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Protein

Leukosialin

Gene

Spn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN). Negatively regulates Th2 cell differentiation and predisposes the differentiation of T-cells towards a Th1 lineage commitment. Promotes the expression of IFN-gamma by T-cells during T-cell receptor (TCR) activation of naive cells and induces the expression of IFN-gamma by CD4+ T-cells and to a lesser extent by CD8+ T-cells. Plays a role in preparing T-cells for cytokine sensing and differentiation into effector cells by inducing the expression of cytokine receptors IFNGR and IL4R, promoting IFNGR and IL4R signaling and by mediating the clustering of IFNGR with TCR. Acts as a major E-selectin ligand responsible for Th17 cell rolling on activated vasculature and recruitment during inflammation. Mediates Th17 cells, but not Th1 cells, adhesion to E-selectin. Acts as a T-cell counter-receptor for SIGLEC1.By similarity
CD43 cytoplasmic tail: Protects cells from apoptotic signals, promoting cell survival.By similarity

GO - Molecular functioni

  • heat shock protein binding Source: RGD
  • Hsp70 protein binding Source: RGD
  • protein domain specific binding Source: RGD

GO - Biological processi

Names & Taxonomyi

Protein namesi
Recommended name:
Leukosialin
Alternative name(s):
Leukocyte sialoglycoprotein
Sialophorin
W3/13 antigen
CD_antigen: CD43
Cleaved into the following chain:
CD43 cytoplasmic tail
Short name:
CD43-ct
Short name:
CD43ct
Gene namesi
Name:Spn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3750. Spn.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini8 – 231ExtracellularSequence analysisAdd BLAST224
Transmembranei232 – 254HelicalSequence analysisAdd BLAST23
Topological domaini255 – 378CytoplasmicSequence analysisAdd BLAST124

Keywords - Cellular componenti

Cell projection, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi259 – 261KRR → NGG: Loss of interaction with EZR, MSN and RDX and co-localization to microvilli. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei‹1 – 7›7
ChainiPRO_00000215908 – 378LeukosialinAdd BLAST371
ChainiPRO_0000443408255 – 378CD43 cytoplasmic tailBy similarityAdd BLAST124

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi13O-linked (GalNAc...) threonine1
Glycosylationi15O-linked (GalNAc...) threonine1
Glycosylationi20O-linked (GalNAc...) threonine1
Glycosylationi23O-linked (GalNAc...) serine1
Glycosylationi25O-linked (GalNAc...) serine1
Glycosylationi27O-linked (GalNAc...) serine1
Glycosylationi28O-linked (GalNAc...) threonine1
Glycosylationi29O-linked (GalNAc...) serine1
Glycosylationi33O-linked (GalNAc...) serine1
Glycosylationi34O-linked (GalNAc...) threonine1
Glycosylationi36O-linked (GalNAc...) serine1
Glycosylationi37O-linked (GalNAc...) serine1
Glycosylationi40O-linked (GalNAc...) threonine1
Glycosylationi108O-linked (GalNAc...) serine1
Glycosylationi113O-linked (GalNAc...) serine1
Glycosylationi118O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi120O-linked (GalNAc...) threonine1
Glycosylationi124O-linked (GalNAc...) threonine1
Glycosylationi125O-linked (GalNAc...) serine1
Glycosylationi126O-linked (GalNAc...) serine1
Glycosylationi174O-linked (GalNAc...) threonine1
Glycosylationi176O-linked (GalNAc...) serine1
Glycosylationi180O-linked (GalNAc...) serine1
Glycosylationi183O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi187O-linked (GalNAc...) serine1
Glycosylationi189O-linked (GalNAc...) threonine1
Modified residuei268PhosphoserineBy similarity1
Modified residuei276PhosphothreonineCombined sources1
Modified residuei311PhosphoserineBy similarity1
Modified residuei316PhosphothreonineBy similarity1
Modified residuei322PhosphoserineBy similarity1
Modified residuei326PhosphoserineCombined sources1
Modified residuei330Phosphoserine; by PKC/PRKCQCombined sources1
Modified residuei354PhosphoserineCombined sources1
Modified residuei361PhosphothreonineCombined sources1

Post-translational modificationi

Has a high content of sialic acid and O-linked carbohydrate structures.
Phosphorylation at Ser-330 is regulated by chemokines, requires its association with ERM proteins (EZR, RDX and MSN) and is essential for its function in the regulation of T-cell trafficking to lymph nodes.By similarity
Cleavage by CTSG releases its extracellular domain and triggers its intramembrane proteolysis by gamma-secretase releasing the CD43 cytoplasmic tail chain (CD43-ct) which translocates to the nucleus.By similarity
CD43 cytoplasmic tail: Sumoylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP13838.
PRIDEiP13838.

PTM databases

iPTMnetiP13838.
PhosphoSitePlusiP13838.

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Interacts with HIPK2 via the cytoplasmic domain (By similarity). Interacts with SIGLEC1 (PubMed:11238599). Interacts with EZR, MSN and RDX (PubMed:9472040).By similarity2 Publications

GO - Molecular functioni

  • heat shock protein binding Source: RGD
  • Hsp70 protein binding Source: RGD
  • protein domain specific binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000051894.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni255 – 285Required for interaction with EZR, MSN and RDX and for co-localization to microvilli1 PublicationAdd BLAST31

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J161. Eukaryota.
ENOG410YXQE. LUCA.
HOGENOMiHOG000294199.
HOVERGENiHBG006258.
InParanoidiP13838.
PhylomeDBiP13838.
TreeFamiTF337688.

Sequencei

Sequence statusi: Fragment.

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

P13838-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
WAQVVSQENL PNTMTMLPFT PNSESPSTSE ALSTYSSIAT VPVTEDPKES
60 70 80 90 100
ISPWGQTTAP ASSIPLGTPE LSSFFFTSAG ASGNTPVPEL TTSQEVSTEA
110 120 130 140 150
SLVLFPKSSG VASDPPVTIT NPATSSAVAS TSLETFKGTS APPVTVTSST
160 170 180 190 200
MTSGPFVATT VSSETSGPPV TMATGSLGPS KETHGLSATI ATSSGESSSV
210 220 230 240 250
AGGTPVFSTK ISTTSTPNPI TTVPPRPGSS GMLLVSMLIA LTVVLVLVAL
260 270 280 290 300
LLLWRQRQKR RTGALTLSRG GKRNGTVDAW AGPARVPDEE ATTASGSGGN
310 320 330 340 350
KSSGAPETDG SGQRPTLTTF FSRRKSRQGS VALEELKPGT GPNLKGEEEP
360 370
LVGSEDEAVE TPTSDGPQAK DGAAPQSL
Length:378
Mass (Da):38,426
Last modified:January 1, 1990 - v1
Checksum:i231CC80E8A8A257C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00090 mRNA. Translation: CAA68281.1.
PIRiS00842.
UniGeneiRn.11144.

Genome annotation databases

UCSCiRGD:3750. rat.

Similar proteinsi

Entry informationi

Entry nameiLEUK_RAT
AccessioniPrimary (citable) accession number: P13838
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: March 28, 2018
This is version 110 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome