P16150 (LEUK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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	T cell costimulation Inferred from electronic annotation. Source: Compara blood coagulation Traceable author statement. Source: Reactome cell surface receptor signaling pathway Inferred from electronic annotation. Source: Compara cellular defense response Traceable author statement PubMed 1683685. Source: ProtInc chemotaxis Traceable author statement PubMed 10753822. Source: ProtInc defense response to bacterium Inferred from direct assay PubMed 10899905. Source: MGI establishment or maintenance of cell polarity Traceable author statement PubMed 10753822. Source: ProtInc immune response Traceable author statement PubMed 2023632. Source: ProtInc leukocyte migration Traceable author statement. Source: Reactome negative regulation of T cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of cell adhesion Traceable author statement PubMed 10753822. Source: ProtInc negative regulation of type IV hypersensitivity Inferred from electronic annotation. Source: Compara negative thymic T cell selection Inferred from electronic annotation. Source: Compara positive regulation of T cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of tumor necrosis factor biosynthetic process Inferred from direct assay PubMed 10899905. Source: MGI regulation of defense response to virus Inferred from electronic annotation. Source: Compara response to protozoan Inferred from electronic annotation. Source: Compara
Cellular_component	basement membrane Inferred from electronic annotation. Source: Compara cell surface Inferred from direct assay PubMed 20605918. Source: UniProtKB external side of plasma membrane Inferred from electronic annotation. Source: Compara extracellular space Inferred from direct assay PubMed 10899905. Source: MGI integral to plasma membrane Traceable author statement PubMed 2023632. Source: ProtInc uropod Inferred from electronic annotation. Source: Compara
Molecular_function	bacterial cell surface binding Inferred from direct assay PubMed 10899905. Source: MGI transmembrane signaling receptor activity Traceable author statement PubMed 1683685. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Ref.6
	Chain	20 – 400	381	Leukosialin		PRO_0000021588
Regions
	Topological domain	20 – 253	234	Extracellular Potential
	Transmembrane	254 – 276	23	Helical; Potential
	Topological domain	277 – 400	124	Cytoplasmic Potential
Amino acid modifications
	Modified residue	291	1	Phosphoserine Ref.7
	Modified residue	351	1	Phosphoserine Ref.7
	Modified residue	355	1	Phosphoserine Ref.9 Ref.10
	Modified residue	368	1	Phosphoserine Ref.11
	Glycosylation	21	1	O-linked (GalNAc...) Ref.6
	Glycosylation	22	1	O-linked (GalNAc...) Ref.6
	Glycosylation	26	1	O-linked (GalNAc...) Ref.6
	Glycosylation	28	1	O-linked (GalNAc...) Ref.6
	Glycosylation	29	1	O-linked (GalNAc...) Ref.6
	Glycosylation	35	1	O-linked (GalNAc...) Ref.6
	Glycosylation	36	1	O-linked (GalNAc...) Ref.6
	Glycosylation	37	1	O-linked (GalNAc...) Ref.6
	Glycosylation	41	1	O-linked (GalNAc...) Ref.6
	Glycosylation	42	1	O-linked (GalNAc...) Ref.6
	Glycosylation	46	1	O-linked (GalNAc...) Ref.6
	Glycosylation	47	1	O-linked (GalNAc...) Ref.6
	Glycosylation	48	1	O-linked (GalNAc...) Ref.6
	Glycosylation	50	1	O-linked (GalNAc...) Ref.6
	Glycosylation	58	1	O-linked (GalNAc...) Ref.6
	Glycosylation	69	1	O-linked (GalNAc...) Ref.6
	Glycosylation	99	1	O-linked (GalNAc...) Ref.6
	Glycosylation	103	1	O-linked (GalNAc...) Ref.6
	Glycosylation	109	1	O-linked (GalNAc...) Ref.6
	Glycosylation	113	1	O-linked (GalNAc...) Ref.6
	Glycosylation	114	1	O-linked (GalNAc...) Ref.6
	Glycosylation	136	1	O-linked (GalNAc...) Ref.6
	Glycosylation	137	1	O-linked (GalNAc...) Ref.6
	Glycosylation	173	1	O-linked (GalNAc...) Ref.6
	Glycosylation	178	1	O-linked (GalNAc...) Ref.6
	Glycosylation	239	1	N-linked (GlcNAc...) Ref.6
Natural variations
	Natural variant	22	1	T → I. Corresponds to variant rs2229653 [ dbSNP | Ensembl ].		VAR_051091
	Natural variant	93	1	T → A. Corresponds to variant rs2229654 [ dbSNP | Ensembl ].		VAR_051092

Sequences

	Sequence		Length	Mass (Da)
	P16150 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: C9C9AB8435D5E1FE	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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]	"Phosphorylation of the major leukocyte surface sialoglycoprotein, leukosialin, is increased by phorbol 12-myristate 13-acetate." Piller V., Piller F., Fukuda M. J. Biol. Chem. 264:18824-18831(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-291 AND SER-351.
[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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: T-cell.
[9]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, MASS SPECTROMETRY. Tissue: Platelet.
[10]	Carrascal M., Abian J. Submitted (JAN-2008) to UniProtKB Cited for: PHOSPHORYLATION AT SER-355, MASS SPECTROMETRY. Tissue: T-cell.
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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] [Europe PMC] [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_001030288.2. NP_003114.1. NM_003123.4.
UniGene	Hs.632188.
3D structure databases
ProteinModelPortal	P16150.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000353238.
PTM databases
GlycoSuiteDB	P16150.
PhosphoSite	P16150.
Polymorphism databases
DMDM	126213.
Proteomic databases
PaxDb	P16150.
PeptideAtlas	P16150.
PRIDE	P16150.
Protocols and materials databases
DNASU	6693.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000360121; ENSP00000353238; ENSG00000197471. ENST00000395389; ENSP00000378787; ENSG00000197471. ENST00000563039; ENSP00000455266; ENSG00000197471.
GeneID	6693.
KEGG	hsa:6693.
UCSC	uc002dtm.3. human.
Organism-specific databases
CTD	6693.
GeneCards	GC16P029674.
HGNC	HGNC:11249. SPN.
HPA	CAB002666.
MIM	182160. gene.
neXtProt	NX_P16150.
PharmGKB	PA36079.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG47487.
HOGENOM	HOG000294199.
HOVERGEN	HBG006258.
InParanoid	P16150.
KO	K06477.
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
ProtoNet	Search...
Other
GenomeRNAi	6693.
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:	April 3, 2013
This is version 124 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.