|  Help  |  About  |  Contact Us

Search our database by keyword

- or -

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 1 to 1 out of 1 for Ppfia3

Category restricted to ProteinDomain (x)

0.016s

Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Family
Description: Liprin-alpha-3 is a member of the LAR (leukocyte common antigen-related) protein tyrosine phosphatase-interacting protein (liprin) family []. Liprin-alpha family proteins in mammals are expressed at high levels in the brain and are engaged in high-affinity interactions with many presynaptic active zone proteins []. Liprin-alpha-3 is one of the predominant Liprin isoforms in the hippocampus [, ]. It interacts with RIM1-alpha and other active zone proteins to form a protein scaffold in the presynaptic nerve terminal [].Liprin was originally identified as binding partners of the receptor protein tyrosine phosphatase LAR (leukocyte common antigen-related), which functions in axon guidance and mammary gland development []. In vertebrates, there are two families of liprins, liprin-alpha and liprin-beta, which have four (alpha1-4) and two (beta1-2) members. Liprins contain an N-terminal coiled-coil domain and a C-terminal liprin homology (LH) region comprised of three sterile alpha motif (SAM) domains. The N-terminal coiled coils of liprin-alpha act as binding regions for several synaptic protein, while the SAM repeats can bind to both phosphatases and protein kinases []. The autophosphorylation of liprin regulates its association with LAR []. Interestingly, all Liprin-alpha genes are subject to alternative splicing, which is regulated in a developmental manner []. The structure of the human CASK/liprin-alpha/liprin-beta ternary complex has been revealed [].