P13838 (LEUK_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 85.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Leukosialin Alternative name(s): Leukocyte sialoglycoprotein Sialophorin W3/13 antigen CD_antigen=CD43 | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 378 AA. |
| Sequence status | Fragment. |
| 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 By similarity. |
| Subunit structure | Interacts with HIPK2 via the cytoplasmic domain. Interacts with RDX By similarity. Ref.2 |
| Subcellular location | |
| 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 | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | chronic inflammatory response Inferred from expression pattern PubMed 10486239. Source: RGD monocyte activationInferred from expression pattern PubMed 9400815. Source: RGD thymocyte aggregationInferred from mutant phenotype PubMed 1382990. Source: RGD |
| Cellular_component | cell surface Inferred from direct assay PubMed 7758131. Source: RGD cleavage furrowInferred from direct assay PubMed 8421057. Source: RGD integral to membraneInferred from electronic annotation. Source: UniProtKB-KW membraneInferred from direct assay PubMed 10233680. Source: RGD microvillusInferred from direct assay PubMed 8421057. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | ‹1 – 7 | ›7 | |||||||
| Chain | 8 – 378 | 371 | Leukosialin | PRO_0000021590 | |||||
Regions | |||||||||
| Topological domain | 8 – 231 | 224 | Extracellular Potential | ||||||
| Transmembrane | 232 – 254 | 23 | Helical; Potential | ||||||
| Topological domain | 255 – 378 | 124 | Cytoplasmic Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 268 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 326 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 330 | 1 | Phosphoserine By similarity | ||||||
| Glycosylation | 13 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 15 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 20 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 23 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 25 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 27 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 28 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 29 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 33 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 34 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 36 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 37 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 40 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 108 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 113 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 118 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 120 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 124 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 125 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 126 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 174 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 176 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 180 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 183 | 1 | O-linked (GalNAc...) Potential | ||||||
| Glycosylation | 187 | 1 | O-linked (GalNAc...) | ||||||
| Glycosylation | 189 | 1 | O-linked (GalNAc...) | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
Sequences
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References
| [1] | "The sequence of rat leukosialin (W3/13 antigen) reveals a molecule with O-linked glycosylation of one third of its extracellular amino acids." Killeen N., Barclay A.N., Willis A.C., Williams A.F. EMBO J. 6:4029-4034(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Thymocyte. |
| [2] | "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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y00090 mRNA. Translation: CAA68281.1. |
| IPI | IPI00361205. |
| PIR | S00842. |
| UniGene | Rn.11144. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10116.ENSRNOP00000051894. |
Proteomic databases | |
| PaxDb | P13838. |
| PRIDE | P13838. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| UCSC | RGD:3750. rat. |
Organism-specific databases | |
| RGD | 3750. Spn. |
Phylogenomic databases | |
| eggNOG | NOG47487. |
| HOGENOM | HOG000294199. |
| HOVERGEN | HBG006258. |
| InParanoid | P13838. |
| OrthoDB | EOG4KSPK7. |
Gene expression databases | |
| Genevestigator | P13838. |
Family and domain databases | |
| ProtoNet | Search... |
Entry information
| Entry name | LEUK_RAT | ||||||||
| Accession | Primary (citable) accession number: P13838 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||

Clusters with
