Derlin-2 (Degradation in endoplasmic reticulum protein 2) (DERtrin-2) (Der1-like protein 2) (F-LAN-1) (F-LANa)
1_MAYQS 6_ LRLEY 11_ LQIPP 16_ VSRAY 21_ TTACV 26_ LTTAA 31_ VQLEL 36_ ITPFQ 41_ LYFNP 46_ ELIFK 51_ HFQIW 56_ RLITN 61_ FLFFG 66_ PVGFN 71_ FLFNM 76_ IFLYR 81_ YCRML 86_ EEGSF 91_ RGRTA 96_ DFVFM 101_ FLFGG 106_ FLMTL 111_ FGLFV 116_ SLVFL 121_ GQAFT 126_ IMLVY 131_ VWSRR 136_ NPYVR 141_ MNFFG 146_ LLNFQ 151_ APFLP 156_ WVLMG 161_ FSLLL 166_ GNSII 171_ VDLLG 176_ IAVGH 181_ IYFFL 186_ EDVFP 191_ NQPGG 196_ IRILK 201_ TPSIL 206_ KAIFD 211_ TPDED 216_ PNYNP 221_ LPEER 226_ PGGFA 231_WGEGQ
1: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and misfolded glycoproteins (PubMed:16186509, PubMed:16449189). May also be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation (PubMed:26565908)
2: (Microbial infection) In contrast to DERL1, it is not involved in the degradation of MHC class I heavy chains following infection by cytomegaloviruses