This entry includes fungal vacuolar membrane proteases, such as PFF1 from yeast, which may be involved in vacuolar sorting and osmoregulation []. It is an homologue of human ERMP1 [].According to AlphaFold structure predictions, these proteins consist of a M28 peptidase domain () at the N-terminal, a central transmembrane domain () and a C-terminal domain with an elongated ��-sandwich-like fold, similar to the Mu homology domain (MHD) (). This entry represents the C-terminal MHD-like domain of PFF1 and its fungal homologues.
This entry includes fungal vacuolar membrane proteases, such as PFF1 from yeast, which may be involved in vacuolar sorting and osmoregulation []. It is the homologue of human ERMP1 [].According to AlphaFold structure predictions, these proteins consist of a M28 peptidase domain () at the N-terminal, a central transmembrane domain (TM) and a C-terminal domain with an elongated ��-sandwich-like fold (), similar to the Mu homology domain (MHD) (). This entry represents the TM domain of PFF1 and its fungal homologues.
Endoplasmic reticulum metallopeptidase 1 (ERMP1, also known as Felix-ina, FXNA or Fxna peptidase) is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, Fxna may play a crucial role in processing proteins required for the organisation of somatic cells and oocytes into discrete follicular structures, although which proteins are hydrolysed has not yet been determined []. This entry also includes vacuolar membrane proteases from fungi, such as PFF1 from yeast which are homologues of human ERMP1 []. PFF1 may be involved in vacuolar sorting and osmoregulation [].
