UniProt functional annotation for P23468

UniProt code: P23468.

Organism: Homo sapiens (Human).
Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
 
Function: Can bidirectionally induce pre- and post-synaptic differentiation of neurons by mediating interaction with IL1RAP and IL1RAPL1 trans-synaptically. Involved in pre-synaptic differentiation through interaction with SLITRK2. {ECO:0000250|UniProtKB:Q64487}.
 
Catalytic activity: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE- ProRule:PRU10044};
Subunit: Interacts with PPFIA1, PPFIA2 and PPFIA3 (PubMed:9624153). Interacts (via extracellular domain) with SLITRK4 (via LRR 1 and 2 repeats). Interacts with SLITRK2; induces presynaptic differentiation. Interacts (via the second immunoglobilin domain) with IL1RAPL1 (via the first immunoglobilin domain); induces pre- and postsynaptic differentiation of neurons and synapse formation. Interacts (via the third immunoglobilin domain) with IL1RAP (via the first immunoglobilin domain); induces pre- and postsynaptic differentiation of neurons (By similarity). {ECO:0000250|UniProtKB:Q64487, ECO:0000269|PubMed:9624153}.
Subcellular location: Membrane; Single-pass type I membrane protein.
Ptm: A cleavage occurs, separating the extracellular domain from the transmembrane segment. This process called 'ectodomain shedding' is thought to be involved in receptor desensitization, signal transduction and/or membrane localization. {ECO:0000269|PubMed:7896816}.
Miscellaneous: [Isoform 1]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Similarity: Belongs to the protein-tyrosine phosphatase family. Receptor class 2A subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.