CLM1_RAT
ID CLM1_RAT Reviewed; 332 AA.
AC Q566E6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=CMRF35-like molecule 1;
DE Short=CLM-1;
DE AltName: Full=CD300 antigen-like family member F;
DE AltName: CD_antigen=CD300f;
DE Flags: Precursor;
GN Name=Cd300lf; Synonyms=Clm1;
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 [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).
CC -!- FUNCTION: Acts as an inhibitory receptor for myeloid cells and mast
CC cells. Positively regulates the phagocytosis of apoptotic cells
CC (efferocytosis) via phosphatidylserine (PS) recognition; recognizes and
CC binds PS as a ligand which is expressed on the surface of apoptotic
CC cells. Plays an important role in the maintenance of immune
CC homeostasis, by promoting macrophage-mediated efferocytosis and by
CC inhibiting dendritic cell-mediated efferocytosis. Negatively regulates
CC Fc epsilon receptor-dependent mast cell activation and allergic
CC responses via binding to ceramide and sphingomyelin which act as
CC ligands. May act as a coreceptor for interleukin 4 (IL-4). Associates
CC with and regulates IL-4 receptor alpha-mediated responses by augmenting
CC IL-4- and IL-13-induced signaling. Negatively regulates the Toll-like
CC receptor (TLR) signaling mediated by MYD88 and TRIF through activation
CC of PTPN6/SHP-1 and PTPN11/SHP-2. Inhibits osteoclast formation. Induces
CC macrophage cell death upon engagement. {ECO:0000250|UniProtKB:Q6SJQ7,
CC ECO:0000250|UniProtKB:Q8TDQ1}.
CC -!- SUBUNIT: Interacts with PTPN6/SHP-1 in a tyrosine phosphorylation
CC dependent manner. Interacts with IL4R. {ECO:0000250|UniProtKB:Q6SJQ7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Phosphorylated on tyrosine. {ECO:0000250|UniProtKB:Q6SJQ7}.
CC -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
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DR EMBL; BC093593; AAH93593.1; -; mRNA.
DR RefSeq; NP_001020282.1; NM_001025111.1.
DR AlphaFoldDB; Q566E6; -.
DR SMR; Q566E6; -.
DR STRING; 10116.ENSRNOP00000033887; -.
DR GlyGen; Q566E6; 1 site.
DR PaxDb; Q566E6; -.
DR Ensembl; ENSRNOT00000039284; ENSRNOP00000033887; ENSRNOG00000021424.
DR GeneID; 287818; -.
DR KEGG; rno:287818; -.
DR CTD; 146722; -.
DR RGD; 1309733; Cd300lf.
DR eggNOG; ENOG502S7MA; Eukaryota.
DR GeneTree; ENSGT00940000154332; -.
DR InParanoid; Q566E6; -.
DR OrthoDB; 1494510at2759; -.
DR PhylomeDB; Q566E6; -.
DR TreeFam; TF334441; -.
DR PRO; PR:Q566E6; -.
DR Proteomes; UP000002494; Chromosome 10.
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:0097001; F:ceramide binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005136; F:interleukin-4 receptor binding; ISS:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0001618; F:virus receptor activity; ISO:RGD.
DR GO; GO:0035772; P:interleukin-13-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:2000426; P:negative regulation of apoptotic cell clearance; ISS:UniProtKB.
DR GO; GO:0033004; P:negative regulation of mast cell activation; ISS:UniProtKB.
DR GO; GO:0034125; P:negative regulation of MyD88-dependent toll-like receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030316; P:osteoclast differentiation; ISO:RGD.
DR GO; GO:2000427; P:positive regulation of apoptotic cell clearance; ISS:UniProtKB.
DR GO; GO:1902216; P:positive regulation of interleukin-4-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; ISS:UniProtKB.
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; Lipid-binding; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..332
FT /note="CMRF35-like molecule 1"
FT /id="PRO_0000247827"
FT TOPO_DOM 19..181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..125
FT /note="Ig-like V-type"
FT REGION 251..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 243
FT /note="Phosphatase-binding"
FT /evidence="ECO:0000250"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..109
FT /evidence="ECO:0000250|UniProtKB:Q6SJQ7"
FT DISULFID 55..63
FT /evidence="ECO:0000250|UniProtKB:Q6SJQ7"
SQ SEQUENCE 332 AA; 36823 MW; 7249D9D7EF5D67C0 CRC64;
MHLSLLALFL FWISGCFTAQ DPVTGPEEVS GYEQGSLTVW CRYGSWWKDY SKYWCRGPKR
SSCEIRVETD ASERLVKENH VSIRDDQTNF TFTVTMEDLR MSDAGIYWCG ITKAGYDHMF
KVHVSINPVP TTPTTTSTTT IFTVTTTVKE TSTLSTQTSH YSDNRYDSGG VGDGNGFLDL
SVLLPVISAA LLLLLLVVSL IAWRMVRRQK KAAGPPSGQA DSVTHILCPP KPHVQPLEDD
LCYANLSLQQ PRTSPLKKGS SMSSSGKDHQ EEVEYVTMAP FPREEISYAA LSLASLGQEP
TYSNTACLVT HGPRTNLGEE TTEYSSIRRP MP
