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Protein

Leukosialin

Gene

Spn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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).By similarity

GO - Molecular functioni

  • protein domain specific binding Source: RGD

GO - Biological processi

  • chronic inflammatory response Source: RGD
  • monocyte activation Source: RGD
  • 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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3750. Spn.

Subcellular locationi

Topology

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

GO - Cellular componenti

  • cell surface Source: RGD
  • cleavage furrow Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: RGD
  • microvillus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei‹1 – 7›7
ChainiPRO_00000215908 – 378LeukosialinAdd BLAST371

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi13O-linked (GalNAc...)1
Glycosylationi15O-linked (GalNAc...)1
Glycosylationi20O-linked (GalNAc...)1
Glycosylationi23O-linked (GalNAc...)1
Glycosylationi25O-linked (GalNAc...)1
Glycosylationi27O-linked (GalNAc...)1
Glycosylationi28O-linked (GalNAc...)1
Glycosylationi29O-linked (GalNAc...)1
Glycosylationi33O-linked (GalNAc...)1
Glycosylationi34O-linked (GalNAc...)1
Glycosylationi36O-linked (GalNAc...)1
Glycosylationi37O-linked (GalNAc...)1
Glycosylationi40O-linked (GalNAc...)1
Glycosylationi108O-linked (GalNAc...)1
Glycosylationi113O-linked (GalNAc...)1
Glycosylationi118O-linked (GalNAc...)Sequence analysis1
Glycosylationi120O-linked (GalNAc...)1
Glycosylationi124O-linked (GalNAc...)1
Glycosylationi125O-linked (GalNAc...)1
Glycosylationi126O-linked (GalNAc...)1
Glycosylationi174O-linked (GalNAc...)1
Glycosylationi176O-linked (GalNAc...)1
Glycosylationi180O-linked (GalNAc...)1
Glycosylationi183O-linked (GalNAc...)Sequence analysis1
Glycosylationi187O-linked (GalNAc...)1
Glycosylationi189O-linked (GalNAc...)1
Modified residuei268PhosphoserineBy similarity1
Modified residuei276PhosphothreonineCombined sources1
Modified residuei311PhosphoserineBy similarity1
Modified residuei316PhosphothreonineBy similarity1
Modified residuei322PhosphoserineBy similarity1
Modified residuei326PhosphoserineCombined sources1
Modified residuei330PhosphoserineCombined sources1
Modified residuei354PhosphoserineCombined sources1
Modified residuei361PhosphothreonineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP13838.
PRIDEiP13838.

PTM databases

iPTMnetiP13838.
PhosphoSitePlusiP13838.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSRNOG00000036711.

Interactioni

Subunit structurei

Interacts with HIPK2 via the cytoplasmic domain. Interacts with RDX (By similarity).By similarity

GO - Molecular functioni

  • protein domain specific binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000051894.

Family & Domainsi

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000051894.

PTM databases

iPTMnetiP13838.
PhosphoSitePlusiP13838.

Proteomic databases

PaxDbiP13838.
PRIDEiP13838.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3750. rat.

Organism-specific databases

RGDi3750. Spn.

Phylogenomic databases

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

Gene expression databases

BgeeiENSRNOG00000036711.

Family and domain databases

ProtoNetiSearch...

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: November 2, 2016
This is version 105 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.