Q91Y57 · SIG12_MOUSE
- ProteinSialic acid-binding Ig-like lectin 12
- GeneSiglec12
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids467 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Putative adhesion molecule that mediates sialic-acid dependent binding to cells. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may 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.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | external side of plasma membrane | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | monosaccharide binding | |
Molecular Function | sialic acid binding | |
Biological Process | cell adhesion | |
Biological Process | inflammatory response | |
Biological Process | negative regulation of inflammatory response | |
Biological Process | negative regulation of phagocytosis, engulfment | |
Biological Process | phagocytosis, engulfment |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSialic acid-binding Ig-like lectin 12
- Short namesSiglec-12
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ91Y57
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 19-353 | Extracellular | ||||
Sequence: QNPQEVFTLNVERKVVVQEGLCVLVPCNFSYLKKRLTDWTDSDPVHGFWYREGTDRRKDSIVATNNPIRKAVKETRNRFFLLGDPWRNDCSLNIREIRKKDAGLYFFRLERGKTKYNYMWDKMTLVVTALTNTPQILLPETLEAGHPSNLTCSVPWDCGWTAPPIFSWTGTSVSFLSTNTTGSSVLTITPQPQDHGTNLTCQVTLPGTNVSTRMTIRLNVSYAPKNLTVTIYQGADSVSTILKNGSSLPISEGQSLRLICSTDSYPPANLSWSWDNLTLCPSKLSKPGLLELFPVHLKHGGVYTCQAQHALGSQHISLSLSPQSSATLSEMMMGT | ||||||
Transmembrane | 354-374 | Helical | ||||
Sequence: FVGSGVTALLFLSVCILLLAV | ||||||
Topological domain | 375-467 | Cytoplasmic | ||||
Sequence: RSYRRKPARPAVVAPHPDALKVSVSQNPLVESQADDSSEPLPSILEAAPSSTEEEIHYATLSFHEMKPMNLWGQQDTTTEYSEIKFPQRTAWP |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 432 | Abolishes binding to PTPN6 and PTPN11. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 455 | Reduces binding to PTPN6. | ||||
Sequence: Y → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 35 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MLLLLLLLLLWGIKGVEG | ||||||
Chain | PRO_0000014954 | 19-467 | Sialic acid-binding Ig-like lectin 12 | |||
Sequence: QNPQEVFTLNVERKVVVQEGLCVLVPCNFSYLKKRLTDWTDSDPVHGFWYREGTDRRKDSIVATNNPIRKAVKETRNRFFLLGDPWRNDCSLNIREIRKKDAGLYFFRLERGKTKYNYMWDKMTLVVTALTNTPQILLPETLEAGHPSNLTCSVPWDCGWTAPPIFSWTGTSVSFLSTNTTGSSVLTITPQPQDHGTNLTCQVTLPGTNVSTRMTIRLNVSYAPKNLTVTIYQGADSVSTILKNGSSLPISEGQSLRLICSTDSYPPANLSWSWDNLTLCPSKLSKPGLLELFPVHLKHGGVYTCQAQHALGSQHISLSLSPQSSATLSEMMMGTFVGSGVTALLFLSVCILLLAVRSYRRKPARPAVVAPHPDALKVSVSQNPLVESQADDSSEPLPSILEAAPSSTEEEIHYATLSFHEMKPMNLWGQQDTTTEYSEIKFPQRTAWP | ||||||
Disulfide bond | 40↔176 | |||||
Sequence: CVLVPCNFSYLKKRLTDWTDSDPVHGFWYREGTDRRKDSIVATNNPIRKAVKETRNRFFLLGDPWRNDCSLNIREIRKKDAGLYFFRLERGKTKYNYMWDKMTLVVTALTNTPQILLPETLEAGHPSNLTCSVPWDC | ||||||
Disulfide bond | 45↔108 | |||||
Sequence: CNFSYLKKRLTDWTDSDPVHGFWYREGTDRRKDSIVATNNPIRKAVKETRNRFFLLGDPWRNDC | ||||||
Glycosylation | 46 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 167 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 170↔219 | |||||
Sequence: CSVPWDCGWTAPPIFSWTGTSVSFLSTNTTGSSVLTITPQPQDHGTNLTC | ||||||
Glycosylation | 197 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 216 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 227 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 237 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 244 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 262 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 278↔323 | |||||
Sequence: CSTDSYPPANLSWSWDNLTLCPSKLSKPGLLELFPVHLKHGGVYTC | ||||||
Glycosylation | 287 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 294 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 432 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 455 | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Phosphorylation of Tyr-432 is required for binding to PTPN6 and PTPN11. Phosphorylation of Tyr-455 is involved in binding to PTPN6. Tyr-432 needs to be phosphorylated prior to Tyr-455.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed by monocytic/myeloid lineage cells. Found at higher levels in spleen, liver and heart. Found at lower levels in kidney and lung.
Gene expression databases
Interaction
Subunit
Homodimer; disulfide-linked. Interacts with PTPN6/SHP-1 and PTPN11/SHP-2 upon phosphorylation.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q91Y57 | Tlr4 Q9QUK6 | 3 | EBI-16826475, EBI-1534575 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 21-141 | Ig-like V-type | ||||
Sequence: PQEVFTLNVERKVVVQEGLCVLVPCNFSYLKKRLTDWTDSDPVHGFWYREGTDRRKDSIVATNNPIRKAVKETRNRFFLLGDPWRNDCSLNIREIRKKDAGLYFFRLERGKTKYNYMWDKM | ||||||
Domain | 152-239 | Ig-like C2-type 1 | ||||
Sequence: PQILLPETLEAGHPSNLTCSVPWDCGWTAPPIFSWTGTSVSFLSTNTTGSSVLTITPQPQDHGTNLTCQVTLPGTNVSTRMTIRLNVS | ||||||
Domain | 242-339 | Ig-like C2-type 2 | ||||
Sequence: PKNLTVTIYQGADSVSTILKNGSSLPISEGQSLRLICSTDSYPPANLSWSWDNLTLCPSKLSKPGLLELFPVHLKHGGVYTCQAQHALGSQHISLSLS | ||||||
Motif | 430-435 | ITIM motif | ||||
Sequence: IHYATL | ||||||
Motif | 453-458 | SLAM-like motif | ||||
Sequence: TEYSEI |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length467
- Mass (Da)51,901
- Last updated2011-07-27 v3
- ChecksumE220C29755FE21DE
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0U1RPP9 | A0A0U1RPP9_MOUSE | Siglece | 221 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 2 | in Ref. 2; AAK49917 | ||||
Sequence: L → M | ||||||
Sequence conflict | 24 | in Ref. 2; AAK49917 | ||||
Sequence: V → G | ||||||
Sequence conflict | 102 | in Ref. 2; AAK49917 | ||||
Sequence: D → E | ||||||
Sequence conflict | 234 | in Ref. 1; AAG38598 | ||||
Sequence: I → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF317298 EMBL· GenBank· DDBJ | AAG38598.1 EMBL· GenBank· DDBJ | mRNA | ||
AF329269 EMBL· GenBank· DDBJ | AAK49917.1 EMBL· GenBank· DDBJ | mRNA | ||
AC151989 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |