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Leukosialin (B-cell differentiation antigen LP-3) (Leukocyte sialoglycoprotein) (Lymphocyte antigen 48) (Ly-48) (Sialophorin) (CD antigen CD43)

 LEUK_MOUSE              Reviewed;         395 AA.
P15702;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
05-DEC-2018, entry version 157.
RecName: Full=Leukosialin;
AltName: Full=B-cell differentiation antigen LP-3;
AltName: Full=Leukocyte sialoglycoprotein;
AltName: Full=Lymphocyte antigen 48;
Short=Ly-48;
AltName: Full=Sialophorin;
AltName: CD_antigen=CD43;
Contains:
RecName: Full=CD43 cytoplasmic tail {ECO:0000303|PubMed:19696198};
Short=CD43-ct {ECO:0000303|PubMed:19696198};
Short=CD43ct {ECO:0000303|PubMed:19696198};
Flags: Precursor;
Name=Spn;
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 [GENOMIC DNA].
STRAIN=DBA/2J; TISSUE=Liver;
PubMed=2347365; DOI=10.1002/eji.1830200424;
Cyster J.G., Somoza C., Killeen N., Williams A.F.;
"Protein sequence and gene structure for mouse leukosialin (CD43), a T
lymphocyte mucin without introns in the coding sequence.";
Eur. J. Immunol. 20:875-881(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=B10.P; TISSUE=Liver;
PubMed=2144340; DOI=10.1093/nar/18.16.4932;
Dorfman K.S., Litaker K.S., Baecher C.M., Frelinger J.G.;
"The nucleotide sequence of Ly 48 (mouse leukosialin, sialophorin):
the mouse homolog of CD43.";
Nucleic Acids Res. 18:4932-4932(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=7514104; DOI=10.1006/cimm.1994.1133;
Shiota J., Nishimura H., Okamoto H., Yu B., Hattori S., Abe M.,
Okada T., Nozawa S., Tsurui H., Hirose S.;
"A unique murine CD43 epitope Lp-3: distinct distribution from another
CD43 epitope S7.";
Cell. Immunol. 155:402-413(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 345-383.
STRAIN=C57BL/6J;
PubMed=1973410; DOI=10.1007/BF02115004;
Baecher C.M., Dorfman K.S., Mattei M.-G., Frelinger J.G.;
"cDNA cloning and localization of the mouse leukosialin gene (Ly48) to
chromosome 7.";
Immunogenetics 31:307-314(1990).
[5]
INTERACTION WITH HIPK2.
PubMed=11078605; DOI=10.1006/cimm.2000.1716;
Wang W., Link V., Green J.M.;
"Identification and cloning of a CD43-associated serine/threonine
kinase.";
Cell. Immunol. 205:34-39(2000).
[6]
FUNCTION, AND INTERACTION WITH SIGLEC1.
PubMed=11238599; DOI=10.4049/jimmunol.166.6.3637;
van den Berg T.K., Nath D., Ziltener H.J., Vestweber D., Fukuda M.,
van Die I., Crocker P.R.;
"CD43 functions as a T cell counterreceptor for the macrophage
adhesion receptor sialoadhesin (Siglec-1).";
J. Immunol. 166:3637-3640(2001).
[7]
FUNCTION.
PubMed=11728336; DOI=10.1016/S1074-7613(01)00224-2;
Allenspach E.J., Cullinan P., Tong J., Tang Q., Tesciuba A.G.,
Cannon J.L., Takahashi S.M., Morgan R., Burkhardt J.K., Sperling A.I.;
"ERM-dependent movement of CD43 defines a novel protein complex distal
to the immunological synapse.";
Immunity 15:739-750(2001).
[8]
FUNCTION, PHOSPHORYLATION AT SER-343 AND SER-347, AND MUTAGENESIS OF
SER-343 AND SER-347.
PubMed=17638845; DOI=10.1182/blood-2007-01-065276;
Mody P.D., Cannon J.L., Bandukwala H.S., Blaine K.M., Schilling A.B.,
Swier K., Sperling A.I.;
"Signaling through CD43 regulates CD4 T-cell trafficking.";
Blood 110:2974-2982(2007).
[9]
FUNCTION.
PubMed=18490738;
Cannon J.L., Collins A., Mody P.D., Balachandran D., Henriksen K.J.,
Smith C.E., Tong J., Clay B.S., Miller S.D., Sperling A.I.;
"CD43 regulates Th2 differentiation and inflammation.";
J. Immunol. 180:7385-7393(2008).
[10]
FUNCTION, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, AND
SUMOYLATION.
PubMed=19696198; DOI=10.1182/blood-2009-06-228791;
Seo W., Ziltener H.J.;
"CD43 processing and nuclear translocation of CD43 cytoplasmic tail
are required for cell homeostasis.";
Blood 114:3567-3577(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339; SER-343; SER-347;
SER-371 AND THR-378, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
FUNCTION, PHOSPHORYLATION AT SER-347, MUTAGENESIS OF SER-347 AND
276-LYS--ARG-278, SUBCELLULAR LOCATION, AND INTERACTION WITH EZR.
PubMed=21289089; DOI=10.1091/mbc.E10-07-0586;
Cannon J.L., Mody P.D., Blaine K.M., Chen E.J., Nelson A.D.,
Sayles L.J., Moore T.V., Clay B.S., Dulin N.O., Shilling R.A.,
Burkhardt J.K., Sperling A.I.;
"CD43 interaction with ezrin-radixin-moesin (ERM) proteins regulates
T-cell trafficking and CD43 phosphorylation.";
Mol. Biol. Cell 22:954-963(2011).
[13]
FUNCTION.
PubMed=26700769; DOI=10.4049/jimmunol.1501171;
Velazquez F., Grodecki-Pena A., Knapp A., Salvador A.M., Nevers T.,
Croce K., Alcaide P.;
"CD43 functions as an E-selectin ligand for Th17 cells in vitro and is
required for rolling on the vascular endothelium and Th17 cell
recruitment during inflammation in vivo.";
J. Immunol. 196:1305-1316(2016).
[14]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 272-291 IN COMPLEX WITH RDX.
PubMed=18614175; DOI=10.1016/j.jmb.2008.05.085;
Takai Y., Kitano K., Terawaki S., Maesaki R., Hakoshima T.;
"Structural basis of the cytoplasmic tail of adhesion molecule CD43
and its binding to ERM proteins.";
J. Mol. Biol. 381:634-644(2008).
-!- FUNCTION: Predominant cell surface sialoprotein of leukocytes
which regulates multiple T-cell functions, including T-cell
activation, proliferation, differentiation, trafficking and
migration. Positively regulates T-cell trafficking to lymph-nodes
via its association with ERM proteins (EZR, RDX and MSN)
(PubMed:17638845, PubMed:21289089, PubMed:11728336). Negatively
regulates Th2 cell differentiation and predisposes the
differentiation of T-cells towards a Th1 lineage commitment
(PubMed:18490738). Promotes the expression of IFN-gamma by T-cells
during T-cell receptor (TCR) activation of naive cells and induces
the expression of IFN-gamma by CD4(+) T-cells and to a lesser
extent by CD8(+) T-cells. Plays a role in preparing T-cells for
cytokine sensing and differentiation into effector cells by
inducing the expression of cytokine receptors IFNGR and IL4R,
promoting IFNGR and IL4R signaling and by mediating the clustering
of IFNGR with TCR (By similarity). Acts as a major E-selectin
ligand responsible for Th17 cell rolling on activated vasculature
and recruitment during inflammation. Mediates Th17 cells, but not
Th1 cells, adhesion to E-selectin (PubMed:26700769). Acts as a T-
cell counter-receptor for SIGLEC1 (PubMed:11238599).
{ECO:0000250|UniProtKB:P16150, ECO:0000269|PubMed:11238599,
ECO:0000269|PubMed:11728336, ECO:0000269|PubMed:17638845,
ECO:0000269|PubMed:18490738, ECO:0000269|PubMed:21289089,
ECO:0000269|PubMed:26700769}.
-!- FUNCTION: CD43 cytoplasmic tail: Protects cells from apoptotic
signals, promoting cell survival. {ECO:0000269|PubMed:19696198}.
-!- SUBUNIT: Interacts with HIPK2 via the cytoplasmic domain
(PubMed:11078605). Interacts with SIGLEC1 (PubMed:11238599).
Interacts with RDX (PubMed:18614175). Interacts with EZR
(PubMed:21289089). Interacts with MSN (By similarity).
{ECO:0000250|UniProtKB:P13838, ECO:0000269|PubMed:11078605,
ECO:0000269|PubMed:11238599, ECO:0000269|PubMed:18614175,
ECO:0000269|PubMed:21289089}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
membrane protein {ECO:0000255}. Cell projection, microvillus
{ECO:0000250|UniProtKB:P13838}. Cell projection, uropodium
{ECO:0000269|PubMed:21289089}. Note=Localizes to the uropodium and
microvilli via its interaction with ERM proteins (EZR, RDX and
MSN). {ECO:0000250|UniProtKB:P13838, ECO:0000269|PubMed:21289089}.
-!- SUBCELLULAR LOCATION: CD43 cytoplasmic tail: Nucleus
{ECO:0000269|PubMed:19696198}. Nucleus, PML body
{ECO:0000269|PubMed:19696198}.
-!- TISSUE SPECIFICITY: Cell surface of thymocytes, T-lymphocytes,
neutrophils, plasma cells and myelomas.
-!- PTM: Phosphorylation at Ser-347 is regulated by chemokines,
requires its association with ERM proteins (EZR, RDX and MSN) and
is essential for its function in the regulation of T-cell
trafficking to lymph nodes. {ECO:0000269|PubMed:17638845,
ECO:0000269|PubMed:21289089}.
-!- PTM: Has a high content of sialic acid and O-linked carbohydrate
structures.
-!- PTM: Cleavage by CTSG releases its extracellular domain and
triggers its intramembrane proteolysis by gamma-secretase
releasing the CD43 cytoplasmic tail chain (CD43-ct) which
translocates to the nucleus. {ECO:0000269|PubMed:19696198}.
-!- PTM: CD43 cytoplasmic tail: Sumoylated.
{ECO:0000269|PubMed:19696198}.
-----------------------------------------------------------------------
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EMBL; X17018; CAA34884.1; -; Genomic_DNA.
EMBL; X52609; CAA36840.1; -; Genomic_DNA.
EMBL; S70677; AAB30765.1; -; mRNA.
EMBL; M30693; AAA39457.1; -; mRNA.
CCDS; CCDS21858.1; -.
PIR; A43545; A43545.
RefSeq; NP_001032899.1; NM_001037810.2.
RefSeq; NP_033285.1; NM_009259.5.
RefSeq; XP_006507585.1; XM_006507522.3.
UniGene; Mm.283714; -.
PDB; 2EMS; X-ray; 2.90 A; B=272-291.
PDBsum; 2EMS; -.
ProteinModelPortal; P15702; -.
SMR; P15702; -.
STRING; 10090.ENSMUSP00000049534; -.
iPTMnet; P15702; -.
PhosphoSitePlus; P15702; -.
EPD; P15702; -.
PaxDb; P15702; -.
PeptideAtlas; P15702; -.
PRIDE; P15702; -.
Ensembl; ENSMUST00000049931; ENSMUSP00000049534; ENSMUSG00000051457.
Ensembl; ENSMUST00000143713; ENSMUSP00000122787; ENSMUSG00000051457.
GeneID; 20737; -.
KEGG; mmu:20737; -.
UCSC; uc009juh.2; mouse.
CTD; 6693; -.
MGI; MGI:98384; Spn.
eggNOG; ENOG410J161; Eukaryota.
eggNOG; ENOG410YXQE; LUCA.
GeneTree; ENSGT00390000017626; -.
HOGENOM; HOG000294199; -.
HOVERGEN; HBG006258; -.
InParanoid; P15702; -.
KO; K06477; -.
OMA; DVTWGPS; -.
OrthoDB; EOG091G0MEV; -.
PhylomeDB; P15702; -.
TreeFam; TF337688; -.
Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
Reactome; R-MMU-210991; Basigin interactions.
EvolutionaryTrace; P15702; -.
PRO; PR:P15702; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000051457; Expressed in 206 organ(s), highest expression level in mesenteric lymph node.
CleanEx; MM_SPN; -.
ExpressionAtlas; P15702; baseline and differential.
Genevisible; P15702; MM.
GO; GO:0005604; C:basement membrane; IDA:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0032154; C:cleavage furrow; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005902; C:microvillus; ISS:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0001931; C:uropod; IDA:UniProtKB.
GO; GO:0031072; F:heat shock protein binding; IPI:CAFA.
GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
GO; GO:0032609; P:interferon-gamma production; ISS:UniProtKB.
GO; GO:0050901; P:leukocyte tethering or rolling; IMP:UniProtKB.
GO; GO:0007162; P:negative regulation of cell adhesion; IDA:MGI.
GO; GO:0050868; P:negative regulation of T cell activation; IMP:MGI.
GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:UniProtKB.
GO; GO:0001808; P:negative regulation of type IV hypersensitivity; IMP:MGI.
GO; GO:0045060; P:negative thymic T cell selection; IMP:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IGI:MGI.
GO; GO:2000406; P:positive regulation of T cell migration; IMP:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:MGI.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IMP:MGI.
GO; GO:0050688; P:regulation of defense response to virus; IMP:MGI.
GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
GO; GO:0050776; P:regulation of immune response; IMP:MGI.
GO; GO:2000404; P:regulation of T cell migration; IMP:UniProtKB.
GO; GO:0001562; P:response to protozoan; IDA:MGI.
GO; GO:0031295; P:T cell costimulation; IDA:MGI.
GO; GO:0050852; P:T cell receptor signaling pathway; ISO:MGI.
GO; GO:0002296; P:T-helper 1 cell lineage commitment; ISS:UniProtKB.
GO; GO:0071594; P:thymocyte aggregation; ISO:MGI.
InterPro; IPR038829; Leukosialin.
PANTHER; PTHR35265; PTHR35265; 1.
1: Evidence at protein level;
3D-structure; Cell projection; Complete proteome;
Direct protein sequencing; Glycoprotein; Membrane; Nucleus;
Phosphoprotein; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 19
CHAIN 20 395 Leukosialin.
/FTId=PRO_0000021589.
CHAIN 272 395 CD43 cytoplasmic tail.
{ECO:0000305|PubMed:19696198}.
/FTId=PRO_0000443407.
TOPO_DOM 20 248 Extracellular. {ECO:0000255}.
TRANSMEM 249 271 Helical. {ECO:0000255}.
TOPO_DOM 272 395 Cytoplasmic. {ECO:0000255}.
REGION 272 302 Required for interaction with EZR, MSN
and RDX and for co-localization to
microvilli.
{ECO:0000250|UniProtKB:P13838}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000250|UniProtKB:P16150}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000250|UniProtKB:P16150}.
MOD_RES 333 333 Phosphothreonine.
{ECO:0000250|UniProtKB:P16150}.
MOD_RES 339 339 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:17638845}.
MOD_RES 347 347 Phosphoserine; by PKC/PRKCQ.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:21289089}.
MOD_RES 371 371 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 378 378 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 167 167 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 276 278 KRR->NGG: Loss of phosphorylation,
interaction with EZR and localization to
the uropodium.
{ECO:0000269|PubMed:21289089}.
MUTAGEN 343 343 S->A: Reduced phosphorylation.
Significant loss of phosphorylation; when
associated with A-347.
{ECO:0000269|PubMed:17638845}.
MUTAGEN 347 347 S->A: Reduced phosphorylation.
Significant loss of phosphorylation; when
associated with A-343.
{ECO:0000269|PubMed:17638845,
ECO:0000269|PubMed:21289089}.
MUTAGEN 347 347 S->D: No loss of phosphorylation or
localization to the uropodium. Loss of
interaction with EZR.
{ECO:0000269|PubMed:21289089}.
STRAND 280 283 {ECO:0000244|PDB:2EMS}.
TURN 285 288 {ECO:0000244|PDB:2EMS}.
SEQUENCE 395 AA; 40038 MW; 369F201B04DBC055 CRC64;
MALHLLLLFG ACWVQVASPD SLQRTTMLPS TPHITAPSTS EAQNASPSVS VGSGTVDSKE
TISPWGQTTI PVSLTPLETT ELSSLETSAG ASMSTPVPEP TASQEVSSKT SALLPEPSNV
ASDPPVTAAN PVTDGPAANP VTDGTAASTS ISKGTSAPPT TVTTSSNETS GPSVATTVSS
KTSGPPVTTA TGSLGPSSEM HGLPATTATS SVESSSVARG TSVSSRKTST TSTQDPITTR
SPSQESSGML LVPMLIALVV VLALVALLLL WRQRQKRRTG ALTLSGGGKR NGVVDAWAGP
ARVPDEEATT TSGAGGNKGS EVLETEGSGQ RPTLTTFFSR RKSRQGSLVL EELKPGSGPN
LKGEEEPLVG SEDEAVETPT SDGPQAKDEA APQSL


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