CLM2_MOUSE
ID CLM2_MOUSE Reviewed; 196 AA.
AC Q8K249;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=CMRF35-like molecule 2;
DE Short=CLM-2;
DE AltName: Full=CD300 antigen-like family member E;
DE AltName: CD_antigen=CD300e;
DE Flags: Precursor;
GN Name=Cd300e; Synonyms=Cd300le, Clm2;
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].
RA Colonna M.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
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 STRAIN=FVB/N; 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).
CC -!- FUNCTION: Probably acts as an activating receptor. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TYROBP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
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DR EMBL; AY457048; AAR27939.1; -; mRNA.
DR EMBL; AF437879; AAN86136.1; -; mRNA.
DR EMBL; AL607025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034097; AAH34097.1; -; mRNA.
DR EMBL; BC039971; AAH39971.1; -; mRNA.
DR CCDS; CCDS25618.1; -.
DR RefSeq; NP_742047.1; NM_172050.3.
DR RefSeq; XP_006533136.1; XM_006533073.1.
DR RefSeq; XP_006533137.1; XM_006533074.1.
DR AlphaFoldDB; Q8K249; -.
DR SMR; Q8K249; -.
DR STRING; 10090.ENSMUSP00000054883; -.
DR GlyGen; Q8K249; 1 site.
DR PhosphoSitePlus; Q8K249; -.
DR PaxDb; Q8K249; -.
DR PRIDE; Q8K249; -.
DR Antibodypedia; 2708; 300 antibodies from 28 providers.
DR DNASU; 217306; -.
DR Ensembl; ENSMUST00000062787; ENSMUSP00000054883; ENSMUSG00000048498.
DR GeneID; 217306; -.
DR KEGG; mmu:217306; -.
DR UCSC; uc007mgk.1; mouse.
DR CTD; 342510; -.
DR MGI; MGI:2387602; Cd300e.
DR VEuPathDB; HostDB:ENSMUSG00000048498; -.
DR eggNOG; ENOG502SRT9; Eukaryota.
DR GeneTree; ENSGT00940000162923; -.
DR HOGENOM; CLU_051023_3_0_1; -.
DR InParanoid; Q8K249; -.
DR OMA; CRIQTVW; -.
DR OrthoDB; 1494510at2759; -.
DR PhylomeDB; Q8K249; -.
DR TreeFam; TF334441; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-2172127; DAP12 interactions.
DR BioGRID-ORCS; 217306; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Cyth2; mouse.
DR PRO; PR:Q8K249; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K249; protein.
DR Bgee; ENSMUSG00000048498; Expressed in spleen and 20 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 2.60.40.10; -; 1.
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.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..196
FT /note="CMRF35-like molecule 2"
FT /id="PRO_0000320124"
FT TOPO_DOM 18..171
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..122
FT /note="Ig-like V-type"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..104
FT /evidence="ECO:0000250"
SQ SEQUENCE 196 AA; 21822 MW; E23888479CB556E8 CRC64;
MRLCAGLLLL CFQGCLSLTG PGSVSGYVGG SLRVQCQYSP SYKGYMKYWC RGPHDTTCKT
IVETDGSEKE KRSGPVSIRD HASNSTITVI MEDLSEDNAG SYWCKIQTSF IWDSWSRDPS
VSVRVNVFPA TTPTLPATTA ILPLVNSGQN LRISTNVMFI FQLWSLLSSI QFQVLVFLKL
PLFLSMLCAI FWVNRL