Meiosis regulator and mRNA stability factor 1 (also known as meiosis arrest female protein 1, MARF1, or Limkain-b1) was first identified as a novel peroxisomal autoantigen that co-localizes with a subset of cytoplasmic microbodies marked by ABCD3 []. Later, it was found that it is an essential regulator of oogenesis required for female meiotic progression and retrotransposon surveillance, therefore, involved in the maintenance of genomic integrity. It acts as a RNAse that efficiently cleaves ssRNAs and down-regulates RNA transcripts, either at transcriptional of post-transcriptional level [, ]. It may function both as an adaptor to recruit specific RNA targets and an effector to catalyse the specific cleavages of target RNAs. MARF1 consists of three major domains, the N-terminal NYN domain, two RNA recognition motifs (RRMs) and a C-terminal repeat of LOTUS (also known as OST-HTH) domains.
This entry represents the RNA recognition motif 1 (RRM1) of MARF1 (also known as Limkain-b1).MARF1 was first identified as a novel peroxisomal autoantigen that co-localizes with a subset of cytoplasmic microbodies marked by ABCD3 []. Later, it was found to be an essential protein for controlling meiosis and retrotransposon surveillance in mouse oocytes. It may function both as an adaptor to recruit specific RNA targets and an effector to catalyse the specific cleavages of target RNAs []. MARF1 contains an N-terminal NYN domain, two central RRMs, and C-terminal OST-HTH/LOTUS domains [, ].
This entry represents the RNA recognition motif 2 (RRM2) of MARF1 (also known as Limkain-b1).MARF1 was first identified as a novel peroxisomal autoantigen that co-localizes with a subset of cytoplasmic microbodies marked by ABCD3 []. Later, it was found to be an essential protein for controlling meiosis and retrotransposon surveillance in mouse oocytes. It may function both as an adaptor to recruit specific RNA targets and an effector to catalyse the specific cleavages of target RNAs []. MARF1 contains an N-terminal NYN domain, two central RRMs, and C-terminal OST-HTH/LOTUS domains [, ].
Ge-1, also known as EDC4 (enhancer of mRNA-decapping protein 4), is a regulator of mRNA decapping to function in the mRNA P-bodies within the cytoplasm. It has been shown to interact with mTORC1 [], coenzyme A synthase []and MARF1 []. It is also involved in the regulation of immune system [].This entry also includes EDC4 homologues from fungi and plants [].
This entry represents the first and second LOTUS domains of MARF1. This domain provides RNA-binding properties to this protein, acting as an adapter to recruit targets for the effector domain NYN at the N-terminal (RNase activity) [].Meiosis regulator and mRNA stability factor 1 (also known as meiosis arrest female protein 1, MARF1, or Limkain-b1) was first identified as a novel peroxisomal autoantigen that co-localizes with a subset of cytoplasmic microbodies marked by ABCD3 []. Later, it was found that it is an essential regulator of oogenesis required for female meiotic progression and retrotransposon surveillance, therefore, involved in the maintenance of genomic integrity. It acts as a RNAse that efficiently cleaves ssRNAs and down-regulates RNA transcripts, either at transcriptional of post-transcriptional level [, ]. It may function both as an adaptor to recruit specific RNA targets and an effector to catalyse the specific cleavages of target RNAs. MARF1 consists of three major domains, the N-terminal NYN domain, two RNA recognition motifs (RRMs) and a C-terminal repeat of LOTUS (also known as OST-HTH) domains.
