CLM3_MOUSE
ID CLM3_MOUSE Reviewed; 245 AA.
AC Q6SJQ5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=CMRF35-like molecule 3 {ECO:0000303|PubMed:14662855};
DE Short=CLM-3 {ECO:0000303|PubMed:14662855};
DE AltName: Full=CD300 antigen-like family member H {ECO:0000305};
DE AltName: Full=CD300 molecule-like family member D3 {ECO:0000312|MGI:MGI:2687214};
DE Flags: Precursor;
GN Name=Cd300ld3 {ECO:0000312|MGI:MGI:2687214};
GN Synonyms=Cd300lh {ECO:0000312|MGI:MGI:2687214},
GN Clm3 {ECO:0000303|PubMed:14662855}, Lmir7 {ECO:0000312|MGI:MGI:2687214};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=14662855; DOI=10.4049/jimmunol.171.12.6541;
RA Chung D.-H., Humphrey M.B., Nakamura M.C., Ginzinger D.G., Seaman W.E.,
RA Daws M.R.;
RT "CMRF-35-like molecule-1, a novel mouse myeloid receptor, can inhibit
RT osteoclast formation.";
RL J. Immunol. 171:6541-6548(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH FCER1G, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF 177-ASN--TRP-182 AND 189-SER--VAL-198.
RC STRAIN=C57BL/6J; TISSUE=Mast cell;
RX PubMed=20817736; DOI=10.1074/jbc.m110.137166;
RA Enomoto Y., Yamanishi Y., Izawa K., Kaitani A., Takahashi M., Maehara A.,
RA Oki T., Takamatsu R., Kajikawa M., Takai T., Kitamura T., Kitaura J.;
RT "Characterization of leukocyte mono-immunoglobulin-like receptor 7
RT (LMIR7)/CLM-3 as an activating receptor: its similarities to and
RT differences from LMIR4/CLM-5.";
RL J. Biol. Chem. 285:35274-35283(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
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 [5]
RP FUNCTION, INTERACTION WITH TLR9, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION.
RX PubMed=21940676; DOI=10.4049/jimmunol.1003806;
RA Wu Y., Zhu X., Li N., Chen T., Yang M., Yao M., Liu X., Jin B., Wang X.,
RA Cao X.;
RT "CMRF-35-like molecule 3 preferentially promotes TLR9-triggered
RT proinflammatory cytokine production in macrophages by enhancing TNF
RT receptor-associated factor 6 ubiquitination.";
RL J. Immunol. 187:4881-4889(2011).
CC -!- FUNCTION: Acts as an activating receptor inducing cytokine production
CC in mast cells. Can act as a positive regulator of TLR9 signaling in
CC macrophages, leading to enhanced production of pro-inflammatory
CC cytokines. {ECO:0000269|PubMed:20817736, ECO:0000269|PubMed:21940676}.
CC -!- SUBUNIT: Interacts with FCER1G; the interaction may be indirect.
CC Interacts with TLR9. {ECO:0000269|PubMed:20817736,
CC ECO:0000269|PubMed:21940676}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Early endosome
CC {ECO:0000269|PubMed:21940676}. Lysosome {ECO:0000269|PubMed:21940676}.
CC -!- TISSUE SPECIFICITY: Highly expressed in bone marrow-derived mast cells
CC and macrophages, peripheral blood monocytes and CD11c+ cells, with
CC weaker expression detected in CD11b cells in bone marrow and peripheral
CC blood. Not detected in B220+ cells in bone marrow or spleen, in Thy-
CC 1.2+ or CD3+ cells in peripheral blood, spleen or thymus, or in NK1.1+
CC cells in spleen (at protein level). Widely expressed in various tissues
CC including heart, liver, spleen, lung, kidney, brain, bone marrow,
CC thymus, axillary lymph node and mesenteric lymph node. Highly expressed
CC in macrophage cell lines J774.1 and RAW 264.7 and in mast cell line
CC MC/9. Weak expression detected in B-lineage cell lines WEHI-231 and A20
CC and in dendritic cell line DC2.4. Not detected in other myeloid cell
CC lines or T-lineage cell lines. {ECO:0000269|PubMed:20817736,
CC ECO:0000269|PubMed:21940676}.
CC -!- INDUCTION: Down-regulated in macrophages by single-stranded CpG
CC oligodeoxynucleotide stimulation. {ECO:0000269|PubMed:21940676}.
CC -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
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DR EMBL; AY457049; AAR27940.1; -; mRNA.
DR EMBL; AL607025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC119352; AAI19353.1; -; mRNA.
DR EMBL; BC120623; AAI20624.1; -; mRNA.
DR CCDS; CCDS25617.1; -.
DR RefSeq; NP_954671.1; NM_199201.1.
DR AlphaFoldDB; Q6SJQ5; -.
DR SMR; Q6SJQ5; -.
DR STRING; 10090.ENSMUSP00000090116; -.
DR iPTMnet; Q6SJQ5; -.
DR PhosphoSitePlus; Q6SJQ5; -.
DR MaxQB; Q6SJQ5; -.
DR PaxDb; Q6SJQ5; -.
DR PRIDE; Q6SJQ5; -.
DR DNASU; 382551; -.
DR Ensembl; ENSMUST00000092459; ENSMUSP00000090116; ENSMUSG00000069607.
DR GeneID; 382551; -.
DR KEGG; mmu:382551; -.
DR UCSC; uc007mgi.2; mouse.
DR CTD; 382551; -.
DR MGI; MGI:2687214; Cd300ld3.
DR VEuPathDB; HostDB:ENSMUSG00000069607; -.
DR eggNOG; ENOG502S7MA; Eukaryota.
DR GeneTree; ENSGT00940000154332; -.
DR HOGENOM; CLU_051023_3_0_1; -.
DR InParanoid; Q6SJQ5; -.
DR OMA; MENAGHE; -.
DR OrthoDB; 1494510at2759; -.
DR PhylomeDB; Q6SJQ5; -.
DR TreeFam; TF334441; -.
DR BioGRID-ORCS; 382551; 5 hits in 34 CRISPR screens.
DR ChiTaRS; Cyth3; mouse.
DR PRO; PR:Q6SJQ5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6SJQ5; protein.
DR Bgee; ENSMUSG00000069607; Expressed in granulocyte and 37 other tissues.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
DR GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; IDA:MGI.
DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Endosome; Immunity; Immunoglobulin domain;
KW Lysosome; Membrane; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..245
FT /note="CMRF35-like molecule 3"
FT /id="PRO_0000320125"
FT TOPO_DOM 19..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..124
FT /note="Ig-like V-type"
FT REGION 177..182
FT /note="Important for maintaining surface expression and for
FT interaction with FCER1G"
FT /evidence="ECO:0000269|PubMed:20817736"
FT REGION 189..198
FT /note="Important for maintaining surface expression and for
FT interaction with FCER1G"
FT /evidence="ECO:0000269|PubMed:20817736"
FT DISULFID 40..108
FT /evidence="ECO:0000250"
FT MUTAGEN 177..182
FT /note="NSLFIW->SRPHTR: Increases surface expression in
FT transfected pro-B cells and enhances interaction with
FT FCER1G. Slightly increases surface expression and enhances
FT interaction with FCER1G; when associated with 189-Y--L-
FT 198."
FT /evidence="ECO:0000269|PubMed:20817736"
FT MUTAGEN 189..198
FT /note="SFLLMVFVVV->YFLLMVFVEL: Reduces surface expression
FT in transfected pro-B cells and enhances interaction with
FT FCER1G. Slightly increases surface expression in
FT transfected pro-B cells and enhances interaction with
FT FCER1G; when associated with 177-S--R-182."
FT /evidence="ECO:0000269|PubMed:20817736"
SQ SEQUENCE 245 AA; 27312 MW; 781FAB5E03608F4D CRC64;
MWQFPALLFL FLPGCCTAQD PVTGPEEVSG QEQGSLTVQC RYDSGWKDYK KYWCRGAYWK
SCEILVETDA SEQLVKENRV SIRDDQTDFI FTVTMEDLRM SDADIYWCGI TKAGTDPMFK
VNVNIDPEIS TTIMTTTATV LPSTVLTSTV LTSTVLTPTT PTTESIGTEN IGQVTQNSLF
IWSLLSSISF LLMVFVVVPL LLSMLSAVLW VNRPQRHYGG GEIGLVETHR SDALDGEKHF
PGDEK
