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CMRF35-like molecule 8 (CLM-8) (CD300 antigen-like family member A) (CMRF-35-H9) (CMRF35-H9) (CMRF35-H) (IRC1/IRC2) (Immunoglobulin superfamily member 12) (IgSF12) (Inhibitory receptor protein 60) (IRp60) (NK inhibitory receptor) (CD antigen CD300a)

 CLM8_HUMAN              Reviewed;         299 AA.
Q9UGN4; A8MW96; O95100; Q9HD97; Q9P0F3; Q9UBK4; Q9UMS9; Q9UMT0;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 2.
25-OCT-2017, entry version 146.
RecName: Full=CMRF35-like molecule 8;
Short=CLM-8;
AltName: Full=CD300 antigen-like family member A;
AltName: Full=CMRF-35-H9;
Short=CMRF35-H9;
AltName: Full=CMRF35-H;
AltName: Full=IRC1/IRC2;
AltName: Full=Immunoglobulin superfamily member 12;
Short=IgSF12;
AltName: Full=Inhibitory receptor protein 60;
Short=IRp60;
AltName: Full=NK inhibitory receptor;
AltName: CD_antigen=CD300a;
Flags: Precursor;
Name=CD300A; Synonyms=CMRF35H, IGSF12; ORFNames=HSPC083;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
PHOSPHORYLATION.
TISSUE=Lymphoid tissue;
PubMed=10540326;
DOI=10.1002/(SICI)1521-4141(199910)29:10<3148::AID-IMMU3148>3.0.CO;2-L;
Cantoni C., Bottino C., Augugliaro R., Morelli L., Marcenaro E.,
Castriconi R., Vitale M., Pende D., Sivori S., Millo R., Biassoni R.,
Moretta L., Moretta A.;
"Molecular and functional characterization of IRp60, a member of the
immunoglobulin superfamily that functions as an inhibitory receptor in
human NK cells.";
Eur. J. Immunol. 29:3148-3159(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT GLN-111.
TISSUE=Lymphoid tissue;
Cantoni C., Biassoni R.;
"IRC1 isoforms.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=9701027; DOI=10.1093/intimm/10.7.891;
Green B.J., Clark G.J., Hart D.N.J.;
"The CMRF-35 mAb recognizes a second leukocyte membrane molecule with
a domain similar to the poly Ig receptor.";
Int. Immunol. 10:891-899(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=10746781; DOI=10.1034/j.1399-0039.2000.550201.x;
Clark G.J., Green B.J., Hart D.N.J.;
"The CMRF-35H gene structure predicts for an independently expressed
member of an ITIM/ITAM pair of molecules localized to human chromosome
17.";
Tissue Antigens 55:101-109(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Umbilical cord blood;
Zhang Q.H., Ye M., Zhou J., Shen Y., Wu X.Y., Guan Z.Q., Wang L.,
Fan H.Y., Mao Y.F., Dai M., Huang Q.H., Chen S.J., Chen Z.;
"Human partial CDS cloned from CD34+ stem cells.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
PubMed=16339535; DOI=10.4049/jimmunol.175.12.7989;
Bachelet I., Munitz A., Moretta A., Moretta L., Levi-Schaffer F.;
"The inhibitory receptor IRp60 (CD300a) is expressed and functional on
human mast cells.";
J. Immunol. 175:7989-7995(2005).
[9]
FUNCTION.
PubMed=22043923; DOI=10.1111/j.1365-2567.2011.03528.x;
Kim E.J., Lee S.M., Suk K., Lee W.H.;
"CD300a and CD300f differentially regulate the MyD88 and TRIF-mediated
TLR signalling pathways through activation of SHP-1 and/or SHP-2 in
human monocytic cell lines.";
Immunology 135:226-235(2012).
[10]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 19-128.
Dimasi N., Marquez J.A.;
"The crystal structure of IRp60 ectodomain.";
Submitted (JUN-2007) to the PDB data bank.
[11]
VARIANT GLN-111.
PubMed=12483297; DOI=10.1007/s00439-002-0851-y;
Speckman R.A., Wright Daw J.A., Helms C., Duan S., Cao L.,
Taillon-Miller P., Kwok P.Y., Menter A., Bowcock A.M.;
"Novel immunoglobulin superfamily gene cluster, mapping to a region of
human chromosome 17q25, linked to psoriasis susceptibility.";
Hum. Genet. 112:34-41(2003).
-!- FUNCTION: 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
(PubMed:10746781, PubMed:16339535, PubMed:9701027). Negatively
regulates the Toll-like receptor (TLR) signaling mediated by MYD88
but not TRIF through activation of PTPN6 (PubMed:22043923).
{ECO:0000269|PubMed:10746781, ECO:0000269|PubMed:16339535,
ECO:0000269|PubMed:22043923, ECO:0000269|PubMed:9701027}.
-!- SUBUNIT: Upon tyrosine-phosphorylation, interacts with PTN6/SHP-1
and PTPN11/SHP-2 and INPP5D. {ECO:0000250|UniProtKB:Q6SJQ0}.
-!- INTERACTION:
O76015:KRT38; NbExp=3; IntAct=EBI-10320732, EBI-1047263;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
type I membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=IRC1a;
IsoId=Q9UGN4-1; Sequence=Displayed;
Name=2; Synonyms=IRC1c;
IsoId=Q9UGN4-2; Sequence=VSP_010559;
Name=3; Synonyms=IRC1b;
IsoId=Q9UGN4-3; Sequence=VSP_010558;
Name=4;
IsoId=Q9UGN4-4; Sequence=VSP_010559, VSP_041246;
-!- TISSUE SPECIFICITY: Expressed not only by natural killer (NK)
cells but also by T-cell subsets, B-cells, dendritic cells, mast
cells, granulocytes and monocytes. {ECO:0000269|PubMed:10540326,
ECO:0000269|PubMed:16339535, ECO:0000269|PubMed:9701027}.
-!- PTM: Phosphorylated on tyrosine. {ECO:0000269|PubMed:10540326,
ECO:0000269|PubMed:16339535}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6SJQ0}.
-!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF28906.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAF28906.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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EMBL; AJ238323; CAB66145.1; -; mRNA.
EMBL; AJ010101; CAB52291.1; -; mRNA.
EMBL; AJ010102; CAB52292.1; -; mRNA.
EMBL; AJ010103; CAB52293.1; -; mRNA.
EMBL; AJ224864; CAB55347.1; -; mRNA.
EMBL; AF020314; AAD01646.1; -; mRNA.
EMBL; AF176991; AAF89957.1; -; Genomic_DNA.
EMBL; AF176985; AAF89957.1; JOINED; Genomic_DNA.
EMBL; AF176986; AAF89957.1; JOINED; Genomic_DNA.
EMBL; AF176987; AAF89957.1; JOINED; Genomic_DNA.
EMBL; AF176988; AAF89957.1; JOINED; Genomic_DNA.
EMBL; AF176989; AAF89957.1; JOINED; Genomic_DNA.
EMBL; AF176990; AAF89957.1; JOINED; Genomic_DNA.
EMBL; AF161346; AAF28906.1; ALT_SEQ; mRNA.
EMBL; AC079325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC032352; AAH32352.1; -; mRNA.
CCDS; CCDS32720.1; -. [Q9UGN4-1]
CCDS; CCDS58590.1; -. [Q9UGN4-2]
CCDS; CCDS82196.1; -. [Q9UGN4-4]
RefSeq; NP_001243770.1; NM_001256841.1. [Q9UGN4-2]
RefSeq; NP_001317386.1; NM_001330457.1. [Q9UGN4-4]
RefSeq; NP_009192.2; NM_007261.3. [Q9UGN4-1]
UniGene; Hs.9688; -.
PDB; 2Q87; X-ray; 1.70 A; A/B/C=19-125.
PDBsum; 2Q87; -.
ProteinModelPortal; Q9UGN4; -.
SMR; Q9UGN4; -.
BioGrid; 116445; 2.
IntAct; Q9UGN4; 3.
STRING; 9606.ENSP00000353259; -.
iPTMnet; Q9UGN4; -.
PhosphoSitePlus; Q9UGN4; -.
BioMuta; CD300A; -.
DMDM; 126302534; -.
EPD; Q9UGN4; -.
PaxDb; Q9UGN4; -.
PeptideAtlas; Q9UGN4; -.
PRIDE; Q9UGN4; -.
TopDownProteomics; Q9UGN4-1; -. [Q9UGN4-1]
Ensembl; ENST00000310828; ENSP00000308188; ENSG00000167851. [Q9UGN4-2]
Ensembl; ENST00000360141; ENSP00000353259; ENSG00000167851. [Q9UGN4-1]
Ensembl; ENST00000361933; ENSP00000354564; ENSG00000167851. [Q9UGN4-3]
Ensembl; ENST00000392625; ENSP00000376401; ENSG00000167851. [Q9UGN4-4]
GeneID; 11314; -.
KEGG; hsa:11314; -.
UCSC; uc002jkv.5; human. [Q9UGN4-1]
CTD; 11314; -.
DisGeNET; 11314; -.
EuPathDB; HostDB:ENSG00000167851.13; -.
GeneCards; CD300A; -.
HGNC; HGNC:19319; CD300A.
HPA; HPA011645; -.
MIM; 606790; gene.
neXtProt; NX_Q9UGN4; -.
OpenTargets; ENSG00000167851; -.
PharmGKB; PA142672149; -.
eggNOG; ENOG410IXT8; Eukaryota.
eggNOG; ENOG410ZH9V; LUCA.
GeneTree; ENSGT00470000042273; -.
HOVERGEN; HBG100050; -.
InParanoid; Q9UGN4; -.
KO; K06719; -.
OMA; AWRMFQK; -.
OrthoDB; EOG091G0RAD; -.
PhylomeDB; Q9UGN4; -.
TreeFam; TF334441; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-6798695; Neutrophil degranulation.
EvolutionaryTrace; Q9UGN4; -.
GeneWiki; CD300A; -.
GenomeRNAi; 11314; -.
PRO; PR:Q9UGN4; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000167851; -.
CleanEx; HS_CD300A; -.
ExpressionAtlas; Q9UGN4; baseline and differential.
Genevisible; Q9UGN4; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0008429; F:phosphatidylethanolamine binding; IDA:UniProtKB.
GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:1902569; P:negative regulation of activation of Janus kinase activity; IDA:UniProtKB.
GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:UniProtKB.
GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; IDA:UniProtKB.
GO; GO:1902567; P:negative regulation of eosinophil activation; IDA:UniProtKB.
GO; GO:2000417; P:negative regulation of eosinophil migration; IDA:UniProtKB.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; IDA:UniProtKB.
GO; GO:0043305; P:negative regulation of mast cell degranulation; IDA:UniProtKB.
GO; GO:0034125; P:negative regulation of MyD88-dependent toll-like receptor signaling pathway; IMP:UniProtKB.
GO; GO:1902564; P:negative regulation of neutrophil activation; IDA:UniProtKB.
GO; GO:0051134; P:negative regulation of NK T cell activation; IDA:UniProtKB.
GO; GO:0060101; P:negative regulation of phagocytosis, engulfment; IMP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IDA:UniProtKB.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 299 CMRF35-like molecule 8.
/FTId=PRO_0000014682.
TOPO_DOM 18 180 Extracellular. {ECO:0000255}.
TRANSMEM 181 201 Helical. {ECO:0000255}.
TOPO_DOM 202 299 Cytoplasmic. {ECO:0000255}.
DOMAIN 19 123 Ig-like V-type.
MOD_RES 293 293 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q6SJQ0}.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 103 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 14 209 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_010558.
VAR_SEQ 14 126 Missing (in isoform 2 and isoform 4).
{ECO:0000303|Ref.2, ECO:0000303|Ref.5}.
/FTId=VSP_010559.
VAR_SEQ 223 258 Missing (in isoform 4).
{ECO:0000303|Ref.5}.
/FTId=VSP_041246.
VARIANT 111 111 R -> Q (in dbSNP:rs2272111).
{ECO:0000269|PubMed:12483297,
ECO:0000269|Ref.2}.
/FTId=VAR_030797.
CONFLICT 28 29 VG -> W (in Ref. 3; AAD01646 and 4;
AAF89957). {ECO:0000305}.
CONFLICT 39 39 E -> Q (in Ref. 4; AAF89957).
{ECO:0000305}.
CONFLICT 189 189 L -> M (in Ref. 5; AAF28906).
{ECO:0000305}.
CONFLICT 193 193 L -> M (in Ref. 5; AAF28906).
{ECO:0000305}.
CONFLICT 209 209 K -> KWIK (in Ref. 3; AAD01646).
{ECO:0000305}.
CONFLICT 260 260 S -> F (in Ref. 5; AAF28906).
{ECO:0000305}.
STRAND 20 27 {ECO:0000244|PDB:2Q87}.
STRAND 32 37 {ECO:0000244|PDB:2Q87}.
HELIX 40 42 {ECO:0000244|PDB:2Q87}.
STRAND 45 51 {ECO:0000244|PDB:2Q87}.
STRAND 54 57 {ECO:0000244|PDB:2Q87}.
STRAND 61 66 {ECO:0000244|PDB:2Q87}.
STRAND 70 72 {ECO:0000244|PDB:2Q87}.
STRAND 75 80 {ECO:0000244|PDB:2Q87}.
HELIX 81 83 {ECO:0000244|PDB:2Q87}.
STRAND 85 92 {ECO:0000244|PDB:2Q87}.
HELIX 95 97 {ECO:0000244|PDB:2Q87}.
STRAND 99 106 {ECO:0000244|PDB:2Q87}.
STRAND 117 125 {ECO:0000244|PDB:2Q87}.
SEQUENCE 299 AA; 33201 MW; 978461DA87E86269 CRC64;
MWLPWALLLL WVPGCFALSK CRTVAGPVGG SLSVQCPYEK EHRTLNKYWC RPPQIFLCDK
IVETKGSAGK RNGRVSIRDS PANLSFTVTL ENLTEEDAGT YWCGVDTPWL RDFHDPVVEV
EVSVFPASTS MTPASITAAK TSTITTAFPP VSSTTLFAVG ATHSASIQEE TEEVVNSQLP
LLLSLLALLL LLLVGASLLA WRMFQKWIKA GDHSELSQNP KQAATQSELH YANLELLMWP
LQEKPAPPRE VEVEYSTVAS PREELHYASV VFDSNTNRIA AQRPREEEPD SDYSVIRKT


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