CLM4_MOUSE
ID CLM4_MOUSE Reviewed; 228 AA.
AC Q7TSN2; Q7TN55; Q8JZM5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=CMRF-35-like molecule 4 {ECO:0000303|PubMed:14662855};
DE Short=CLM-4 {ECO:0000303|PubMed:14662855};
DE AltName: Full=CD300C molecule 2 {ECO:0000312|MGI:MGI:2153249};
DE AltName: Full=Dendritic cell-derived Ig-like receptor 1;
DE Short=DIgR1 {ECO:0000303|PubMed:11549249};
DE AltName: Full=Immunoglobulin superfamily member 7;
DE Short=IgSF7;
DE AltName: Full=Leukocyte mono-Ig-like receptor 2 {ECO:0000303|PubMed:12893283};
DE AltName: Full=Myeloid-associated immunoglobulin-like receptor 2;
DE Short=MAIR-2;
DE Short=MAIR-II {ECO:0000303|PubMed:12874256};
DE Flags: Precursor;
GN Name=Cd300c2 {ECO:0000312|MGI:MGI:2153249};
GN Synonyms=Cd300c, Clm4 {ECO:0000303|PubMed:14662855}, Igsf7, Lmir2;
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], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Dendritic cell;
RX PubMed=11549249; DOI=10.1006/bbrc.2001.5539;
RA Luo K., Zhang W., Sui L., Li N., Zhang M., Ma X., Zhang L., Cao X.;
RT "DIgR1, a novel membrane receptor of the immunoglobulin gene superfamily,
RT is preferentially expressed by antigen-presenting cells.";
RL Biochem. Biophys. Res. Commun. 287:35-41(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH TYROBP; HCST AND FCR GAMMA.
RC STRAIN=CBA/J; TISSUE=Mast cell;
RX PubMed=12893283; DOI=10.1016/s0006-291x(03)01245-2;
RA Kumagai H., Oki T., Tamitsu K., Feng S.-Z., Ono M., Nakajima H., Bao Y.-C.,
RA Kawakami Y., Nagayoshi K., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA Kawakami T., Kitamura T.;
RT "Identification and characterization of a new pair of immunoglobulin-like
RT receptors LMIR1 and 2 derived from murine bone marrow-derived mast cells.";
RL Biochem. Biophys. Res. Commun. 307:719-729(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH TYROBP.
RX PubMed=12874256; DOI=10.1084/jem.20021825;
RA Yotsumoto K., Okoshi Y., Shibuya K., Yamazaki S., Tahara-Hanaoka S.,
RA Honda S., Osawa M., Kuroiwa A., Matsuda Y., Tenen D.G., Iwama A.,
RA Nakauchi H., Shibuya A.;
RT "Paired activating and inhibitory immunoglobulin-like receptors, MAIR-I and
RT MAIR-II, regulate mast cell and macrophage activation.";
RL J. Exp. Med. 198:223-233(2003).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [7]
RP FUNCTION, INTERACTION WITH TYROBP AND FCR GAMMA, AND MUTAGENESIS OF
RP LYS-195.
RX PubMed=17202337; DOI=10.4049/jimmunol.178.2.765;
RA Nakahashi C., Tahara-Hanaoka S., Totsuka N., Okoshi Y., Takai T.,
RA Ohkohchi N., Honda S., Shibuya K., Shibuya A.;
RT "Dual assemblies of an activating immune receptor, MAIR-II, with ITAM-
RT bearing adapters DAP12 and FcRgamma chain on peritoneal macrophages.";
RL J. Immunol. 178:765-770(2007).
CC -!- FUNCTION: Acts as an activating receptor in mast cells and macrophages.
CC {ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283,
CC ECO:0000269|PubMed:17202337}.
CC -!- SUBUNIT: Interacts with TYROBP, HCST and FcR gamma.
CC {ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283,
CC ECO:0000269|PubMed:17202337}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11549249,
CC ECO:0000269|PubMed:12893283}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:11549249, ECO:0000269|PubMed:12893283}.
CC -!- TISSUE SPECIFICITY: Present on the surface of mast cells, dendritic
CC cells, peritoneal macrophages and a subset of B-cells (at protein
CC level). {ECO:0000269|PubMed:11549249, ECO:0000269|PubMed:12874256,
CC ECO:0000269|PubMed:12893283}.
CC -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
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DR EMBL; AB098476; BAC80269.1; -; mRNA.
DR EMBL; AB091767; BAC77076.1; -; mRNA.
DR EMBL; AB091768; BAC77077.1; -; mRNA.
DR EMBL; AY457050; AAR27941.1; -; mRNA.
DR EMBL; AL607025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006801; AAH06801.1; -; mRNA.
DR CCDS; CCDS25616.1; -.
DR PIR; JC7761; JC7761.
DR RefSeq; NP_598919.1; NM_134158.1.
DR AlphaFoldDB; Q7TSN2; -.
DR SMR; Q7TSN2; -.
DR BioGRID; 228270; 3.
DR STRING; 10090.ENSMUSP00000090121; -.
DR GlyGen; Q7TSN2; 1 site.
DR PaxDb; Q7TSN2; -.
DR PRIDE; Q7TSN2; -.
DR ProteomicsDB; 279114; -.
DR DNASU; 140497; -.
DR Ensembl; ENSMUST00000092464; ENSMUSP00000090121; ENSMUSG00000044811.
DR GeneID; 140497; -.
DR KEGG; mmu:140497; -.
DR CTD; 140497; -.
DR MGI; MGI:2153249; Cd300c2.
DR VEuPathDB; HostDB:ENSMUSG00000044811; -.
DR eggNOG; ENOG502S8BD; Eukaryota.
DR GeneTree; ENSGT00940000159622; -.
DR HOGENOM; CLU_051023_3_0_1; -.
DR InParanoid; Q7TSN2; -.
DR OMA; RTLNKFW; -.
DR OrthoDB; 1494510at2759; -.
DR TreeFam; TF334441; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 140497; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Cd300c; mouse.
DR PRO; PR:Q7TSN2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q7TSN2; protein.
DR Bgee; ENSMUSG00000044811; Expressed in stroma of bone marrow and 112 other tissues.
DR ExpressionAtlas; Q7TSN2; baseline and differential.
DR Genevisible; Q7TSN2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
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:0001819; P:positive regulation of cytokine production; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..228
FT /note="CMRF-35-like molecule 4"
FT /id="PRO_0000320127"
FT TOPO_DOM 25..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..126
FT /note="Ig-like V-type"
FT REGION 139..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 195
FT /note="Interaction with TYROBP or FcR gamma"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 195
FT /note="K->A: Abolishes interaction with TYROBP or FcR
FT gamma."
FT /evidence="ECO:0000269|PubMed:17202337"
FT CONFLICT 34
FT /note="A -> T (in Ref. 2; BAC80269)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="E -> K (in Ref. 2; BAC80269)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="D -> DPV (in Ref. 3; BAC77077)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="A -> T (in Ref. 2; BAC80269)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="W -> R (in Ref. 2; BAC80269)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="R -> K (in Ref. 2; BAC80269)"
FT /evidence="ECO:0000305"
FT CONFLICT 221..222
FT /note="SR -> TQ (in Ref. 2; BAC80269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 228 AA; 25206 MW; 8A52679EEC27E7C4 CRC64;
MIPRVIRLWL PSALFLSQVP GCVPLHGPST ITGAVGESLS VSCQYEEKFK TKDKFWCRGS
LKVLCKDIVK TSSSEEVRNG RVTIRDHPDN LTFTVTYESL TLEDADTYMC AVDISLFDGS
LGFDKYFKIE LSVVPSEDPV TGSSLESGRD ILESPTSSVG HTHPSVTTDD TIPAPCPQPR
SLRSSLYFWV LVSLKLFLFL SMLGAVLWVN RPQRCSGGSS SRPCYENQ
