Minor histocompatibility antigen H13

Definition:

Catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein, resulting in the release of the fragment from the ER membrane into the cytoplasm. Required to generate lymphocyte cell surface (HLA-E) epitopes derived from MHC class I signal peptides. May be necessary for the removal of the signal peptide that remains attached to the hepatitis C virus core protein after the initial proteolytic processing of the polyprotein. Involved in the intramembrane cleavage of the integral membrane protein PSEN1. Cleaves the integral membrane protein XBP1 isoform 1 in a DERL1/RNF139-dependent manner. May play a role in graft rejection (By similarity).

References:

[1]. Andreas Weihofen, et al. Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science. 2002 Jun 21;296(5576):2215-8. [Content Brief]

[2]. Chia-yi Chen, et al. Signal peptide peptidase functions in ERAD to cleave the unfolded protein response regulator XBP1u. EMBO J. 2014 Nov 3;33(21):2492-506. [Content Brief]

[3]. John McLauchlan, et al. Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets. EMBO J. 2002 Aug 1;21(15):3980-8. [Content Brief]

[4]. M K Lemberg, et al. Intramembrane proteolysis of signal peptides: an essential step in the generation of HLA-E epitopes. J Immunol. 2001 Dec 1;167(11):6441-6. [Content Brief]

[5]. Yuri K Moliaka, et al. Impas 1 possesses endoproteolytic activity against multipass membrane protein substrate cleaving the presenilin 1 holoprotein. FEBS Lett. 2004 Jan 16;557(1-3):185-92. [Content Brief]

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