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P16150 (LEUK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leukosialin
Alternative name(s):
Galactoglycoprotein
Short name=GALGP
Leukocyte sialoglycoprotein
Sialophorin
CD_antigen=CD43
Gene names
Name:SPN
Synonyms:CD43
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.8

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell costimulation

Inferred from electronic annotation. Source: Ensembl

apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

cell surface receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

negative regulation of cell adhesion

Traceable author statement PubMed 10753822. Source: ProtInc

negative regulation of type IV hypersensitivity

Inferred from electronic annotation. Source: Ensembl

negative thymic T cell selection

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

response to protozoan

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 2023632. Source: ProtInc

   Cellular_componentbasement membrane

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 20605918. Source: UniProtKB

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 10899905. Source: MGI

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integral component of plasma membrane

Traceable author statement PubMed 2023632. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

uropod

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiontransmembrane signaling receptor activity

Traceable author statement PubMed 1683685. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.8
Chain20 – 400381Leukosialin
PRO_0000021588

Regions

Topological domain20 – 253234Extracellular Potential
Transmembrane254 – 27623Helical; Potential
Topological domain277 – 400124Cytoplasmic Potential

Amino acid modifications

Modified residue2911Phosphoserine Ref.9
Modified residue3511Phosphoserine Ref.9
Modified residue3551Phosphoserine Ref.11 Ref.12
Modified residue3681Phosphoserine Ref.13
Glycosylation211O-linked (GalNAc...) Ref.8
Glycosylation221O-linked (GalNAc...) Ref.8
Glycosylation261O-linked (GalNAc...) Ref.8
Glycosylation281O-linked (GalNAc...) Ref.8
Glycosylation291O-linked (GalNAc...) Ref.8
Glycosylation351O-linked (GalNAc...) Ref.8
Glycosylation361O-linked (GalNAc...) Ref.8
Glycosylation371O-linked (GalNAc...) Ref.8
Glycosylation411O-linked (GalNAc...) Ref.8
Glycosylation421O-linked (GalNAc...) Ref.8
Glycosylation461O-linked (GalNAc...) Ref.8
Glycosylation471O-linked (GalNAc...) Ref.8
Glycosylation481O-linked (GalNAc...) Ref.8
Glycosylation501O-linked (GalNAc...) Ref.8
Glycosylation581O-linked (GalNAc...) Ref.8
Glycosylation691O-linked (GalNAc...) Ref.8
Glycosylation991O-linked (GalNAc...) Ref.8
Glycosylation1031O-linked (GalNAc...) Ref.8
Glycosylation1091O-linked (GalNAc...) Ref.8
Glycosylation1131O-linked (GalNAc...) Ref.8
Glycosylation1141O-linked (GalNAc...) Ref.8
Glycosylation1361O-linked (GalNAc...) Ref.8
Glycosylation1371O-linked (GalNAc...) Ref.8
Glycosylation1731O-linked (GalNAc...) Ref.8
Glycosylation1781O-linked (GalNAc...) Ref.8
Glycosylation2391N-linked (GlcNAc...) Ref.8

Natural variations

Natural variant221T → I.
Corresponds to variant rs2229653 [ dbSNP | Ensembl ].
VAR_051091
Natural variant931T → A.
Corresponds to variant rs2229654 [ dbSNP | Ensembl ].
VAR_051092

Sequences

Sequence LengthMass (Da)Tools
P16150 [UniParc].

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

FASTA40040,322
        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' 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]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Spleen and Thymus.
[6]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[12]Carrascal M., Abian J.
Submitted (JAN-2008) to UniProtKB
Cited for: PHOSPHORYLATION AT SER-355, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: T-cell.
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"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.
AK292626 mRNA. Translation: BAF85315.1.
AK313750 mRNA. Translation: BAG36490.1.
CH471238 Genomic DNA. Translation: EAW80015.1.
BC012350 mRNA. Translation: AAH12350.1.
PIRA39822.
RefSeqNP_001025459.1. NM_001030288.2.
NP_003114.1. NM_003123.4.
XP_005276570.1. XM_005276513.1.
UniGeneHs.632188.

3D structure databases

ProteinModelPortalP16150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112571. 4 interactions.
STRING9606.ENSP00000353238.

PTM databases

PhosphoSiteP16150.
UniCarbKBP16150.

Polymorphism databases

DMDM126213.

Proteomic databases

PaxDbP16150.
PeptideAtlasP16150.
PRIDEP16150.

Protocols and materials databases

DNASU6693.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360121; ENSP00000353238; ENSG00000197471.
ENST00000395389; ENSP00000378787; ENSG00000197471.
ENST00000563039; ENSP00000455266; ENSG00000197471.
GeneID101929889.
6693.
KEGGhsa:101929889.
hsa:6693.
UCSCuc002dtm.4. human.

Organism-specific databases

CTD6693.
GeneCardsGC16P029674.
HGNCHGNC:11249. SPN.
HPACAB002666.
HPA055244.
MIM182160. gene.
neXtProtNX_P16150.
PharmGKBPA36079.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47487.
HOGENOMHOG000294199.
HOVERGENHBG006258.
InParanoidP16150.
KOK06477.
OMAGSLAMEE.
OrthoDBEOG7HXCVB.
PhylomeDBP16150.
TreeFamTF337688.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP16150.
BgeeP16150.
CleanExHS_SPN.
GenevestigatorP16150.

Family and domain databases

ProtoNetSearch...

Other

GeneWikiCD43.
NextBio26089.
PMAP-CutDBP16150.
PROP16150.
SOURCESearch...

Entry information

Entry nameLEUK_HUMAN
AccessionPrimary (citable) accession number: P16150
Secondary accession number(s): A8K9B1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

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

Human cell differentiation molecules

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