Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P13838

- LEUK_RAT

UniProt

P13838 - LEUK_RAT

Protein

Leukosialin

Gene

Spn

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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

    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

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei‹1 – 7›7
    Chaini8 – 378371LeukosialinPRO_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...)Sequence Analysis
    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...)Sequence Analysis
    Glycosylationi187 – 1871O-linked (GalNAc...)
    Glycosylationi189 – 1891O-linked (GalNAc...)
    Modified residuei268 – 2681PhosphoserineBy similarity
    Modified residuei326 – 3261PhosphoserineBy similarity
    Modified residuei330 – 3301PhosphoserineBy 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.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000051894.

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini8 – 231224ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini255 – 378124CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei232 – 25423HelicalSequence AnalysisAdd
    BLAST

    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

    « Hide

    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

    Experimental Info

    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: October 1, 2014
    This is version 91 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