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Showing Protein Sialic acid-binding Ig-like lectin 10 (HMDBP14320)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 0 metabolites
Identification
HMDB Protein ID HMDBP14320
Secondary Accession Numbers None
Name Sialic acid-binding Ig-like lectin 10
Synonyms
  1. Siglec-10
  2. Sialic acid-binding Ig-like lectin G
  3. Siglec-G
  4. mSiglec-G
Gene Name SIGLEC10
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid (PubMed:20038598). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, seems to act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules (By similarity). Involved in negative regulation of B-cell antigen receptor signaling and specifically acts on B1 cells to inhibit Ca(2+) signaling, cellular expansion and antibody secretion (PubMed:17572677). The inhibition of B cell activation is dependent on PTPN6/SHP-1 (PubMed:23836061). In association with CD24 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90 (PubMed:19264983). In association with CD24 may regulate the immune repsonse of natural killer (NK) cells (By similarity). Plays a role in the control of autoimmunity (PubMed:20200274). During initiation of adaptive immune responses by CD8-alpha(+) dendritic cells inhibits cross-presentation by impairing the formation of MHC class I-peptide complexes. The function seems to implicate recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex consequently promoting phagosomal acidification (PubMed:27548433).(Microbial infection) During infection by RNA viruses inhibits DDX58/RIG-I signaling in macrophages by promoting its CBL-dependent ubiquitination and degradation via PTPN11/SHP-2.
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
cell adhesion
negative regulation of inflammatory response to wounding
negative regulation of calcium-mediated signaling
negative regulation of immunoglobulin production
regulation of B cell proliferation
hematopoietic progenitor cell differentiation
innate immune response
adaptive immune response
regulation of immune response
Cellular Component
plasma membrane
integral to membrane
Molecular Function
SH2 domain binding
carbohydrate binding
phosphatase binding
sialic acid binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 688
Molecular Weight 76883.625
Theoretical pI 6.718
Pfam Domain Function
Signals
  • 1-17;
Transmembrane Regions
  • 544-564;
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q80ZE3
UniProtKB/Swiss-Prot Entry Name SIG10_MOUSE
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Huttlin EL, Jedrychowski MP, Elias JE, Goswami T, Rad R, Beausoleil SA, Villen J, Haas W, Sowa ME, Gygi SP: A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89. doi: 10.1016/j.cell.2010.12.001. [PubMed:21183079 ]
  2. Church DM, Goodstadt L, Hillier LW, Zody MC, Goldstein S, She X, Bult CJ, Agarwala R, Cherry JL, DiCuccio M, Hlavina W, Kapustin Y, Meric P, Maglott D, Birtle Z, Marques AC, Graves T, Zhou S, Teague B, Potamousis K, Churas C, Place M, Herschleb J, Runnheim R, Forrest D, Amos-Landgraf J, Schwartz DC, Cheng Z, Lindblad-Toh K, Eichler EE, Ponting CP: Lineage-specific biology revealed by a finished genome assembly of the mouse. PLoS Biol. 2009 May 5;7(5):e1000112. doi: 10.1371/journal.pbio.1000112. Epub 2009 May 26. [PubMed:19468303 ]
  3. Chen GY, Tang J, Zheng P, Liu Y: CD24 and Siglec-10 selectively repress tissue damage-induced immune responses. Science. 2009 Mar 27;323(5922):1722-5. doi: 10.1126/science.1168988. Epub 2009 Mar 5. [PubMed:19264983 ]
  4. Aizawa H, Zimmermann N, Carrigan PE, Lee JJ, Rothenberg ME, Bochner BS: Molecular analysis of human Siglec-8 orthologs relevant to mouse eosinophils: identification of mouse orthologs of Siglec-5 (mSiglec-F) and Siglec-10 (mSiglec-G). Genomics. 2003 Nov;82(5):521-30. doi: 10.1016/s0888-7543(03)00171-x. [PubMed:14559209 ]
  5. Hoffmann A, Kerr S, Jellusova J, Zhang J, Weisel F, Wellmann U, Winkler TH, Kneitz B, Crocker PR, Nitschke L: Siglec-G is a B1 cell-inhibitory receptor that controls expansion and calcium signaling of the B1 cell population. Nat Immunol. 2007 Jul;8(7):695-704. doi: 10.1038/ni1480. Epub 2007 Jun 17. [PubMed:17572677 ]
  6. Duong BH, Tian H, Ota T, Completo G, Han S, Vela JL, Ota M, Kubitz M, Bovin N, Paulson JC, Nemazee D: Decoration of T-independent antigen with ligands for CD22 and Siglec-G can suppress immunity and induce B cell tolerance in vivo. J Exp Med. 2010 Jan 18;207(1):173-87. doi: 10.1084/jem.20091873. Epub 2009 Dec 28. [PubMed:20038598 ]
  7. Jellusova J, Wellmann U, Amann K, Winkler TH, Nitschke L: CD22 x Siglec-G double-deficient mice have massively increased B1 cell numbers and develop systemic autoimmunity. J Immunol. 2010 Apr 1;184(7):3618-27. doi: 10.4049/jimmunol.0902711. Epub 2010 Mar 3. [PubMed:20200274 ]
  8. Chen W, Han C, Xie B, Hu X, Yu Q, Shi L, Wang Q, Li D, Wang J, Zheng P, Liu Y, Cao X: Induction of Siglec-G by RNA viruses inhibits the innate immune response by promoting RIG-I degradation. Cell. 2013 Jan 31;152(3):467-78. doi: 10.1016/j.cell.2013.01.011. [PubMed:23374343 ]
  9. Hutzler S, Ozgor L, Naito-Matsui Y, Klasener K, Winkler TH, Reth M, Nitschke L: The ligand-binding domain of Siglec-G is crucial for its selective inhibitory function on B1 cells. J Immunol. 2014 Jun 1;192(11):5406-14. doi: 10.4049/jimmunol.1302875. Epub 2014 Apr 30. [PubMed:24790146 ]
  10. Ding Y, Guo Z, Liu Y, Li X, Zhang Q, Xu X, Gu Y, Zhang Y, Zhao D, Cao X: The lectin Siglec-G inhibits dendritic cell cross-presentation by impairing MHC class I-peptide complex formation. Nat Immunol. 2016 Oct;17(10):1167-75. doi: 10.1038/ni.3535. Epub 2016 Aug 22. [PubMed:27548433 ]