Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Selp. (This text reflects annotations as of Thursday, July 24, 2014.)

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a 140 kDa protein that is stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. This protein redistributes to the plasma membrane during platelet activation and degranulation and mediates the interaction of activated endothelial cells or platelets with leukocytes. The membrane protein is a calcium-dependent receptor that binds to sialylated forms of Lewis blood group carbohydrate antigens on neutrophils and monocytes. Alternative splice variants may occur but are not well documented. [provided by RefSeq, Jul 2008]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Selp
  • performs the following molecular functions:
    • calcium-dependent protein binding ^[9]
    • glycoprotein binding ^[1]
    • sialic acid binding ^[1]
  • is located in the following cellular components:
    • external side of plasma membrane ^{[1, 6, 11, 12]}
    • membrane ^{[2, 5]}
• The gene product of Selp has been shown to bind to the gene products of Cd24a. ^{[1, 4, 8, 9]}
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Selp
  • participates in the following biological processes:
    • heterophilic cell-cell adhesion ^{[1, 7]}
    • inflammatory response ^[5]
    • leukocyte cell-cell adhesion ^{[1, 7]}
    • leukocyte migration ^[3]
    • leukocyte tethering or rolling ^[2]
    • positive regulation of leukocyte migration ^[6]
    • positive regulation of platelet activation ^[10]
• Researchers have inferred, based on genetic interactions, that the gene product of Selp
  • participates in the following biological processes:
    • positive regulation of leukocyte migration based on interactions with Sele ^[6]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Selp:
  • participates in the following biological processes:
    • blood vessel morphogenesis
    • cellular response to interleukin-6
    • inflammatory response
    • leukocyte cell-cell adhesion
    • leukocyte migration
    • positive regulation of cell adhesion
    • positive regulation of phosphatidylinositol 3-kinase signaling
    • regulation of cellular extravasation
    • regulation of integrin activation
    • single organismal cell-cell adhesion
  • performs the following molecular functions:
    • fucose binding
    • heparin binding
    • lipopolysaccharide binding
    • oligosaccharide binding
    • sialic acid binding
  • is located in the following cellular components:
    • cytoplasm
    • external side of plasma membrane
    • extracellular space
    • nucleus
    • platelet alpha granule membrane

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Summary text based on GO annotations supported by structural data

• Selp encodes a protein or proteins that contain the following InterPro domains: C-type lectin, C-type lectin fold, C-type lectin, conserved site, C-type lectin-like, EGF-like, conserved site, Epidermal growth factor-like domain, Selectin superfamily, Sushi/SCR/CCP, indicating that the gene product:
  • participates in the following biological processes:
    • cell adhesion
  • performs the following molecular functions:
    • carbohydrate binding

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Selp indicates that it:
  • participates in the following biological processes:
    • cell adhesion
  • is located in the following cellular components:
    • integral component of membrane

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References

1. Aigner S et al. (1995) Heat stable antigen (mouse CD24) supports myeloid cell binding to endothelial and platelet P-selectin. Int Immunol, 7:1557-65. (PubMed:8562500)
2. Dole VS et al. (2005) Activated platelets induce Weibel-Palade-body secretion and leukocyte rolling in vivo: role of P-selectin. Blood, 106:2334-9. (PubMed:15956287)
3. Fernekorn U et al. (2004) Functional involvement of P-selectin and MAdCAM-1 in the recruitment of alpha4beta7-integrin-expressing monocyte-like cells to the pregnant mouse uterus. Eur J Immunol, 34:3423-33. (PubMed:15484189)
4. Ghai R et al. (2013) Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins. Proc Natl Acad Sci U S A, 110:E643-52. (PubMed:23382219)
5. Mayadas TN et al. (1993) Leukocyte rolling and extravasation are severely compromised in P selectin-deficient mice. Cell, 74:541-54. (PubMed:7688665)
6. Mullaly SC et al. (2006) The role of TLR2 in vivo following challenge with Staphylococcus aureus and prototypic ligands. J Immunol, 177:8154-63. (PubMed:17114491)
7. Ruppert M et al. (1995) The L1 adhesion molecule is a cellular ligand for VLA-5. J Cell Biol, 131:1881-91. (PubMed:8557754)
8. Sammar M et al. (1997) Heat-stable antigen (mouse CD24) in the brain: dual but distinct interaction with P-selectin and L1. Biochim Biophys Acta, 1337:287-94. (PubMed:9048906)
9. Sammar M et al. (1994) Heat-stable antigen (CD24) as ligand for mouse P-selectin. Int Immunol, 6:1027-36. (PubMed:7524641)
10. Stahl AL et al. (2006) Lipopolysaccharide from enterohemorrhagic Escherichia coli binds to platelets through TLR4 and CD62 and is detected on circulating platelets in patients with hemolytic uremic syndrome. Blood, 108:167-76. (PubMed:16514062)
11. Stone EL et al. (2009) Glycosyltransferase function in core 2-type protein O glycosylation. Mol Cell Biol, 29:3770-82. (PubMed:19349303)
12. Vogel KU et al. (2013) Roquin Paralogs 1 and 2 Redundantly Repress the Icos and Ox40 Costimulator mRNAs and Control Follicular Helper T Cell Differentiation. Immunity, 38:655-68. (PubMed:23583643)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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