 -!- 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; M85233; AAA31195.1; -; mRNA.
DR EMBL; D16545; BAA21770.1; -; mRNA.
DR RefSeq; NP_001075664.1; NM_001082195.2.
DR AlphaFoldDB; Q28680; -.
DR SMR; Q28680; -.
DR STRING; 9986.ENSOCUP00000003648; -.
DR GeneID; 100008983; -.
DR KEGG; ocu:100008983; -.
DR CTD; 929; -.
DR eggNOG; ENOG502SNYQ; Eukaryota.
DR InParanoid; Q28680; -.
DR OrthoDB; 1097023at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0071726; P:cellular response to diacyl bacterial lipopeptide; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
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:0009617; P:response to bacterium; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR016337; Monocyte_diff_Ag_CD14.
DR PANTHER; PTHR10630; PTHR10630; 1.
DR PIRSF; PIRSF002017; CD14; 1.
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_0000020889"
FT PROPEP 343..372
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000020890"
FT REPEAT 54..82
FT /note="LRR 1"
FT REPEAT 83..118
FT /note="LRR 2"
FT REPEAT 119..145
FT /note="LRR 3"
FT REPEAT 146..173
FT /note="LRR 4"
FT REPEAT 174..197
FT /note="LRR 5"
FT REPEAT 198..225
FT /note="LRR 6"
FT REPEAT 226..252
FT /note="LRR 7"
FT REPEAT 253..275
FT /note="LRR 8"
FT REPEAT 276..296
FT /note="LRR 9"
FT REPEAT 297..318
FT /note="LRR 10"
FT REPEAT 319..346
FT /note="LRR 11"
FT REGION 287..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 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..36
FT /evidence="ECO:0000250|UniProtKB:P08571"
FT DISULFID 34..51
FT /evidence="ECO:0000250|UniProtKB:P08571"
FT DISULFID 188..218
FT /evidence="ECO:0000250|UniProtKB:P08571"
FT DISULFID 242..269
FT /evidence="ECO:0000250|UniProtKB:P08571"
SQ SEQUENCE 372 AA; 39992 MW; F9D6A997DD8825CC CRC64;
MEPVPCLLLL LLPLLRASTD TPEPCELDDD DIRCVCNFSD PQPDWSSALQ CMPAVQVEMW
GGGHSLEQFL RQADLYTDQR RYADVVKALR VRRLTVGAVQ VPAPLLLGVL RVLGYSRLKE
LALEDIEVTG TAPPPPPLEA TGPALSTLSL RNVSWPKGGA WLSELQQWLK PGLQVLNIAQ
AHTLAFSCEQ VRTFSALTTL DLSENPGLGE RGLVAALCPH KFPALQDLAL RNAGMKTLQG
VCAALAEAGV QPHHLDLSHN SLRADTQRCI WPSALNSLNL SFTGLQQVPK GLPAKLNVLD
LSCNKLNRAP QPGELPKVVN LSLDGNPFLV PGASKLQEDL TNSGVFPACP PSPLAMGMSG
TLALLQGARG FI
