CLM8_MOUSE
ID CLM8_MOUSE Reviewed; 318 AA.
AC Q6SJQ0; B9EIB1; Q7TN56; Q7TSN3; Q8CFN3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=CMRF35-like molecule 8;
DE Short=CLM-8;
DE AltName: Full=CD300 antigen-like family member A;
DE AltName: Full=Leukocyte mono-Ig-like receptor 1;
DE AltName: Full=Mast cell-derived paired immunoglobulin-like receptor 1;
DE AltName: Full=Myeloid-associated immunoglobulin-like receptor 1;
DE Short=MAIR-1;
DE Short=MAIR-I;
DE AltName: CD_antigen=CD300a;
DE Flags: Precursor;
GN Name=Cd300a; Synonyms=Clm8, Lmir1, Mcpir1;
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH PTPN6; PTPN11
RP AND INPP5D.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, GLYCOSYLATION,
RP PHOSPHORYLATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF TYR-237.
RC TISSUE=Fetal liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Yoshimoto M., Sekine S., Yazaki M., Sawada M.;
RT "Molecular cloning of an NK inhibitory receptor-related gene expressed in a
RT mouse microglial cell line, Ra2.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16339535; DOI=10.4049/jimmunol.175.12.7989;
RA Bachelet I., Munitz A., Moretta A., Moretta L., Levi-Schaffer F.;
RT "The inhibitory receptor IRp60 (CD300a) is expressed and functional on
RT human mast cells.";
RL J. Immunol. 175:7989-7995(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-303, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
CC -!- FUNCTION: Inhibitory receptor which may contribute to the down-
CC regulation of cytolytic activity in natural killer (NK) cells, and to
CC the down-regulation of mast cell degranulation (PubMed:12874256,
CC PubMed:12893283, PubMed:16339535). Negatively regulates the Toll-like
CC receptor (TLR) signaling mediated by MYD88 but not TRIF through
CC activation of PTPN6 (By similarity). {ECO:0000250|UniProtKB:Q9UGN4,
CC ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283,
CC ECO:0000269|PubMed:16339535}.
CC -!- SUBUNIT: Upon tyrosine-phosphorylation, interacts with PTN6/SHP-1 and
CC PTPN11/SHP-2 and INPP5D. {ECO:0000269|PubMed:12893283}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12874256,
CC ECO:0000269|PubMed:12893283}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12874256, ECO:0000269|PubMed:12893283}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=b;
CC IsoId=Q6SJQ0-1; Sequence=Displayed;
CC Name=2; Synonyms=a;
CC IsoId=Q6SJQ0-2; Sequence=VSP_031608;
CC -!- TISSUE SPECIFICITY: Present on the surface of the majority of myeloid
CC cells and a subset of B-cells. Present on the surface of NK cells after
CC IL-12 stimulation. {ECO:0000269|PubMed:12874256,
CC ECO:0000269|PubMed:12893283, ECO:0000269|PubMed:16339535}.
CC -!- PTM: Phosphorylated on tyrosine. {ECO:0000269|PubMed:12874256,
CC ECO:0000269|PubMed:12893283}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12874256}.
CC -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
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DR EMBL; AB095675; BAC80268.1; -; mRNA.
DR EMBL; AB091765; BAC77074.1; -; mRNA.
DR EMBL; AB091766; BAC77075.1; -; mRNA.
DR EMBL; AY457054; AAR27945.1; -; mRNA.
DR EMBL; AB065156; BAC22595.1; -; mRNA.
DR EMBL; AK045869; BAC32515.1; -; mRNA.
DR EMBL; AL669969; CAM18755.1; -; Genomic_DNA.
DR EMBL; AL669969; CAM18756.1; -; Genomic_DNA.
DR EMBL; BC139296; AAI39297.1; -; mRNA.
DR EMBL; BC139297; AAI39298.1; -; mRNA.
DR CCDS; CCDS25613.1; -. [Q6SJQ0-1]
DR CCDS; CCDS83923.1; -. [Q6SJQ0-2]
DR RefSeq; NP_001334583.1; NM_001347654.1. [Q6SJQ0-2]
DR RefSeq; NP_739564.1; NM_170758.3. [Q6SJQ0-1]
DR AlphaFoldDB; Q6SJQ0; -.
DR SMR; Q6SJQ0; -.
DR BioGRID; 229881; 3.
DR STRING; 10090.ENSMUSP00000102192; -.
DR GlyGen; Q6SJQ0; 1 site.
DR iPTMnet; Q6SJQ0; -.
DR PhosphoSitePlus; Q6SJQ0; -.
DR MaxQB; Q6SJQ0; -.
DR PaxDb; Q6SJQ0; -.
DR PeptideAtlas; Q6SJQ0; -.
DR PRIDE; Q6SJQ0; -.
DR ProteomicsDB; 281643; -. [Q6SJQ0-1]
DR ProteomicsDB; 281644; -. [Q6SJQ0-2]
DR DNASU; 217303; -.
DR Ensembl; ENSMUST00000045151; ENSMUSP00000036773; ENSMUSG00000034652. [Q6SJQ0-2]
DR Ensembl; ENSMUST00000106582; ENSMUSP00000102192; ENSMUSG00000034652. [Q6SJQ0-1]
DR GeneID; 217303; -.
DR KEGG; mmu:217303; -.
DR UCSC; uc007mfy.1; mouse. [Q6SJQ0-1]
DR UCSC; uc007mfz.1; mouse. [Q6SJQ0-2]
DR CTD; 11314; -.
DR MGI; MGI:2443411; Cd300a.
DR VEuPathDB; HostDB:ENSMUSG00000034652; -.
DR eggNOG; ENOG502S7MA; Eukaryota.
DR GeneTree; ENSGT00940000163981; -.
DR HOGENOM; CLU_051023_0_0_1; -.
DR InParanoid; Q6SJQ0; -.
DR OMA; WRMIRRH; -.
DR OrthoDB; 1494510at2759; -.
DR PhylomeDB; Q6SJQ0; -.
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; 217303; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q6SJQ0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6SJQ0; protein.
DR Bgee; ENSMUSG00000034652; Expressed in granulocyte and 93 other tissues.
DR Genevisible; Q6SJQ0; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0019902; F:phosphatase binding; IPI:MGI.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; ISO:MGI.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0051649; P:establishment of localization in cell; IDA:MGI.
DR GO; GO:0043303; P:mast cell degranulation; IDA:MGI.
DR GO; GO:1902569; P:negative regulation of activation of Janus kinase activity; ISO:MGI.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; ISO:MGI.
DR GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; ISO:MGI.
DR GO; GO:1902567; P:negative regulation of eosinophil activation; ISO:MGI.
DR GO; GO:2000417; P:negative regulation of eosinophil migration; ISO:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; ISO:MGI.
DR GO; GO:0043305; P:negative regulation of mast cell degranulation; IDA:MGI.
DR GO; GO:0034125; P:negative regulation of MyD88-dependent toll-like receptor signaling pathway; ISO:MGI.
DR GO; GO:1902564; P:negative regulation of neutrophil activation; ISO:MGI.
DR GO; GO:0051134; P:negative regulation of NK T cell activation; ISO:MGI.
DR GO; GO:0060101; P:negative regulation of phagocytosis, engulfment; ISO:MGI.
DR GO; GO:0014063; P:negative regulation of serotonin secretion; IDA:MGI.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:MGI.
DR GO; GO:0050856; P:regulation of T cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0001820; P:serotonin secretion; IDA:MGI.
DR GO; GO:0002552; P:serotonin secretion by mast cell; 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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunity; Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..318
FT /note="CMRF35-like molecule 8"
FT /id="PRO_0000320132"
FT TOPO_DOM 28..185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..129
FT /note="Ig-like V-type"
FT REGION 139..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 303
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 142..145
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12874256"
FT /id="VSP_031608"
FT MUTAGEN 237
FT /note="Y->F: Abolishes internalization after cross-
FT linking."
FT /evidence="ECO:0000269|PubMed:12874256"
FT CONFLICT 35
FT /note="S -> T (in Ref. 1; BAC80268)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="E -> Q (in Ref. 1; BAC80268)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="R -> Q (in Ref. 1; BAC80268)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="V -> G (in Ref. 1; BAC80268)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="I -> V (in Ref. 1; BAC80268)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="E -> D (in Ref. 1; BAC80268)"
FT /evidence="ECO:0000305"
FT CONFLICT 118..126
FT /note="SLFDGSLGF -> PFFNAPLGL (in Ref. 1; BAC80268)"
FT /evidence="ECO:0000305"
FT CONFLICT 172..173
FT /note="GH -> DR (in Ref. 1; BAC80268)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="R -> G (in Ref. 3; AAR27945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 35629 MW; 490EDBD46AF0A7C6 CRC64;
MTQLASAVWL PTLLLLLLLF WLPGCVPLHG PSTMSGSVGE SLSVSCRYEE KFKTKDKYWC
RVSLKILCKD IVKTSSSEEA RSGRVTIRDH PDNLTFTVTY ESLTLEDADT YMCAVDISLF
DGSLGFDKYF KIELSVVPSE DPVSSPGPTL ETPVVSTSLP TKGPALGSNT EGHREHDYSQ
GLRLPALLSV LALLLFLLVG TSLLAWRMFQ KRLVKADRHP ELSQNLRQAS EQNECQYVNL
QLHTWSLREE PVLPSQVEVV EYSTLALPQE ELHYSSVAFN SQRQDSHANG DSLHQPQDQK
AEYSEIQKPR KGLSDLYL
