Q96LC7 · SIG10_HUMAN
- ProteinSialic acid-binding Ig-like lectin 10
- GeneSIGLEC10
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids697 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | plasma membrane | |
Molecular Function | carbohydrate binding | |
Molecular Function | phosphatase binding | |
Molecular Function | SH2 domain binding | |
Molecular Function | sialic acid binding | |
Biological Process | adaptive immune response | |
Biological Process | cell adhesion | |
Biological Process | innate immune response | |
Biological Process | negative regulation of inflammatory response to wounding |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSialic acid-binding Ig-like lectin 10
- Short namesSiglec-10
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96LC7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 1
Isoform 2
Isoform 3
Isoform 4
Isoform 5
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 17-550 | Extracellular | ||||
Sequence: MDGRFWIRVQESVMVPEGLCISVPCSFSYPRQDWTGSTPAYGYWFKAVTETTKGAPVATNHQSREVEMSTRGRFQLTGDPAKGNCSLVIRDAQMQDESQYFFRVERGSYVRYNFMNDGFFLKVTALTQKPDVYIPETLEPGQPVTVICVFNWAFEECPPPSFSWTGAALSSQGTKPTTSHFSVLSFTPRPQDHNTDLTCHVDFSRKGVSAQRTVRLRVAYAPRDLVISISRDNTPALEPQPQGNVPYLEAQKGQFLRLLCAADSQPPATLSWVLQNRVLSSSHPWGPRPLGLELPGVKAGDSGRYTCRAENRLGSQQRALDLSVQYPPENLRVMVSQANRTVLENLGNGTSLPVLEGQSLCLVCVTHSSPPARLSWTQRGQVLSPSQPSDPGVLELPRVQVEHEGEFTCHARHPLGSQHVSLSLSVHYSPKLLGPSCSWEAEGLHCSCSSQASPAPSLRWWLGEELLEGNSSQDSFEVTPSSAGPWANSSLSLHGGLSSGLRLRCEAWNVHGAQSGSILQLPDKKGLISTAFSN | ||||||
Transmembrane | 551-571 | Helical | ||||
Sequence: GAFLGIGITALLFLCLALIIM | ||||||
Topological domain | 572-697 | Cytoplasmic | ||||
Sequence: KILPKRRTQTETPRPRFSRHSTILDYINVVPTAGPLAQKRNQKATPNSPRTPLPPGAPSPESKKNQKKQYQLPSFPEPKSSTQAPESQESQEELHYATLNFPGVRPRPEARMPKGTQADYAEVKFQ |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 119 | Disrupts interaction with CD24. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_019955 | 226 | in dbSNP:rs9304711 | |||
Sequence: A → V | ||||||
Natural variant | VAR_019956 | 520 | in dbSNP:rs1833785 | |||
Sequence: R → S | ||||||
Mutagenesis | 667 | Abolishes binding to PTPN6. | ||||
Sequence: Y → F |
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.
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.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-16 | UniProt | |||||
Sequence: MLLPLLLSSLLGGSQA | |||||||
Chain | PRO_0000014950 | 17-697 | UniProt | Sialic acid-binding Ig-like lectin 10 | |||
Sequence: MDGRFWIRVQESVMVPEGLCISVPCSFSYPRQDWTGSTPAYGYWFKAVTETTKGAPVATNHQSREVEMSTRGRFQLTGDPAKGNCSLVIRDAQMQDESQYFFRVERGSYVRYNFMNDGFFLKVTALTQKPDVYIPETLEPGQPVTVICVFNWAFEECPPPSFSWTGAALSSQGTKPTTSHFSVLSFTPRPQDHNTDLTCHVDFSRKGVSAQRTVRLRVAYAPRDLVISISRDNTPALEPQPQGNVPYLEAQKGQFLRLLCAADSQPPATLSWVLQNRVLSSSHPWGPRPLGLELPGVKAGDSGRYTCRAENRLGSQQRALDLSVQYPPENLRVMVSQANRTVLENLGNGTSLPVLEGQSLCLVCVTHSSPPARLSWTQRGQVLSPSQPSDPGVLELPRVQVEHEGEFTCHARHPLGSQHVSLSLSVHYSPKLLGPSCSWEAEGLHCSCSSQASPAPSLRWWLGEELLEGNSSQDSFEVTPSSAGPWANSSLSLHGGLSSGLRLRCEAWNVHGAQSGSILQLPDKKGLISTAFSNGAFLGIGITALLFLCLALIIMKILPKRRTQTETPRPRFSRHSTILDYINVVPTAGPLAQKRNQKATPNSPRTPLPPGAPSPESKKNQKKQYQLPSFPEPKSSTQAPESQESQEELHYATLNFPGVRPRPEARMPKGTQADYAEVKFQ | |||||||
Disulfide bond | 36↔173 | UniProt | |||||
Sequence: CISVPCSFSYPRQDWTGSTPAYGYWFKAVTETTKGAPVATNHQSREVEMSTRGRFQLTGDPAKGNCSLVIRDAQMQDESQYFFRVERGSYVRYNFMNDGFFLKVTALTQKPDVYIPETLEPGQPVTVICVFNWAFEEC | |||||||
Disulfide bond | 41↔101 | UniProt | |||||
Sequence: CSFSYPRQDWTGSTPAYGYWFKAVTETTKGAPVATNHQSREVEMSTRGRFQLTGDPAKGNC | |||||||
Glycosylation | 100 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 164↔215 | UniProt | |||||
Sequence: CVFNWAFEECPPPSFSWTGAALSSQGTKPTTSHFSVLSFTPRPQDHNTDLTC | |||||||
Disulfide bond | 276↔323 | UniProt | |||||
Sequence: CAADSQPPATLSWVLQNRVLSSSHPWGPRPLGLELPGVKAGDSGRYTC | |||||||
Glycosylation | 355 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 364 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 380↔425 | UniProt | |||||
Sequence: CVTHSSPPARLSWTQRGQVLSPSQPSDPGVLELPRVQVEHEGEFTC | |||||||
Glycosylation | 486 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 504 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 630 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 645 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 667 | UniProt | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q96LC7 | S P0DTC2 | 2 | EBI-8502656, EBI-25474821 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-121 | Ig-like V-type | ||||
Sequence: DGRFWIRVQESVMVPEGLCISVPCSFSYPRQDWTGSTPAYGYWFKAVTETTKGAPVATNHQSREVEMSTRGRFQLTGDPAKGNCSLVIRDAQMQDESQYFFRVE | ||||||
Domain | 146-231 | Ig-like C2-type 1 | ||||
Sequence: PDVYIPETLEPGQPVTVICVFNWAFEECPPPSFSWTGAALSSQGTKPTTSHFSVLSFTPRPQDHNTDLTCHVDFSRKGVSAQRTVR | ||||||
Domain | 251-339 | Ig-like C2-type 2 | ||||
Sequence: PALEPQPQGNVPYLEAQKGQFLRLLCAADSQPPATLSWVLQNRVLSSSHPWGPRPLGLELPGVKAGDSGRYTCRAENRLGSQQRALDLS | ||||||
Domain | 344-441 | Ig-like C2-type 3 | ||||
Sequence: PENLRVMVSQANRTVLENLGNGTSLPVLEGQSLCLVCVTHSSPPARLSWTQRGQVLSPSQPSDPGVLELPRVQVEHEGEFTCHARHPLGSQHVSLSLS | ||||||
Motif | 595-600 | ITIM motif 1 | ||||
Sequence: LDYINV | ||||||
Region | 606-697 | Disordered | ||||
Sequence: PLAQKRNQKATPNSPRTPLPPGAPSPESKKNQKKQYQLPSFPEPKSSTQAPESQESQEELHYATLNFPGVRPRPEARMPKGTQADYAEVKFQ | ||||||
Compositional bias | 633-666 | Polar residues | ||||
Sequence: SKKNQKKQYQLPSFPEPKSSTQAPESQESQEELH | ||||||
Motif | 665-670 | ITIM motif 2 | ||||
Sequence: LHYATL |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe 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.
- Name1
- SynonymsLong
- Length697
- Mass (Da)76,592
- Last updated2006-11-28 v3
- ChecksumE1B787F34CF7201A
Q96LC7-2
- Name2
- SynonymsShort, Sv1
- Differences from canonical
- 445-539: Missing
Q96LC7-3
- Name3
- SynonymsSv3
- Differences from canonical
- 141-198: Missing
Q96LC7-4
- Name4
- SynonymsSv4
- Differences from canonical
- 125-214: Missing
Q96LC7-5
- Name5
- SynonymsSv2
Q96LC7-6
- Name6
Q96LC7-7
- Name7
Q96LC7-8
- Name8
Q96LC7-9
- Name9
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 28 | in Ref. 4; AAK51124 | ||||
Sequence: S → P | ||||||
Alternative sequence | VSP_002561 | 125-214 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 127 | in Ref. 5; AAQ88703 | ||||
Sequence: R → T | ||||||
Sequence conflict | 134 | in Ref. 4; AAK51124 | ||||
Sequence: G → R | ||||||
Alternative sequence | VSP_002562 | 140-185 | in isoform 5 | |||
Sequence: TALTQKPDVYIPETLEPGQPVTVICVFNWAFEECPPPSFSWTGAAL → TGMRWGGNPCLSHWGGTLGTAYGLSREGSQGPLQHKNLPPRSLSQP | ||||||
Alternative sequence | VSP_045365 | 141-188 | in isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_002564 | 141-198 | in isoform 3, isoform 6 and isoform 8 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_045888 | 146-228 | in isoform 9 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_002563 | 186-697 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_045853 | 252 | in isoform 8 | |||
Sequence: A → D | ||||||
Alternative sequence | VSP_045854 | 253-342 | in isoform 8 | |||
Sequence: Missing | ||||||
Sequence conflict | 268 | in Ref. 6; AK303514 | ||||
Sequence: K → R | ||||||
Sequence conflict | 344 | in Ref. 3; AAK92542 | ||||
Sequence: P → S | ||||||
Sequence conflict | 440 | in Ref. 4; AAK51124 | ||||
Sequence: L → P | ||||||
Alternative sequence | VSP_002565 | 445-539 | in isoform 2, isoform 6, isoform 7, isoform 8 and isoform 9 | |||
Sequence: Missing | ||||||
Sequence conflict | 564 | in Ref. 6; AK303514 | ||||
Sequence: L → P | ||||||
Sequence conflict | 587 | in Ref. 3; AAK92542 | ||||
Sequence: R → K | ||||||
Sequence conflict | 624 | in Ref. 5; AAQ88703 | ||||
Sequence: L → P | ||||||
Sequence conflict | 625 | in Ref. 3; AAK92542 | ||||
Sequence: P → S | ||||||
Compositional bias | 633-666 | Polar residues | ||||
Sequence: SKKNQKKQYQLPSFPEPKSSTQAPESQESQEELH |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |