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UniProt functional annotation for P15151 | ||
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| UniProt code: P15151. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| Function: | |
Mediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors: CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. May also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Plays a role in mediating tumor cell invasion and migration. {ECO:0000269|PubMed:15471548, ECO:0000269|PubMed:15607800}. |
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| Function: | |
(Microbial infection) Acts as a receptor for poliovirus. May play a role in axonal transport of poliovirus, by targeting virion-PVR- containing endocytic vesicles to the microtubular network through interaction with DYNLT1. This interaction would drive the virus- containing vesicle to the axonal retrograde transport. {ECO:0000269|PubMed:2538245}. |
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| Function: | |
(Microbial infection) Acts as a receptor for Pseudorabies virus. {ECO:0000269|PubMed:9616127}. |
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| Function: | |
(Microbial infection) Is prevented to reach cell surface upon infection by Human cytomegalovirus /HHV-5, presumably to escape immune recognition of infected cell by NK cells. {ECO:0000269|PubMed:15640804}. |
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| Biophysicochemical properties: | |
Kinetic parameters: KM=72 nM for VTN; |
| Subunit: | |
Can form trans-heterodimers with NECTIN3. The extracellular domain interacts with VTN, CD226 and CD96. The cytoplasmic domain interacts with DYNLT1. Binds with high affinity to TIGIT. {ECO:0000269|PubMed:11437656, ECO:0000269|PubMed:11751937, ECO:0000269|PubMed:12759359, ECO:0000269|PubMed:15034010, ECO:0000269|PubMed:15039383, ECO:0000269|PubMed:15194795, ECO:0000269|PubMed:16216929, ECO:0000269|PubMed:19011627, ECO:0000269|PubMed:22421438}. |
| Subunit: | |
(Microbial infection) Interacts with poliovirus capsid proteins. {ECO:0000269|PubMed:2538245}. |
| Subunit: | |
(Microbial infection) Interacts with human cytomegalovirus /HHV-5 UL141 protein. {ECO:0000269|PubMed:15640804}. |
| Subunit: | |
(Microbial infection) Interacts with pseudorabies virus gD protein. {ECO:0000269|PubMed:9616127}. |
| Subcellular location: | |
[Isoform Alpha]: Cell membrane; Single-pass type I membrane protein. |
| Subcellular location: | |
[Isoform Delta]: Cell membrane; Single-pass type I membrane protein. |
| Subcellular location: | |
[Isoform Beta]: Secreted. |
| Subcellular location: | |
[Isoform Gamma]: Secreted. |
| Induction: | |
Transcriptionally regulated by SHH. {ECO:0000269|PubMed:11983699}. |
| Domain: | |
Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). The phosphorylated ITIM motif can bind the SH2 domain of several SH2- containing phosphatases. {ECO:0000269|PubMed:1851992}. |
| Ptm: | |
N-glycosylated. N-glycan at Asn-120: Hex5HexNAc4. {ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22171320}. |
| Ptm: | |
Phosphorylated by Src kinases on tyrosine residues in the ITIM motif upon ligation. Interaction with TIGIT is required for Phosphorylation. {ECO:0000269|PubMed:15194502, ECO:0000269|PubMed:22421438}. |
| Miscellaneous: | |
The V-type domain is necessary and sufficient for virus binding and uptake. |
| Similarity: | |
Belongs to the nectin family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.