Leukosialin precursor - Homo sapiens (Human)

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P16150 (LEUK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 111. History...

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

Documents (5) |

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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):
Galactoglycoprotein
Short name=GALGP
Leukocyte sialoglycoprotein
Sialophorin
CD_antigen=CD43

Gene names

Name:	SPN
Synonyms:	CD43

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	400 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 By similarity. 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 By similarity.
Subunit structure	Interacts with HIPK2 via the cytoplasmic domain. Interacts with RDX By similarity.
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	Glycosylated; has a high content of sialic acid and O-linked carbohydrate structures. Ref.6

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation Traceable author statement. Source: Reactome cellular defense response Traceable author statement. Source: ProtInc chemotaxis Traceable author statement. Source: ProtInc defense response to bacterium Inferred from direct assay. Source: MGI establishment or maintenance of cell polarity Traceable author statement. Source: ProtInc immune response Traceable author statement. Source: ProtInc leukocyte migration Traceable author statement. Source: Reactome negative regulation of cell adhesion Traceable author statement. Source: ProtInc positive regulation of tumor necrosis factor biosynthetic process Inferred from direct assay. Source: MGI
Cellular component	extracellular space Inferred from direct assay. Source: MGI integral to plasma membrane Traceable author statement. Source: ProtInc
Molecular function	bacterial cell surface binding Inferred from direct assay. Source: MGI transmembrane signaling receptor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Ref.6

Chain

20 – 400

381

Leukosialin

PRO_0000021588

Regions

Topological domain

20 – 253

234

Extracellular Potential

Transmembrane

254 – 276

Helical; Potential

Topological domain

277 – 400

124

Cytoplasmic Potential

Amino acid modifications

Modified residue

291

Phosphoserine Ref.10

Modified residue

341

Phosphothreonine Ref.8

Modified residue

351

Phosphoserine By similarity

Modified residue

355

Phosphoserine Ref.7 Ref.9

Modified residue

368

Phosphoserine Ref.10

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

O-linked (GalNAc...) Ref.6

Glycosylation

103

O-linked (GalNAc...) Ref.6

Glycosylation

109

O-linked (GalNAc...) Ref.6

Glycosylation

113

O-linked (GalNAc...) Ref.6

Glycosylation

114

O-linked (GalNAc...) Ref.6

Glycosylation

136

O-linked (GalNAc...) Ref.6

Glycosylation

137

O-linked (GalNAc...) Ref.6

Glycosylation

173

O-linked (GalNAc...) Ref.6

Glycosylation

178

O-linked (GalNAc...) Ref.6

Glycosylation

239

N-linked (GlcNAc...) Ref.6

Natural variations

Natural variant

T → I.
Corresponds to variant rs2229653 [ dbSNP | Ensembl ].

VAR_051091

Natural variant

T → A.
Corresponds to variant rs2229654 [ dbSNP | Ensembl ].

VAR_051092

Sequences

Sequence

Length

Mass (Da)

Tools

P16150 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: C9C9AB8435D5E1FE
Show »

FASTA

400

40,322

        10         20         30         40         50         60 
MATLLLLLGV LVVSPDALGS TTAVQTPTSG EPLVSTSEPL SSKMYTTSIT SDPKADSTGD 

        70         80         90        100        110        120 
QTSALPPSTS INEGSPLWTS IGASTGSPLP EPTTYQEVSI KMSSVPQETP HATSHPAVPI 

       130        140        150        160        170        180 
TANSLGSHTV TGGTITTNSP ETSSRTSGAP VTTAASSLET SRGTSGPPLT MATVSLETSK 

       190        200        210        220        230        240 
GTSGPPVTMA TDSLETSTGT TGPPVTMTTG SLEPSSGASG PQVSSVKLST MMSPTTSTNA 

       250        260        270        280        290        300 
STVPFRNPDE NSRGMLPVAV LVALLAVIVL VALLLLWRRR QKRRTGALVL SRGGKRNGVV 

       310        320        330        340        350        360 
DAWAGPAQVP EEGAVTVTVG GSGGDKGSGF PDGEGSSRRP TLTTFFGRRK SRQGSLAMEE 

       370        380        390        400 
LKSGSGPSLK GEEEPLVASE DGAVDAPAPD EPEGGDGAAP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of cDNAs encoding human leukosialin and localization of the leukosialin gene to chromosome 16." Pallant A., Eskenazi A., Mattei M.-G., Fournier R.E.K., Carlsson S.R., Fukuda M., Frelinger J.G. Proc. Natl. Acad. Sci. U.S.A. 86:1328-1332(1989) [PubMed: 2521952] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular characterization of sialophorin (CD43), the lymphocyte surface sialoglycoprotein defective in Wiskott-Aldrich syndrome." Shelley C.S., Remold-O'Donnell E., Davis A.E. III, Bruns G.A.P., Rosen F.S., Carroll M.C., Whitehead D.A.S. Proc. Natl. Acad. Sci. U.S.A. 86:2819-2823(1989) [PubMed: 2784859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Structure of the human sialophorin (CD43) gene. Identification of features atypical of genes encoding integral membrane proteins." Shelley C.S., Remold-O'Donnell E., Rosen F.S., Whitehead D.A.S. Biochem. J. 270:569-576(1990) [PubMed: 2241892] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"A short, novel promoter sequence confers the expression of human leukosialin, a major sialoglycoprotein on leukocytes." Kudo S., Fukuda M. J. Biol. Chem. 266:8483-8489(1991) [PubMed: 1827122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[6]	"Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin)." Schmid K., Hediger M.A., Brossmer R., Collins J.H., Haupt H., Marti T., Offner G.D., Schaller J., Takagaki K., Walsh M.T., Schwick H.G., Rose F.S., Remold-O'Donnell E. Proc. Natl. Acad. Sci. U.S.A. 89:663-667(1992) [PubMed: 1731338] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-245, GLYCOSYLATION AT THR-21; THR-22; THR-26; THR-28; SER-29; SER-35; THR-36; SER-37; SER-41; SER-42; THR-46; THR-47; SER-48; THR-50; THR-58; THR-69; SER-99; SER-103; THR-109; THR-113; SER-114; THR-136; THR-137; THR-173; THR-178 AND ASN-239.
[7]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, MASS SPECTROMETRY. Tissue: Platelet.
[8]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-341, MASS SPECTROMETRY. Tissue: T-cell.
[9]	Carrascal M., Abian J. Submitted (JAN-2008) to UniProtKB Cited for: PHOSPHORYLATION AT SER-355, MASS SPECTROMETRY. Tissue: T-cell.
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291 AND SER-368, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04168 mRNA. Translation: AAA59510.1. J04536 mRNA. Translation: AAB59540.1. X52075 Genomic DNA. Translation: CAA36294.1. M61827 Genomic DNA. Translation: AAA51949.1. BC012350 mRNA. Translation: AAH12350.1.
IPI	IPI00027430.
PIR	A39822.
RefSeq	NP_001025459.1. NM_001030288.1. NP_003114.1. NM_003123.3.
UniGene	Hs.632188.
3D structure databases
ProteinModelPortal	P16150.
ModBase	Search...
Protein-protein interaction databases
STRING	P16150.
PTM databases
GlycoSuiteDB	P16150.
PhosphoSite	P16150.
Polymorphism databases
DMDM	126213.
Proteomic databases
PeptideAtlas	P16150.
PRIDE	P16150.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000360121; ENSP00000353238; ENSG00000197471. ENST00000395389; ENSP00000378787; ENSG00000197471.
GeneID	6693.
KEGG	hsa:6693.
UCSC	uc002dtm.1. human.
Organism-specific databases
CTD	6693.
GeneCards	GC16P029581.
HGNC	HGNC:11249. SPN.
HPA	CAB002666.
MIM	182160. gene.
neXtProt	NX_P16150.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16992.
GeneTree	ENSGT00390000017626.
HOGENOM	HBG126784.
HOVERGEN	HBG006258.
InParanoid	P16150.
OMA	GSLAMEE.
OrthoDB	EOG4KSPK7.
PhylomeDB	P16150.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P16150.
Bgee	P16150.
CleanEx	HS_SPN.
Genevestigator	P16150.
Family and domain databases
KO	K06477.
ProtoNet	Search...
Other
NextBio	26089.
PMAP-CutDB	P16150.
SOURCE	Search...

Entry information

Entry name

LEUK_HUMAN

Accession

Primary (citable) accession number: P16150

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	January 25, 2012
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents