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Signal transducer CD24 (Lymphocyte antigen 52) (Ly-52) (M1/69-J11D heat stable antigen) (HSA) (Nectadrin) (R13-Ag) (X62 heat stable antigen) (CD antigen CD24)

 CD24_MOUSE              Reviewed;          76 AA.
P24807; P26691;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 1.
22-NOV-2017, entry version 143.
RecName: Full=Signal transducer CD24;
AltName: Full=Lymphocyte antigen 52;
Short=Ly-52;
AltName: Full=M1/69-J11D heat stable antigen;
Short=HSA;
AltName: Full=Nectadrin;
AltName: Full=R13-Ag;
AltName: Full=X62 heat stable antigen;
AltName: CD_antigen=CD24;
Flags: Precursor;
Name=Cd24; Synonyms=Cd24a, Ly-52;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2118158;
Kay R., Takei F., Humphries R.K.;
"Expression cloning of a cDNA encoding M1/69-J11d heat-stable
antigens.";
J. Immunol. 145:1952-1959(1990).
[2]
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/6 X CBA, and Swiss albino X BALB/c; TISSUE=Spleen;
PubMed=2019286; DOI=10.1002/eji.1830210427;
Wenger R.H., Ayane M., Bose R., Koehler G., Nielsen P.J.;
"The genes for a mouse hematopoietic differentiation marker called the
heat-stable antigen.";
Eur. J. Immunol. 21:1039-1046(1991).
[3]
SEQUENCE REVISION.
Nielsen P.J.;
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6 X CBA; TISSUE=Spleen;
PubMed=8226859;
Wenger R.H., Rochelle J.M., Seldin M.F., Koehler G., Nielsen P.J.;
"The heat stable antigen (mouse CD24) gene is differentially regulated
but has a housekeeping promoter.";
J. Biol. Chem. 268:23345-23352(1993).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[6]
PROTEIN SEQUENCE OF 27-53, AND GLYCOSYLATION AT ASN-27; SER-30;
ASN-39; SER-41; SER-43; ASN-48 AND THR-51.
STRAIN=C57BL/6J;
PubMed=1530634; DOI=10.1016/0006-291X(92)91262-O;
Hitsumoto Y., Nakano A., Ohnishi H., Hamada F., Saheki S.,
Takeuchi N.;
"Purification of the murine heat-stable antigen from erythrocytes.";
Biochem. Biophys. Res. Commun. 187:773-777(1992).
[7]
FUNCTION, AND INTERACTION WITH SIGLEC10 AND HMGB1.
PubMed=19264983; DOI=10.1126/science.1168988;
Chen G.Y., Tang J., Zheng P., Liu Y.;
"CD24 and Siglec-10 selectively repress tissue damage-induced immune
responses.";
Science 323:1722-1725(2009).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20200274; DOI=10.4049/jimmunol.0902711;
Jellusova J., Wellmann U., Amann K., Winkler T.H., Nitschke L.;
"CD22 x Siglec-G double-deficient mice have massively increased B1
cell numbers and develop systemic autoimmunity.";
J. Immunol. 184:3618-3627(2010).
-!- FUNCTION: May have a pivotal role in cell differentiation of
different cell types. May have a specific role in early thymocyte
development. Signaling could be triggered by the binding of a
lectin-like ligand to the CD24 carbohydrates, and transduced by
the release of second messengers derived from the GPI-anchor.
Modulates B-cell activation responses (By similarity). In
association with SIGLEC10 may be involved in the selective
suppression of the immune response to danger-associated molecular
patterns (DAMPs) such as HMGB1, HSP70 and HSP90 (PubMed:19264983).
Plays a role in the control of autoimmunity (PubMed:20200274).
{ECO:0000250|UniProtKB:P25063, ECO:0000269|PubMed:19264983,
ECO:0000269|PubMed:20200274}.
-!- SUBUNIT: Interacts with SIGLEC10; the probable CD24:SIGLEC10
complex is proposed to inhibit HGMB1-mediated tissue damage immune
response. {ECO:0000269|PubMed:19264983}.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
-!- TISSUE SPECIFICITY: In lymphoid, myeloid, and erythroid cells.
-!- PTM: The identity of the N- and O-linked polysaccharides are not
reported in PubMed:1530634. The O-linked polysaccharides on Ser-
30, Ser-41, Ser-43, and Thr-51 are probably the mucin type linked
to GalNAc. {ECO:0000269|PubMed:1530634}.
-!- DISRUPTION PHENOTYPE: Cd22/Siglec10 double-deficient mice develop
autoimmune disease, which is not observed in single-deficient
mice. {ECO:0000269|PubMed:20200274}.
-!- SIMILARITY: Belongs to the CD24 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M58661; AAA39481.1; -; mRNA.
EMBL; X56469; CAA39841.1; -; Genomic_DNA.
EMBL; X72910; CAA51415.1; -; Genomic_DNA.
EMBL; X53825; CAA37822.1; -; mRNA.
EMBL; BC075622; AAH75622.1; -; mRNA.
CCDS; CCDS23821.1; -.
PIR; A43537; A43537.
RefSeq; NP_033976.1; NM_009846.2.
UniGene; Mm.29742; -.
STRING; 10090.ENSMUSP00000057983; -.
iPTMnet; P24807; -.
PaxDb; P24807; -.
PRIDE; P24807; -.
Ensembl; ENSMUST00000058714; ENSMUSP00000057983; ENSMUSG00000047139.
GeneID; 12484; -.
KEGG; mmu:12484; -.
UCSC; uc007ezl.1; mouse.
CTD; 12484; -.
MGI; MGI:88323; Cd24a.
eggNOG; ENOG410JF9E; Eukaryota.
eggNOG; ENOG4111B8V; LUCA.
GeneTree; ENSGT00390000018829; -.
HOVERGEN; HBG005274; -.
InParanoid; P24807; -.
KO; K06469; -.
OMA; QTSVAPF; -.
OrthoDB; EOG091G1CCU; -.
PhylomeDB; P24807; -.
TreeFam; TF338512; -.
PRO; PR:P24807; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000047139; -.
CleanEx; MM_CD24A; -.
ExpressionAtlas; P24807; baseline and differential.
Genevisible; P24807; MM.
GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0060170; C:ciliary membrane; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0031528; C:microvillus membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0045202; C:synapse; IEA:GOC.
GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
GO; GO:0030296; F:protein tyrosine kinase activator activity; ISS:UniProtKB.
GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:MGI.
GO; GO:0030262; P:apoptotic nuclear changes; IDA:MGI.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0032597; P:B cell receptor transport into membrane raft; ISS:UniProtKB.
GO; GO:0001775; P:cell activation; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
GO; GO:0032600; P:chemokine receptor transport out of membrane raft; IMP:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; IMP:UniProtKB.
GO; GO:0072139; P:glomerular parietal epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0072112; P:glomerular visceral epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:MGI.
GO; GO:0034109; P:homotypic cell-cell adhesion; IMP:MGI.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:MGI.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IMP:MGI.
GO; GO:0030889; P:negative regulation of B cell proliferation; IDA:MGI.
GO; GO:0034119; P:negative regulation of erythrocyte aggregation; IMP:MGI.
GO; GO:0034107; P:negative regulation of erythrocyte clearance; IMP:MGI.
GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:MGI.
GO; GO:0050768; P:negative regulation of neurogenesis; IMP:MGI.
GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
GO; GO:0046014; P:negative regulation of T cell homeostatic proliferation; IMP:MGI.
GO; GO:0032913; P:negative regulation of transforming growth factor beta3 production; ISS:UniProtKB.
GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
GO; GO:0031175; P:neuron projection development; IDA:MGI.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISS:UniProtKB.
GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IDA:MGI.
GO; GO:0002904; P:positive regulation of B cell apoptotic process; IDA:MGI.
GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:MGI.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IDA:MGI.
GO; GO:0022409; P:positive regulation of cell-cell adhesion; IDA:MGI.
GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; IDA:MGI.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:0002863; P:positive regulation of inflammatory response to antigenic stimulus; IMP:MGI.
GO; GO:0033625; P:positive regulation of integrin activation; IDA:MGI.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:2000768; P:positive regulation of nephron tubule epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; IDA:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0042103; P:positive regulation of T cell homeostatic proliferation; IMP:MGI.
GO; GO:0002842; P:positive regulation of T cell mediated immune response to tumor cell; IDA:MGI.
GO; GO:0002329; P:pre-B cell differentiation; IMP:MGI.
GO; GO:0045577; P:regulation of B cell differentiation; IMP:MGI.
GO; GO:0022407; P:regulation of cell-cell adhesion; IDA:MGI.
GO; GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; IDA:MGI.
GO; GO:0001959; P:regulation of cytokine-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0043408; P:regulation of MAPK cascade; ISS:UniProtKB.
GO; GO:0042325; P:regulation of phosphorylation; ISS:UniProtKB.
GO; GO:0045730; P:respiratory burst; ISS:UniProtKB.
GO; GO:0043627; P:response to estrogen; ISS:UniProtKB.
GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
GO; GO:0002237; P:response to molecule of bacterial origin; IDA:UniProtKB.
GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:MGI.
GO; GO:0031295; P:T cell costimulation; ISS:UniProtKB.
InterPro; IPR028029; CD24.
PANTHER; PTHR16676; PTHR16676; 1.
Pfam; PF14984; CD24; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
Glycoprotein; GPI-anchor; Immunity; Innate immunity; Lipoprotein;
Membrane; Reference proteome; Signal.
SIGNAL 1 26 {ECO:0000269|PubMed:1530634}.
PEPTIDE 27 53 Signal transducer CD24.
/FTId=PRO_0000020895.
PROPEP 54 76 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000020896.
SITE 45 45 Not glycosylated.
LIPID 53 53 GPI-anchor amidated glycine.
{ECO:0000255}.
CARBOHYD 27 27 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1530634}.
CARBOHYD 30 30 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:1530634}.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1530634}.
CARBOHYD 41 41 O-linked (GalNAc...) serine; partial.
{ECO:0000269|PubMed:1530634}.
CARBOHYD 43 43 O-linked (GalNAc...) serine; partial.
{ECO:0000269|PubMed:1530634}.
CARBOHYD 48 48 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1530634}.
CARBOHYD 51 51 O-linked (GalNAc...) threonine; partial.
{ECO:0000269|PubMed:1530634}.
SEQUENCE 76 AA; 7797 MW; 6853F121B33625EB CRC64;
MGRAMVARLG LGLLLLALLL PTQIYCNQTS VAPFPGNQNI SASPNPSNAT TRGGGSSLQS
TAGLLALSLS LLHLYC


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