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Q62170

- SELPL_MOUSE

UniProt

Q62170 - SELPL_MOUSE

Protein

P-selectin glycoprotein ligand 1

Gene

Selplg

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E- and P-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture.3 Publications

    GO - Molecular functioni

    1. protein binding Source: MGI

    GO - Biological processi

    1. cellular response to interleukin-6 Source: Ensembl
    2. leukocyte adhesive activation Source: UniProtKB
    3. leukocyte tethering or rolling Source: MGI

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Sialic acid

    Enzyme and pathway databases

    ReactomeiREACT_225233. Cell surface interactions at the vascular wall.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    P-selectin glycoprotein ligand 1
    Short name:
    PSGL-1
    Alternative name(s):
    Selectin P ligand
    CD_antigen: CD162
    Gene namesi
    Name:Selplg
    Synonyms:Selp1, Selpl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:106689. Selplg.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi54 – 541Y → F: Greatly decreased P-selectin binding and tethering and rolling of cells. No further reduction of P-selectin binding; when associated with Y-56. Binding of P-selectin completely abolished; when associated with A-55; Y-56 and A-58. 1 Publication
    Mutagenesisi55 – 551T → A: No effect on P-selectin binding. Greatly reduced P-selectin binding and tethering and rolling of cells; when associated with A-58. Binding of P-selectin completely abolished; when associated with Y-54; Y-56 and A-58. 1 Publication
    Mutagenesisi56 – 561Y → F: No effect on P-selectin binding. Greatly decreased P-selectin binding and tethering and rolling of cells; when associated with Y-54. Binding of P-selectin completely abolished; when associated with Y-54; A-55 and A-58. 1 Publication
    Mutagenesisi58 – 581T → A: Greatly decreased P-selectin binding and tethering and rolling of cells. No further reduction in P-selectin binding when associated with A-55. Binding of P-selectin completely abolished; when associated with Y-54; A-55; and Y-56. 1 Publication
    Mutagenesisi66 – 661N → T: No effect on P-selectin binding; when associated with A-261.
    Mutagenesisi261 – 2611N → A: No effect on P-selectin binding; when associated with T-66.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Propeptidei18 – 4124By similarityPRO_0000022304Add
    BLAST
    Chaini42 – 397356P-selectin glycoprotein ligand 1PRO_0000022305Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei42 – 421Pyrrolidone carboxylic acidBy similarity
    Modified residuei54 – 541Sulfotyrosine1 Publication
    Modified residuei56 – 561SulfotyrosineSequence Analysis
    Glycosylationi58 – 581O-linked (GalNAc...)Curated
    Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi261 – 2611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi307 – 307InterchainBy similarity

    Post-translational modificationi

    Displays complex, core-2, sialylated and fucosylated O-linked oligosaccharides, at least some of which appear to contain poly-N-acetyllactosamine with varying degrees of substitution. Mainly disialylated or neutral forms of the core-2 tetrasaccharide, Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH. The GlcN:GalN ratio is approximately 2:1 and the Man:Fuc ratio 3:5. Contains about 14% fucose with alpha-1,3 linkage present in two forms: One species is a disialylated, monofucosylated glycan, and the other, a monosialylated, trifucosylated glycan with a polylactosamine backbone. The fucosylated forms carry the Lewis antigen and are important for interaction with selectins and for functioning. No sulfated O-glycans. Some N-glycosylation By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid, Sulfation

    Proteomic databases

    PaxDbiQ62170.
    PRIDEiQ62170.

    PTM databases

    PhosphoSiteiQ62170.

    Expressioni

    Tissue specificityi

    Highly expressed in blood, bone marrow, brain, adipose tissue, spleen, and thymus. Also expressed in heart, kidney, liver, muscle, ovary, and stomach.1 Publication

    Gene expression databases

    ArrayExpressiQ62170.
    BgeeiQ62170.
    CleanExiMM_SELPLG.
    GenevestigatoriQ62170.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Interacts with P- and E-selectins, through their lectin/EGF domains. Interaction with P-selectin requires sialyl Lewis X glycan modification and tyrosine sulfation, probably on Tyr-54, for high affinity binding By similarity. Dimerization appears not to be required for P-selectin/SELP binding By similarity. Interacts with SNX20 By similarity. Interacts with MSN and SYK; mediates SYK activation downstream of SELPLG By similarity.By similarity

    Protein-protein interaction databases

    DIPiDIP-59330N.
    STRINGi10090.ENSMUSP00000098436.

    Structurei

    Secondary structure

    1
    397
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi337 – 3426

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EMTX-ray2.80C/D/E331-348[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ62170.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini18 – 307290ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini329 – 39769CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei308 – 32821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati126 – 135101
    Repeati136 – 145102
    Repeati146 – 155103
    Repeati156 – 165104
    Repeati166 – 175105
    Repeati176 – 185106
    Repeati186 – 195107
    Repeati196 – 205108
    Repeati206 – 215109
    Repeati216 – 2251010

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni126 – 22510010 X 10 AA tandem repeatsAdd
    BLAST

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG300903.
    HOGENOMiHOG000013048.
    HOVERGENiHBG061628.

    Family and domain databases

    InterProiIPR026195. PSGL-1.
    [Graphical view]
    PANTHERiPTHR17384. PTHR17384. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q62170-1 [UniParc]FASTAAdd to Basket

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    MSPSFLVLLT ILGPGNSLQL QDPWGHETKE APGPVHLRER RQVVGDDDFE    50
    DPDYTYNTDP PELLKNVTNT VAAHPELPTT VVMLERDSTS AGTSERATEK 100
    IATTDPTAPG TGGTAVGMLS TDSATQWSLT SVETVQPAST EVETSQPAPM 150
    EAETSQPAPM EAETSQPAPM EAETSQPAPM EADTSQPAPM EAETSQPAPN 200
    EAETSKPAPT EAETSKPAPT EAETTQLPRI QAVKTLFTTS AATEVPSTEP 250
    TTMETASTES NESTIFLGPS VTHLPDSGLK KGLIVTPGNS PAPTLPGSSD 300
    LIPVKQCLLI ILILASLATI FLVCTVVLAV RLSRKTHMYP VRNYSPTEMI 350
    CISSLLPEGG DGAPVTANGG LPKVQDLKTE PSGDRDGDDL TLHSFLP 397
    Length:397
    Mass (Da):41,842
    Last modified:July 27, 2011 - v2
    Checksum:iD5EB53D493AE26EE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti173 – 1731E → D in CAA62583. (PubMed:8639776)Curated
    Sequence conflicti176 – 1761Q → K in CAA62583. (PubMed:8639776)Curated
    Sequence conflicti180 – 1801M → T in CAA62583. (PubMed:8639776)Curated
    Sequence conflicti183 – 1831D → E in CAA62583. (PubMed:8639776)Curated
    Sequence conflicti186 – 1861Q → K in CAA62583. (PubMed:8639776)Curated
    Sequence conflicti190 – 1901M → T in CAA62583. (PubMed:8639776)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91144 mRNA. Translation: CAA62583.1.
    AC159240 Genomic DNA. No translation available.
    UniGeneiMm.332590.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91144 mRNA. Translation: CAA62583.1 .
    AC159240 Genomic DNA. No translation available.
    UniGenei Mm.332590.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EMT X-ray 2.80 C/D/E 331-348 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59330N.
    STRINGi 10090.ENSMUSP00000098436.

    PTM databases

    PhosphoSitei Q62170.

    Proteomic databases

    PaxDbi Q62170.
    PRIDEi Q62170.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:106689. Selplg.

    Phylogenomic databases

    eggNOGi NOG300903.
    HOGENOMi HOG000013048.
    HOVERGENi HBG061628.

    Enzyme and pathway databases

    Reactomei REACT_225233. Cell surface interactions at the vascular wall.

    Miscellaneous databases

    EvolutionaryTracei Q62170.
    PROi Q62170.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q62170.
    Bgeei Q62170.
    CleanExi MM_SELPLG.
    Genevestigatori Q62170.

    Family and domain databases

    InterProi IPR026195. PSGL-1.
    [Graphical view ]
    PANTHERi PTHR17384. PTHR17384. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Mouse P-selectin glycoprotein ligand-1: molecular cloning, chromosomal localization, and expression of a functional P-selectin receptor."
      Yang J., Galipeau J., Kozak C., Furie B.C., Furie B.
      Blood 87:4176-4186(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INTERACTION WITH SELE AND SELP, TISSUE SPECIFICITY.
      Strain: BALB/c.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "P-Selectin glycoprotein ligand 1 (PSGL-1) is a physiological ligand for E-selectin in mediating T helper 1 lymphocyte migration."
      Hirata T., Merrill-Skoloff G., Aab M., Yang J., Furie B.C., Furie B.
      J. Exp. Med. 192:1669-1676(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SELE AND SELP, FUNCTION.
    4. "P-, E-, and L-selectin mediate migration of activated CD8+ T lymphocytes into inflamed skin."
      Hirata T., Furie B.C., Furie B.
      J. Immunol. 169:4307-4313(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "N-terminal residues in murine P-selectin glycoprotein ligand-1 required for binding to murine P-selectin."
      Xia L., Ramachandran V., McDaniel J.M., Nguyen K.N., Cummings R.D., McEver R.P.
      Blood 101:552-559(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SELP, SULFATION, MUTAGENESIS OF TYR-54; THR-55; TYR-56 AND THR-58.
    6. "Complete identification of E-selectin ligands on neutrophils reveals distinct functions of PSGL-1, ESL-1, and CD44."
      Hidalgo A., Peired A.J., Wild M.K., Vestweber D., Frenette P.S.
      Immunity 26:477-489(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSELPL_MOUSE
    AccessioniPrimary (citable) accession number: Q62170
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 103 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3