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P13838

- LEUK_RAT

UniProt

P13838 - LEUK_RAT

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Protein
Leukosialin
Gene
Spn
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. protein domain specific binding Source: RGD

GO - Biological processi

  1. chronic inflammatory response Source: RGD
  2. monocyte activation Source: RGD
  3. thymocyte aggregation Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Leukosialin
Alternative name(s):
Leukocyte sialoglycoprotein
Sialophorin
W3/13 antigen
CD_antigen: CD43
Gene namesi
Name:Spn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3750. Spn.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini8 – 231224Extracellular Reviewed prediction
Add
BLAST
Transmembranei232 – 25423Helical; Reviewed prediction
Add
BLAST
Topological domaini255 – 378124Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cell surface Source: RGD
  2. cleavage furrow Source: RGD
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: RGD
  5. microvillus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 7›7
Chaini8 – 378371Leukosialin
PRO_0000021590Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi13 – 131O-linked (GalNAc...)
Glycosylationi15 – 151O-linked (GalNAc...)
Glycosylationi20 – 201O-linked (GalNAc...)
Glycosylationi23 – 231O-linked (GalNAc...)
Glycosylationi25 – 251O-linked (GalNAc...)
Glycosylationi27 – 271O-linked (GalNAc...)
Glycosylationi28 – 281O-linked (GalNAc...)
Glycosylationi29 – 291O-linked (GalNAc...)
Glycosylationi33 – 331O-linked (GalNAc...)
Glycosylationi34 – 341O-linked (GalNAc...)
Glycosylationi36 – 361O-linked (GalNAc...)
Glycosylationi37 – 371O-linked (GalNAc...)
Glycosylationi40 – 401O-linked (GalNAc...)
Glycosylationi108 – 1081O-linked (GalNAc...)
Glycosylationi113 – 1131O-linked (GalNAc...)
Glycosylationi118 – 1181O-linked (GalNAc...) Reviewed prediction
Glycosylationi120 – 1201O-linked (GalNAc...)
Glycosylationi124 – 1241O-linked (GalNAc...)
Glycosylationi125 – 1251O-linked (GalNAc...)
Glycosylationi126 – 1261O-linked (GalNAc...)
Glycosylationi174 – 1741O-linked (GalNAc...)
Glycosylationi176 – 1761O-linked (GalNAc...)
Glycosylationi180 – 1801O-linked (GalNAc...)
Glycosylationi183 – 1831O-linked (GalNAc...) Reviewed prediction
Glycosylationi187 – 1871O-linked (GalNAc...)
Glycosylationi189 – 1891O-linked (GalNAc...)
Modified residuei268 – 2681Phosphoserine By similarity
Modified residuei326 – 3261Phosphoserine By similarity
Modified residuei330 – 3301Phosphoserine By similarity

Post-translational modificationi

Has a high content of sialic acid and O-linked carbohydrate structures.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP13838.
PRIDEiP13838.

Expressioni

Tissue specificityi

Cell surface of thymocytes, T-lymphocytes, neutrophils, plasma cells and myelomas.

Gene expression databases

GenevestigatoriP13838.

Interactioni

Subunit structurei

Interacts with HIPK2 via the cytoplasmic domain. Interacts with RDX By similarity.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000051894.

Family & Domainsi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG47487.
HOGENOMiHOG000294199.
HOVERGENiHBG006258.
InParanoidiP13838.
OrthoDBiEOG7HXCVB.
PhylomeDBiP13838.
TreeFamiTF337688.

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13838-1 [UniParc]FASTAAdd to Basket

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WAQVVSQENL PNTMTMLPFT PNSESPSTSE ALSTYSSIAT VPVTEDPKES    50
ISPWGQTTAP ASSIPLGTPE LSSFFFTSAG ASGNTPVPEL TTSQEVSTEA 100
SLVLFPKSSG VASDPPVTIT NPATSSAVAS TSLETFKGTS APPVTVTSST 150
MTSGPFVATT VSSETSGPPV TMATGSLGPS KETHGLSATI ATSSGESSSV 200
AGGTPVFSTK ISTTSTPNPI TTVPPRPGSS GMLLVSMLIA LTVVLVLVAL 250
LLLWRQRQKR RTGALTLSRG GKRNGTVDAW AGPARVPDEE ATTASGSGGN 300
KSSGAPETDG SGQRPTLTTF FSRRKSRQGS VALEELKPGT GPNLKGEEEP 350
LVGSEDEAVE TPTSDGPQAK DGAAPQSL 378
Length:378
Mass (Da):38,426
Last modified:January 1, 1990 - v1
Checksum:i231CC80E8A8A257C
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00090 mRNA. Translation: CAA68281.1.
PIRiS00842.
UniGeneiRn.11144.

Genome annotation databases

UCSCiRGD:3750. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00090 mRNA. Translation: CAA68281.1 .
PIRi S00842.
UniGenei Rn.11144.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000051894.

Proteomic databases

PaxDbi P13838.
PRIDEi P13838.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:3750. rat.

Organism-specific databases

RGDi 3750. Spn.

Phylogenomic databases

eggNOGi NOG47487.
HOGENOMi HOG000294199.
HOVERGENi HBG006258.
InParanoidi P13838.
OrthoDBi EOG7HXCVB.
PhylomeDBi P13838.
TreeFami TF337688.

Gene expression databases

Genevestigatori P13838.

Family and domain databases

ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiLEUK_RAT
AccessioniPrimary (citable) accession number: P13838
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: July 9, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

Dasty 3

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