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Immunogen sequence: MKCEHCTRK ECSKKTKTDD QENVSADAPS PAQENGEKCD TSKHKVLVVS VCPQSLPYFA AKFNLSVTDA SRRLCGFLKS LGVHYVFDTT IAADFSILES QKEFVRRYRQ HSEEERTLPM LTSACPGWVR YAERVLGRPI TAHLCTAKSP QQVMGSLVKD YFARQQNLSP EKIFHVIVAP CYDKKLEALQ ESLPPALHGS RGADCVLTSG EIAQIMEQGD LSVRDAAVDT LFGDLKEDKV TRHDGASSDG HLAHIFRHAA KELFNEDVEE VTYRALRNKD FQEVTLEKNG EVVLRFAAAY GFRNIQNMIL KLKKGKFPFH FVEVLACAGG CLNGRGQAQT PDGHADKALL RQMEGIYADI PVRRPESSAH VQELYQEWLE GINSPKAREV LHTTYQSQER GTHSLDIKW (1-408 aa encoded by BC016440 )
Several proteins have been found to be prenylated and methylated at their carboxyl-terminal ends. Prenylation was initially believed to be important only for membrane attachment. However, another role for prenylation appears to be its importance in protein-protein interactions. The only nuclear proteins known to be prenylated in mammalian cells are prelamin A- and B-type lamins. Prelamin A is farnesylated and carboxymethylated on the cysteine residue of a carboxyl-terminal CaaX motif. This post-translationally modified cysteine residue is removed from prelamin A when it is endoproteolytically processed into mature lamin A. The protein encoded by this gene binds to the prenylated prelamin A carboxyl-terminal tail domain. It may be a component of a prelamin A endoprotease complex. The encoded protein is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited sequence similarity with iron-only bacterial hydrogenases. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene, including one with a novel exon that is generated by RNA editing.
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Protein Aliases: IOP2; Iron-only hydrogenase-like protein 2; Nuclear prelamin A recognition factor; prenyl-dependent prelamin A binding protein
Gene Aliases: 4430402O11Rik; IOP2; NARF; RGD1310894
UniProt ID: (Human) Q9UHQ1, (Mouse) Q9CYQ7, (Rat) Q2YDU6
Entrez Gene ID: (Human) 26502, (Mouse) 67608, (Rat) 360681
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