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Protein

CMRF35-like molecule 8

Gene

Cd300a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Inhibitory receptor which may contribute to the down-regulation of cytolytic activity in natural killer (NK) cells, and to the down-regulation of mast cell degranulation.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity

Enzyme and pathway databases

ReactomeiR-MMU-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

Names & Taxonomyi

Protein namesi
Recommended name:
CMRF35-like molecule 8
Short name:
CLM-8
Alternative name(s):
CD300 antigen-like family member A
Leukocyte mono-Ig-like receptor 1
Mast cell-derived paired immunoglobulin-like receptor 1
Myeloid-associated immunoglobulin-like receptor 1
Short name:
MAIR-1
Short name:
MAIR-I
CD_antigen: CD300a
Gene namesi
Name:Cd300a
Synonyms:Clm8, Lmir1, Mcpir1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2443411. Cd300a.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 185158ExtracellularSequence analysisAdd
BLAST
Transmembranei186 – 20621HelicalSequence analysisAdd
BLAST
Topological domaini207 – 318112CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • mast cell granule Source: GOC
  • membrane Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi237 – 2371Y → F: Abolishes internalization after cross-linking. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence analysisAdd
BLAST
Chaini28 – 318291CMRF35-like molecule 8PRO_0000320132Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 113PROSITE-ProRule annotation
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence analysis
Modified residuei303 – 3031PhosphotyrosineCombined sources

Post-translational modificationi

Phosphorylated on tyrosine.2 Publications
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ6SJQ0.
PaxDbiQ6SJQ0.
PRIDEiQ6SJQ0.

PTM databases

iPTMnetiQ6SJQ0.

Expressioni

Tissue specificityi

Present on the surface of the majority of myeloid cells and a subset of B-cells. Present on the surface of NK cells after IL-12 stimulation.3 Publications

Gene expression databases

BgeeiQ6SJQ0.
CleanExiMM_CD300A.
GenevisibleiQ6SJQ0. MM.

Interactioni

Subunit structurei

Upon tyrosine-phosphorylation, interacts with PTN6/SHP-1 and PTPN11/SHP-2 and INPP5D.1 Publication

Protein-protein interaction databases

BioGridi229881. 3 interactions.
STRINGi10090.ENSMUSP00000102192.

Structurei

3D structure databases

ProteinModelPortaliQ6SJQ0.
SMRiQ6SJQ0. Positions 33-116.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 129102Ig-like V-typeAdd
BLAST

Sequence similaritiesi

Belongs to the CD300 family.Curated

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IXT8. Eukaryota.
ENOG410ZH9V. LUCA.
GeneTreeiENSGT00470000042273.
HOGENOMiHOG000231065.
HOVERGENiHBG100050.
InParanoidiQ6SJQ0.
KOiK06719.
OMAiYSVIRKT.
OrthoDBiEOG7FFMST.
PhylomeDBiQ6SJQ0.
TreeFamiTF334441.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6SJQ0-1) [UniParc]FASTAAdd to basket

Also known as: b

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTQLASAVWL PTLLLLLLLF WLPGCVPLHG PSTMSGSVGE SLSVSCRYEE
60 70 80 90 100
KFKTKDKYWC RVSLKILCKD IVKTSSSEEA RSGRVTIRDH PDNLTFTVTY
110 120 130 140 150
ESLTLEDADT YMCAVDISLF DGSLGFDKYF KIELSVVPSE DPVSSPGPTL
160 170 180 190 200
ETPVVSTSLP TKGPALGSNT EGHREHDYSQ GLRLPALLSV LALLLFLLVG
210 220 230 240 250
TSLLAWRMFQ KRLVKADRHP ELSQNLRQAS EQNECQYVNL QLHTWSLREE
260 270 280 290 300
PVLPSQVEVV EYSTLALPQE ELHYSSVAFN SQRQDSHANG DSLHQPQDQK
310
AEYSEIQKPR KGLSDLYL
Length:318
Mass (Da):35,629
Last modified:February 26, 2008 - v2
Checksum:i490EDBD46AF0A7C6
GO
Isoform 2 (identifier: Q6SJQ0-2) [UniParc]FASTAAdd to basket

Also known as: a

The sequence of this isoform differs from the canonical sequence as follows:
     142-145: Missing.

Show »
Length:314
Mass (Da):35,259
Checksum:iDEFF9509C3A1222D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351S → T in BAC80268 (PubMed:12893283).Curated
Sequence conflicti40 – 401E → Q in BAC80268 (PubMed:12893283).Curated
Sequence conflicti47 – 471R → Q in BAC80268 (PubMed:12893283).Curated
Sequence conflicti62 – 621V → G in BAC80268 (PubMed:12893283).Curated
Sequence conflicti66 – 661I → V in BAC80268 (PubMed:12893283).Curated
Sequence conflicti106 – 1061E → D in BAC80268 (PubMed:12893283).Curated
Sequence conflicti118 – 1269SLFDGSLGF → PFFNAPLGL in BAC80268 (PubMed:12893283).Curated
Sequence conflicti172 – 1732GH → DR in BAC80268 (PubMed:12893283).Curated
Sequence conflicti218 – 2181R → G in AAR27945 (PubMed:14662855).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei142 – 1454Missing in isoform 2. 1 PublicationVSP_031608

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB095675 mRNA. Translation: BAC80268.1.
AB091765 mRNA. Translation: BAC77074.1.
AB091766 mRNA. Translation: BAC77075.1.
AY457054 mRNA. Translation: AAR27945.1.
AB065156 mRNA. Translation: BAC22595.1.
AK045869 mRNA. Translation: BAC32515.1.
AL669969 Genomic DNA. Translation: CAM18755.1.
AL669969 Genomic DNA. Translation: CAM18756.1.
BC139296 mRNA. Translation: AAI39297.1.
BC139297 mRNA. Translation: AAI39298.1.
CCDSiCCDS25613.1. [Q6SJQ0-1]
RefSeqiNP_739564.1. NM_170758.3. [Q6SJQ0-1]
XP_006533133.1. XM_006533070.2. [Q6SJQ0-2]
UniGeneiMm.294439.

Genome annotation databases

EnsembliENSMUST00000045151; ENSMUSP00000036773; ENSMUSG00000034652. [Q6SJQ0-2]
ENSMUST00000106582; ENSMUSP00000102192; ENSMUSG00000034652. [Q6SJQ0-1]
GeneIDi217303.
KEGGimmu:217303.
UCSCiuc007mfy.1. mouse. [Q6SJQ0-1]
uc007mfz.1. mouse. [Q6SJQ0-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB095675 mRNA. Translation: BAC80268.1.
AB091765 mRNA. Translation: BAC77074.1.
AB091766 mRNA. Translation: BAC77075.1.
AY457054 mRNA. Translation: AAR27945.1.
AB065156 mRNA. Translation: BAC22595.1.
AK045869 mRNA. Translation: BAC32515.1.
AL669969 Genomic DNA. Translation: CAM18755.1.
AL669969 Genomic DNA. Translation: CAM18756.1.
BC139296 mRNA. Translation: AAI39297.1.
BC139297 mRNA. Translation: AAI39298.1.
CCDSiCCDS25613.1. [Q6SJQ0-1]
RefSeqiNP_739564.1. NM_170758.3. [Q6SJQ0-1]
XP_006533133.1. XM_006533070.2. [Q6SJQ0-2]
UniGeneiMm.294439.

3D structure databases

ProteinModelPortaliQ6SJQ0.
SMRiQ6SJQ0. Positions 33-116.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229881. 3 interactions.
STRINGi10090.ENSMUSP00000102192.

PTM databases

iPTMnetiQ6SJQ0.

Proteomic databases

MaxQBiQ6SJQ0.
PaxDbiQ6SJQ0.
PRIDEiQ6SJQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045151; ENSMUSP00000036773; ENSMUSG00000034652. [Q6SJQ0-2]
ENSMUST00000106582; ENSMUSP00000102192; ENSMUSG00000034652. [Q6SJQ0-1]
GeneIDi217303.
KEGGimmu:217303.
UCSCiuc007mfy.1. mouse. [Q6SJQ0-1]
uc007mfz.1. mouse. [Q6SJQ0-2]

Organism-specific databases

CTDi11314.
MGIiMGI:2443411. Cd300a.

Phylogenomic databases

eggNOGiENOG410IXT8. Eukaryota.
ENOG410ZH9V. LUCA.
GeneTreeiENSGT00470000042273.
HOGENOMiHOG000231065.
HOVERGENiHBG100050.
InParanoidiQ6SJQ0.
KOiK06719.
OMAiYSVIRKT.
OrthoDBiEOG7FFMST.
PhylomeDBiQ6SJQ0.
TreeFamiTF334441.

Enzyme and pathway databases

ReactomeiR-MMU-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

Miscellaneous databases

NextBioi375729.
PROiQ6SJQ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ6SJQ0.
CleanExiMM_CD300A.
GenevisibleiQ6SJQ0. MM.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a new pair of immunoglobulin-like receptors LMIR1 and 2 derived from murine bone marrow-derived mast cells."
    Kumagai H., Oki T., Tamitsu K., Feng S.-Z., Ono M., Nakajima H., Bao Y.-C., Kawakami Y., Nagayoshi K., Copeland N.G., Gilbert D.J., Jenkins N.A., Kawakami T., Kitamura T.
    Biochem. Biophys. Res. Commun. 307:719-729(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH PTPN6; PTPN11 AND INPP5D.
    Strain: CBA/J.
    Tissue: Mast cell.
  2. "Paired activating and inhibitory immunoglobulin-like receptors, MAIR-I and MAIR-II, regulate mast cell and macrophage activation."
    Yotsumoto K., Okoshi Y., Shibuya K., Yamazaki S., Tahara-Hanaoka S., Honda S., Osawa M., Kuroiwa A., Matsuda Y., Tenen D.G., Iwama A., Nakauchi H., Shibuya A.
    J. Exp. Med. 198:223-233(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, GLYCOSYLATION, PHOSPHORYLATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-237.
    Tissue: Fetal liver.
  3. "CMRF-35-like molecule-1, a novel mouse myeloid receptor, can inhibit osteoclast formation."
    Chung D.-H., Humphrey M.B., Nakamura M.C., Ginzinger D.G., Seaman W.E., Daws M.R.
    J. Immunol. 171:6541-6548(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  4. "Molecular cloning of an NK inhibitory receptor-related gene expressed in a mouse microglial cell line, Ra2."
    Yoshimoto M., Sekine S., Yazaki M., Sawada M.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  8. "The inhibitory receptor IRp60 (CD300a) is expressed and functional on human mast cells."
    Bachelet I., Munitz A., Moretta A., Moretta L., Levi-Schaffer F.
    J. Immunol. 175:7989-7995(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  9. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-303, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCLM8_MOUSE
AccessioniPrimary (citable) accession number: Q6SJQ0
Secondary accession number(s): B9EIB1
, Q7TN56, Q7TSN3, Q8CFN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: January 20, 2016
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.