Q96LC7 · SIG10_HUMAN

  • Protein
    Sialic acid-binding Ig-like lectin 10
  • Gene
    SIGLEC10
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

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 (By similarity).
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 (PubMed:11284738, PubMed:12163025).
Involved in negative regulation of B-cell antigen receptor signaling. The inhibition of B cell activation is dependent on PTPN6/SHP-1 (By similarity).
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 (By similarity).
In association with CD24 may regulate the immune repsonse of natural killer (NK) cells (PubMed:25450598).
Plays a role in the control of autoimmunity (By similarity).
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 (By similarity).

Features

Showing features for binding site.

169750100150200250300350400450500550600650
TypeIDPosition(s)Description
Binding site119N-acetylneuraminate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componentplasma membrane
Molecular Functioncarbohydrate binding
Molecular Functionphosphatase binding
Molecular FunctionSH2 domain binding
Molecular Functionsialic acid binding
Biological Processadaptive immune response
Biological Processcell adhesion
Biological Processinnate immune response
Biological Processnegative regulation of inflammatory response to wounding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Sialic acid-binding Ig-like lectin 10
  • Short names
    Siglec-10
  • Alternative names
    • Siglec-like protein 2

Gene names

    • Name
      SIGLEC10
    • Synonyms
      SLG2
    • ORF names
      UNQ477/PRO940

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q96LC7
  • Secondary accessions
    • A8K1I5
    • A8K3C7
    • C9JJ33
    • C9JM10
    • F8W917

Proteomes

Organism-specific databases

Subcellular Location

Isoform 1

Cell membrane ; Single-pass type I membrane protein

Isoform 2

Cell membrane ; Single-pass type I membrane protein

Isoform 3

Cell membrane ; Single-pass type I membrane protein

Isoform 4

Cell membrane ; Single-pass type I membrane protein

Isoform 5

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain17-550Extracellular
Transmembrane551-571Helical
Topological domain572-697Cytoplasmic

Keywords

Disease & Variants

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis119Disrupts interaction with CD24.
Natural variantVAR_019955226in dbSNP:rs9304711
Natural variantVAR_019956520in dbSNP:rs1833785
Mutagenesis667Abolishes binding to PTPN6.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 861 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
Signal1-16UniProt
ChainPRO_000001495017-697UniProtSialic acid-binding Ig-like lectin 10
Disulfide bond36↔173UniProt
Disulfide bond41↔101UniProt
Glycosylation100UniProtN-linked (GlcNAc...) asparagine
Disulfide bond164↔215UniProt
Disulfide bond276↔323UniProt
Glycosylation355UniProtN-linked (GlcNAc...) asparagine
Glycosylation364UniProtN-linked (GlcNAc...) asparagine
Disulfide bond380↔425UniProt
Glycosylation486UniProtN-linked (GlcNAc...) asparagine
Glycosylation504UniProtN-linked (GlcNAc...) asparagine
Modified residue (large scale data)630PRIDEPhosphoserine
Modified residue (large scale data)645PRIDEPhosphoserine
Modified residue667UniProtPhosphotyrosine

Post-translational modification

Phosphorylation of Tyr-667 is involved in binding to PTPN6.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation). Isoform 5 is found to be the most abundant isoform. Found in lymph node, lung, ovary and appendix. Isoform 1 is found at high levels and isoform 2 at lower levels in bone marrow, spleen and spinal chord. Isoform 2 is also found in brain. Isoform 4 is specifically found in natural killer cells.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with PTPN6/SHP-1 upon phosphorylation (PubMed:12163025).
Interacts with NCF1 (By similarity).
Interacts with CD24; the probable CD24:SIGLEC10 complex is proposed to inhibit HGMB1-mediated tissue damage immune response. Interacts with HMGB1; the interaction is dependent on CD24 (PubMed:19264983).
Interacts with RIGI, CBL and PTPN11 (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
XENO Q96LC7S P0DTC22EBI-8502656, EBI-25474821

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, motif, region, compositional bias.

TypeIDPosition(s)Description
Domain18-121Ig-like V-type
Domain146-231Ig-like C2-type 1
Domain251-339Ig-like C2-type 2
Domain344-441Ig-like C2-type 3
Motif595-600ITIM motif 1
Region606-697Disordered
Compositional bias633-666Polar residues
Motif665-670ITIM motif 2

Domain

Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (9)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 9 isoforms produced by Alternative splicing.

Q96LC7-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    1
  • Synonyms
    Long
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    697
  • Mass (Da)
    76,592
  • Last updated
    2006-11-28 v3
  • Checksum
    E1B787F34CF7201A
MLLPLLLSSLLGGSQAMDGRFWIRVQESVMVPEGLCISVPCSFSYPRQDWTGSTPAYGYWFKAVTETTKGAPVATNHQSREVEMSTRGRFQLTGDPAKGNCSLVIRDAQMQDESQYFFRVERGSYVRYNFMNDGFFLKVTALTQKPDVYIPETLEPGQPVTVICVFNWAFEECPPPSFSWTGAALSSQGTKPTTSHFSVLSFTPRPQDHNTDLTCHVDFSRKGVSAQRTVRLRVAYAPRDLVISISRDNTPALEPQPQGNVPYLEAQKGQFLRLLCAADSQPPATLSWVLQNRVLSSSHPWGPRPLGLELPGVKAGDSGRYTCRAENRLGSQQRALDLSVQYPPENLRVMVSQANRTVLENLGNGTSLPVLEGQSLCLVCVTHSSPPARLSWTQRGQVLSPSQPSDPGVLELPRVQVEHEGEFTCHARHPLGSQHVSLSLSVHYSPKLLGPSCSWEAEGLHCSCSSQASPAPSLRWWLGEELLEGNSSQDSFEVTPSSAGPWANSSLSLHGGLSSGLRLRCEAWNVHGAQSGSILQLPDKKGLISTAFSNGAFLGIGITALLFLCLALIIMKILPKRRTQTETPRPRFSRHSTILDYINVVPTAGPLAQKRNQKATPNSPRTPLPPGAPSPESKKNQKKQYQLPSFPEPKSSTQAPESQESQEELHYATLNFPGVRPRPEARMPKGTQADYAEVKFQ

Q96LC7-2

  • Name
    2
  • Synonyms
    Short, Sv1
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q96LC7-3

  • Name
    3
  • Synonyms
    Sv3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q96LC7-4

  • Name
    4
  • Synonyms
    Sv4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q96LC7-5

  • Name
    5
  • Synonyms
    Sv2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 140-185: TALTQKPDVYIPETLEPGQPVTVICVFNWAFEECPPPSFSWTGAAL → TGMRWGGNPCLSHWGGTLGTAYGLSREGSQGPLQHKNLPPRSLSQP
    • 186-697: Missing

Q96LC7-6

Q96LC7-7

Q96LC7-8

Q96LC7-9

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E9PKV9E9PKV9_HUMANSIGLEC10155
E9PL79E9PL79_HUMANSIGLEC10512
E9PJA1E9PJA1_HUMANSIGLEC10186

Features

Showing features for sequence conflict, alternative sequence, compositional bias.

TypeIDPosition(s)Description
Sequence conflict28in Ref. 4; AAK51124
Alternative sequenceVSP_002561125-214in isoform 4
Sequence conflict127in Ref. 5; AAQ88703
Sequence conflict134in Ref. 4; AAK51124
Alternative sequenceVSP_002562140-185in isoform 5
Alternative sequenceVSP_045365141-188in isoform 7
Alternative sequenceVSP_002564141-198in isoform 3, isoform 6 and isoform 8
Alternative sequenceVSP_045888146-228in isoform 9
Alternative sequenceVSP_002563186-697in isoform 5
Alternative sequenceVSP_045853252in isoform 8
Alternative sequenceVSP_045854253-342in isoform 8
Sequence conflict268in Ref. 6; AK303514
Sequence conflict344in Ref. 3; AAK92542
Sequence conflict440in Ref. 4; AAK51124
Alternative sequenceVSP_002565445-539in isoform 2, isoform 6, isoform 7, isoform 8 and isoform 9
Sequence conflict564in Ref. 6; AK303514
Sequence conflict587in Ref. 3; AAK92542
Sequence conflict624in Ref. 5; AAQ88703
Sequence conflict625in Ref. 3; AAK92542
Compositional bias633-666Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY029277
EMBL· GenBank· DDBJ
AAK40255.1
EMBL· GenBank· DDBJ
Genomic DNA
AY029277
EMBL· GenBank· DDBJ
AAK40256.1
EMBL· GenBank· DDBJ
Genomic DNA
AF310233
EMBL· GenBank· DDBJ
AAK55139.1
EMBL· GenBank· DDBJ
mRNA
AF311905
EMBL· GenBank· DDBJ
AAK92542.1
EMBL· GenBank· DDBJ
mRNA
AY032685
EMBL· GenBank· DDBJ
AAK51124.1
EMBL· GenBank· DDBJ
mRNA
AY358337
EMBL· GenBank· DDBJ
AAQ88703.1
EMBL· GenBank· DDBJ
mRNA
AK289900
EMBL· GenBank· DDBJ
BAF82589.1
EMBL· GenBank· DDBJ
mRNA
AK290542
EMBL· GenBank· DDBJ
BAF83231.1
EMBL· GenBank· DDBJ
mRNA
AK303514
EMBL· GenBank· DDBJ
-mRNA No translation available.
AC008750
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC009955
EMBL· GenBank· DDBJ
AAH09955.2
EMBL· GenBank· DDBJ
mRNA
BC101725
EMBL· GenBank· DDBJ
AAI01726.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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