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Q01102

- LYAM3_MOUSE

UniProt

Q01102 - LYAM3_MOUSE

Protein

P-selectin

Gene

Selp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Ca2+-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with PSGL1.1 Publication

    GO - Molecular functioni

    1. calcium-dependent protein binding Source: MGI
    2. fucose binding Source: Ensembl
    3. glycoprotein binding Source: MGI
    4. heparin binding Source: Ensembl
    5. lipopolysaccharide binding Source: Ensembl
    6. oligosaccharide binding Source: Ensembl
    7. protein binding Source: MGI
    8. sialic acid binding Source: MGI

    GO - Biological processi

    1. cellular response to interleukin-6 Source: MGI
    2. heterophilic cell-cell adhesion Source: MGI
    3. inflammatory response Source: MGI
    4. leukocyte cell-cell adhesion Source: MGI
    5. leukocyte migration Source: MGI
    6. leukocyte tethering or rolling Source: MGI
    7. positive regulation of leukocyte migration Source: MGI
    8. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    9. positive regulation of platelet activation Source: BHF-UCL
    10. regulation of integrin activation Source: UniProtKB

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Lectin

    Enzyme and pathway databases

    ReactomeiREACT_225233. Cell surface interactions at the vascular wall.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    P-selectin
    Alternative name(s):
    CD62 antigen-like family member P
    Granule membrane protein 140
    Short name:
    GMP-140
    Leukocyte-endothelial cell adhesion molecule 3
    Short name:
    LECAM3
    Platelet activation dependent granule-external membrane protein
    Short name:
    PADGEM
    CD_antigen: CD62P
    Gene namesi
    Name:Selp
    Synonyms:Grmp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:98280. Selp.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: MGI
    2. extracellular space Source: Ensembl
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane Source: MGI
    5. nucleus Source: Ensembl
    6. platelet alpha granule membrane Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4141Sequence AnalysisAdd
    BLAST
    Chaini42 – 768727P-selectinPRO_0000017499Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi60 ↔ 158By similarity
    Disulfide bondi131 ↔ 150By similarity
    Disulfide bondi163 ↔ 174By similarity
    Disulfide bondi168 ↔ 183By similarity
    Disulfide bondi185 ↔ 194By similarity
    Disulfide bondi200 ↔ 244By similarity
    Disulfide bondi230 ↔ 257By similarity
    Disulfide bondi262 ↔ 306By similarity
    Disulfide bondi292 ↔ 319By similarity
    Disulfide bondi324 ↔ 368By similarity
    Disulfide bondi354 ↔ 381By similarity
    Disulfide bondi386 ↔ 430By similarity
    Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi416 ↔ 443By similarity
    Disulfide bondi448 ↔ 492By similarity
    Disulfide bondi478 ↔ 505By similarity
    Disulfide bondi510 ↔ 554By similarity
    Disulfide bondi540 ↔ 567By similarity
    Disulfide bondi580 ↔ 624By similarity
    Glycosylationi603 – 6031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi610 ↔ 637By similarity
    Disulfide bondi642 ↔ 686By similarity
    Glycosylationi654 – 6541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi661 – 6611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi672 ↔ 699By similarity
    Glycosylationi679 – 6791N-linked (GlcNAc...)Sequence Analysis
    Lipidationi745 – 7451S-palmitoyl cysteineBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Proteomic databases

    PRIDEiQ01102.

    PTM databases

    PhosphoSiteiQ01102.

    Expressioni

    Tissue specificityi

    Stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Upon cell activation by agonists, P-selectin is transported rapidly to the cell surface.

    Inductioni

    By TNF-alpha. Induced expression in lung, liver, kidney and heart after endotoxin treatment.2 Publications

    Gene expression databases

    BgeeiQ01102.
    CleanExiMM_SELP.
    GenevestigatoriQ01102.

    Interactioni

    Subunit structurei

    Interacts with SNX17. Interacts with PSGL1/SEPL and PODXL2 and mediates neutrophil adhesion and leukocyte rolling. This interaction requires the sialyl-Lewis X epitope of PSGL1 and PODXL2, and specific tyrosine sulfation on PSGL1 By similarity.By similarity

    Structurei

    Secondary structure

    1
    768
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi756 – 7605

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4GXBX-ray1.80B735-768[»]
    ProteinModelPortaliQ01102.
    SMRiQ01102. Positions 42-199, 217-701.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini42 – 709668ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini734 – 76835CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei710 – 73324HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 158101C-type lectinPROSITE-ProRule annotationAdd
    BLAST
    Domaini159 – 19537EGF-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini198 – 25962Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini260 – 32162Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini322 – 38362Sushi 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini384 – 44562Sushi 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini446 – 50762Sushi 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini508 – 56962Sushi 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini578 – 63962Sushi 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini640 – 70162Sushi 8PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni759 – 76810Interaction with SNX17By similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi756 – 7594Endocytosis signalCurated

    Sequence similaritiesi

    Belongs to the selectin/LECAM family.Curated
    Contains 1 C-type lectin domain.PROSITE-ProRule annotation
    Contains 1 EGF-like domain.PROSITE-ProRule annotation
    Contains 8 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Sushi, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG242963.
    GeneTreeiENSGT00750000117319.
    HOGENOMiHOG000236254.
    HOVERGENiHBG052375.
    InParanoidiQ32MF1.
    KOiK06496.
    OMAiTYGVFTN.
    OrthoDBiEOG7DZ8J9.
    PhylomeDBiQ01102.
    TreeFamiTF326910.

    Family and domain databases

    Gene3Di3.10.100.10. 1 hit.
    InterProiIPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR002396. Selectin_superfamily.
    IPR000436. Sushi_SCR_CCP.
    [Graphical view]
    PfamiPF00008. EGF. 1 hit.
    PF00059. Lectin_C. 1 hit.
    PF00084. Sushi. 8 hits.
    [Graphical view]
    PRINTSiPR00343. SELECTIN.
    SMARTiSM00032. CCP. 8 hits.
    SM00034. CLECT. 1 hit.
    SM00181. EGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 1 hit.
    SSF57535. SSF57535. 8 hits.
    PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
    PS50041. C_TYPE_LECTIN_2. 1 hit.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS50923. SUSHI. 8 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q01102-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGCPKGSWT PRLRSVILGG AQLIWFSALI SELVNQKEVA AWTYNYSTKA    50
    YSWNNSRVFC RRHFTDLVAI QNKNEIAHLN DVIPFFNSYY WIGIRKINNK 100
    WTWVGTNKTL TEEAENWADN EPNNKKNNQD CVEIYIKSNS APGKWNDEPC 150
    FKRKRALCYT ASCQDMSCSN QGECIETIGS YTCSCYPGFY GPECEYVKEC 200
    GKVNIPQHVL MNCSHPLGEF SFNSQCTFSC AEGYELDGPG ELQCLASGIW 250
    TNNPPKCDAV QCQSLEAPPH GTMACMHPIA AFAYDSSCKF ECQPGYRARG 300
    SNTLHCTGSG QWSEPLPTCE AIACEPPEIP IHGSMDCVPS TGTFGYNSSC 350
    TFLCAEGFVL KGNDAIQCAD SGQWTAPAPF CEALQCPEFP VPSKAQVNCS 400
    DPFGTLTYQS VCSFSCDEGS LLVGASVIRC LATGHWNGAP PECQAVSCAP 450
    MLSPENGSMT CVQPLGNSTY KSTCQFMCDE GFYLSGPERL DCSPSGHWTG 500
    TPPTCEAIKC PGIFAPEQGN LDCSHVHGEF GVGSICHFSC NEDFELLGSE 550
    NVECTVSGRW SAPPPTCKGI TSLPAPAVRC PALTTPGQGT MSCQHHLGSF 600
    GPNTTCYFGC KTGFTLRGAN SLRCRASGQW TAVTPMCRAV KCSELHMDTA 650
    VAMNCSNPWG NFSYGSTCTF QCPEGQSLNG SVRATCREDG HWSDAMPTCQ 700
    AGTLTIQEAL TYLGGAVAST TGLAVGGTLL ALLRKRLRKK DDGKCPLNPH 750
    SHLGTYGVFT NAAYDPTP 768
    Length:768
    Mass (Da):83,099
    Last modified:April 1, 1993 - v1
    Checksum:iE5173074D2F66E68
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti724 – 7241A → E in AAA37712. (PubMed:1379089)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87861 mRNA. Translation: AAA40008.1.
    M72332 mRNA. Translation: AAA37712.1.
    BC109158 mRNA. Translation: AAI09159.1.
    BC109159 mRNA. Translation: AAI09160.1.
    CCDSiCCDS48422.1.
    PIRiA42755.
    RefSeqiNP_035477.1. NM_011347.2.
    UniGeneiMm.3337.

    Genome annotation databases

    EnsembliENSMUST00000162746; ENSMUSP00000123924; ENSMUSG00000026580.
    GeneIDi20344.
    KEGGimmu:20344.
    UCSCiuc007dhz.2. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    P-selectin

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87861 mRNA. Translation: AAA40008.1 .
    M72332 mRNA. Translation: AAA37712.1 .
    BC109158 mRNA. Translation: AAI09159.1 .
    BC109159 mRNA. Translation: AAI09160.1 .
    CCDSi CCDS48422.1.
    PIRi A42755.
    RefSeqi NP_035477.1. NM_011347.2.
    UniGenei Mm.3337.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4GXB X-ray 1.80 B 735-768 [» ]
    ProteinModelPortali Q01102.
    SMRi Q01102. Positions 42-199, 217-701.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi Q01102.
    ChEMBLi CHEMBL2455.

    PTM databases

    PhosphoSitei Q01102.

    Proteomic databases

    PRIDEi Q01102.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000162746 ; ENSMUSP00000123924 ; ENSMUSG00000026580 .
    GeneIDi 20344.
    KEGGi mmu:20344.
    UCSCi uc007dhz.2. mouse.

    Organism-specific databases

    CTDi 6403.
    MGIi MGI:98280. Selp.

    Phylogenomic databases

    eggNOGi NOG242963.
    GeneTreei ENSGT00750000117319.
    HOGENOMi HOG000236254.
    HOVERGENi HBG052375.
    InParanoidi Q32MF1.
    KOi K06496.
    OMAi TYGVFTN.
    OrthoDBi EOG7DZ8J9.
    PhylomeDBi Q01102.
    TreeFami TF326910.

    Enzyme and pathway databases

    Reactomei REACT_225233. Cell surface interactions at the vascular wall.

    Miscellaneous databases

    NextBioi 298177.
    PROi Q01102.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q01102.
    CleanExi MM_SELP.
    Genevestigatori Q01102.

    Family and domain databases

    Gene3Di 3.10.100.10. 1 hit.
    InterProi IPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR002396. Selectin_superfamily.
    IPR000436. Sushi_SCR_CCP.
    [Graphical view ]
    Pfami PF00008. EGF. 1 hit.
    PF00059. Lectin_C. 1 hit.
    PF00084. Sushi. 8 hits.
    [Graphical view ]
    PRINTSi PR00343. SELECTIN.
    SMARTi SM00032. CCP. 8 hits.
    SM00034. CLECT. 1 hit.
    SM00181. EGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    SSF57535. SSF57535. 8 hits.
    PROSITEi PS00615. C_TYPE_LECTIN_1. 1 hit.
    PS50041. C_TYPE_LECTIN_2. 1 hit.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS50923. SUSHI. 8 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the mouse endothelial selectins. Expression of both E- and P-selectin is inducible by tumor necrosis factor alpha."
      Weller A., Isenmann S., Vestweber D.
      J. Biol. Chem. 267:15176-15183(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    2. "Molecular cloning and analysis of in vivo expression of murine P-selectin."
      Sanders W.E. Jr., Wilson R.W., Ballantyne C.M., Beaudet A.L.
      Blood 80:795-800(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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 SELPLG.

    Entry informationi

    Entry nameiLYAM3_MOUSE
    AccessioniPrimary (citable) accession number: Q01102
    Secondary accession number(s): Q32MF1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 141 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

    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
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3