Leukosialin precursor - Mus musculus (Mouse)

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P15702 (LEUK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 112. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Leukosialin

Alternative name(s):
B-cell differentiation antigen LP-3
Leukocyte sialoglycoprotein
Lymphocyte antigen 48
Short name=Ly-48
Sialophorin
CD_antigen=CD43

Gene names

Name:

Spn

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	395 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	One of the major glycoproteins of thymocytes and T lymphocytes. Plays a role in the physicochemical properties of the T-cell surface and in lectin binding. Presents carbohydrate ligands to selectins. Has an extended rodlike structure that could protrude above the glycocalyx of the cell and allow multiple glycan chains to be accessible for binding. Is a counter-receptor for SN/Siglec-1. During T-cell activation is actively removed from the T-cell-APC (antigen-presenting cell) contact site thus suggesting a negative regulatory role in adaptive immune response. Ref.7
Subunit structure	Interacts with HIPK2 via the cytoplasmic domain. Interacts with RDX. Ref.5 Ref.6
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Cell surface of thymocytes, T-lymphocytes, neutrophils, plasma cells and myelomas.
Post-translational modification	Has a high content of sialic acid and O-linked carbohydrate structures.

Ontologies

Keywords
Cellular component	Membrane
Domain	Signal Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	T cell costimulation Inferred from direct assay PubMed 10429671 PubMed 11380685 PubMed 7790813. Source: MGI apoptotic signaling pathway Inferred from direct assay PubMed 10429671. Source: MGI cell surface receptor signaling pathway Inferred from direct assay PubMed 7790813. Source: MGI defense response to bacterium Inferred from mutant phenotype PubMed 10899905. Source: MGI negative regulation of T cell proliferation Inferred from mutant phenotype PubMed 15117976 PubMed 7566153 PubMed 9645617. Source: MGI negative regulation of cell adhesion Inferred from direct assay PubMed 11937524. Source: MGI negative regulation of type IV hypersensitivity Inferred from mutant phenotype PubMed 9645617. Source: MGI negative thymic T cell selection Inferred from mutant phenotype PubMed 10429671. Source: MGI positive regulation of T cell proliferation Inferred from direct assay PubMed 11380685 PubMed 7790813. Source: MGI positive regulation of tumor necrosis factor biosynthetic process Inferred from mutant phenotype PubMed 10899905. Source: MGI regulation of defense response to virus Inferred from mutant phenotype PubMed 7566153. Source: MGI response to protozoan Inferred from direct assay PubMed 11994475. Source: MGI
Cellular_component	basement membrane Inferred from direct assay Ref.3. Source: MGI external side of plasma membrane Inferred from direct assay PubMed 10943842 PubMed 11380685 Ref.7 PubMed 14635057 PubMed 15117976 PubMed 7477353 Ref.3 PubMed 7566153 PubMed 7790813 PubMed 7795661 PubMed 8920854 PubMed 9645617. Source: MGI extracellular space Inferred from electronic annotation. Source: Compara integral to plasma membrane Inferred from direct assay Ref.7 PubMed 11937524. Source: MGI uropod Inferred from direct assay Ref.7 PubMed 11937524. Source: MGI
Molecular_function	bacterial cell surface binding Inferred from mutant phenotype PubMed 10899905. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Chain

20 – 395

376

Leukosialin

PRO_0000021589

Regions

Topological domain

20 – 248

229

Extracellular Potential

Transmembrane

249 – 271

Helical; Potential

Topological domain

272 – 395

124

Cytoplasmic Potential

Amino acid modifications

Modified residue

285

Phosphoserine By similarity

Modified residue

343

Phosphoserine Ref.8 Ref.9

Modified residue

347

Phosphoserine Ref.8 Ref.9

Glycosylation

167

N-linked (GlcNAc...) Potential

Secondary structure

395

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P15702 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 369F201B04DBC055
Show »

FASTA

395

40,038

        10         20         30         40         50         60 
MALHLLLLFG ACWVQVASPD SLQRTTMLPS TPHITAPSTS EAQNASPSVS VGSGTVDSKE 

        70         80         90        100        110        120 
TISPWGQTTI PVSLTPLETT ELSSLETSAG ASMSTPVPEP TASQEVSSKT SALLPEPSNV 

       130        140        150        160        170        180 
ASDPPVTAAN PVTDGPAANP VTDGTAASTS ISKGTSAPPT TVTTSSNETS GPSVATTVSS 

       190        200        210        220        230        240 
KTSGPPVTTA TGSLGPSSEM HGLPATTATS SVESSSVARG TSVSSRKTST TSTQDPITTR 

       250        260        270        280        290        300 
SPSQESSGML LVPMLIALVV VLALVALLLL WRQRQKRRTG ALTLSGGGKR NGVVDAWAGP 

       310        320        330        340        350        360 
ARVPDEEATT TSGAGGNKGS EVLETEGSGQ RPTLTTFFSR RKSRQGSLVL EELKPGSGPN 

       370        380        390 
LKGEEEPLVG SEDEAVETPT SDGPQAKDEA APQSL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Protein sequence and gene structure for mouse leukosialin (CD43), a T lymphocyte mucin without introns in the coding sequence." Cyster J.G., Somoza C., Killeen N., Williams A.F. Eur. J. Immunol. 20:875-881(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DBA/2J. Tissue: Liver.
[2]	"The nucleotide sequence of Ly 48 (mouse leukosialin, sialophorin): the mouse homolog of CD43." Dorfman K.S., Litaker K.S., Baecher C.M., Frelinger J.G. Nucleic Acids Res. 18:4932-4932(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B10.P. Tissue: Liver.
[3]	"A unique murine CD43 epitope Lp-3: distinct distribution from another CD43 epitope S7." Shiota J., Nishimura H., Okamoto H., Yu B., Hattori S., Abe M., Okada T., Nozawa S., Tsurui H., Hirose S. Cell. Immunol. 155:402-413(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[4]	"cDNA cloning and localization of the mouse leukosialin gene (Ly48) to chromosome 7." Baecher C.M., Dorfman K.S., Mattei M.-G., Frelinger J.G. Immunogenetics 31:307-314(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 345-383. Strain: C57BL/6J.
[5]	"Identification and cloning of a CD43-associated serine/threonine kinase." Wang W., Link V., Green J.M. Cell. Immunol. 205:34-39(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIPK2.
[6]	"CD43 functions as a T cell counterreceptor for the macrophage adhesion receptor sialoadhesin (Siglec-1)." van den Berg T.K., Nath D., Ziltener H.J., Vestweber D., Fukuda M., van Die I., Crocker P.R. J. Immunol. 166:3637-3640(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SN.
[7]	"ERM-dependent movement of CD43 defines a novel protein complex distal to the immunological synapse." 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. Immunity 15:739-750(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"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 SER-343 AND SER-347, MASS SPECTROMETRY. Tissue: Macrophage.
[9]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-347, MASS SPECTROMETRY. Tissue: Melanoma.
[10]	"Structural basis of the cytoplasmic tail of adhesion molecule CD43 and its binding to ERM proteins." Takai Y., Kitano K., Terawaki S., Maesaki R., Hakoshima T. J. Mol. Biol. 381:634-644(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 272-291 IN COMPLEX WITH RDX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X17018 Genomic DNA. Translation: CAA34884.1.
X52609 Genomic DNA. Translation: CAA36840.1.
S70677 mRNA. Translation: AAB30765.1.
M30693 mRNA. Translation: AAA39457.1.

IPI

IPI00133646.

PIR

A43545.

RefSeq

NP_001032899.1. NM_001037810.1.
NP_033285.1. NM_009259.4.

UniGene

Mm.283714.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EMS	X-ray	2.90	B	272-291	[»]

ProteinModelPortal

P15702.

ModBase

Search...

Protein-protein interaction databases

STRING

10090.ENSMUSP00000049534.

PTM databases

PhosphoSite

P15702.

Proteomic databases

PaxDb

P15702.

PRIDE

P15702.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000049931; ENSMUSP00000049534; ENSMUSG00000051457.
ENSMUST00000143713; ENSMUSP00000122787; ENSMUSG00000051457.

GeneID

20737.

KEGG

mmu:20737.

Organism-specific databases

CTD

6693.

MGI

MGI:98384. Spn.

Phylogenomic databases

eggNOG

NOG47487.

HOGENOM

HOG000294199.

HOVERGEN

HBG006258.

InParanoid

P15702.

K06477.

OMA

GSLAMEE.

OrthoDB

EOG4KSPK7.

Gene expression databases

ArrayExpress

P15702.

Bgee

P15702.

CleanEx

MM_SPN.

Genevestigator

P15702.

GermOnline

ENSMUSG00000051457. Mus musculus.

Family and domain databases

ProtoNet

Search...

Other

EvolutionaryTrace

P15702.

NextBio

299365.

SOURCE

Search...

Entry information

Entry name

LEUK_MOUSE

Accession

Primary (citable) accession number: P15702

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	April 3, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents