<Entry>
<Accession>O54965</Accession>
        <ProteinName>E3</ProteinName>
        <GeneName>Rnf13</GeneName>
        <OS_id>10090</OS_id>
        <ReferenceProteome>None</ReferenceProteome>
        <SubcellularLocation>
<Location>SL-0178</Location>
<Location>SL-0179</Location>
<Location>SL-0182</Location>
<Comments>Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43567}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:19292867}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:19292867}; Single-pass type I membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000269|PubMed:20230530}; Single-pass type I membrane protein {ECO:0000255}. Note=The mature protein is subjected to extensive proteolysis that leads to the shedding of the ectodomain into the lumen of vesicles and the release of the C-terminal fragment into the cytosol (PubMed:20230530). Not detected in early endosomes (PubMed:20230530). Treatment of the cells with either PMA or ionomycin stabilizes the full-length protein which relocalizes to recycling endosomes and to the inner nuclear membrane (PubMed:20230530). {ECO:0000269|PubMed:20230530}.</Comments>
</SubcellularLocation>
<CrossReferences>
<CrossReference>
<Database>UNIPROT</Database>
<ID>O54965</ID>
</CrossReference>
<CrossReference>
<Database>UNIPROT</Database>
<ID>O54966</ID>
</CrossReference>
<CrossReference>
<Database>UNIPROT</Database>
<ID>Q6PEA8</ID>
</CrossReference>
<CrossReference>
<Database>Pfam</Database>
<ID>PF02225</ID>
</CrossReference>
<CrossReference>
<Database>Pfam</Database>
<ID>PF13639</ID>
</CrossReference>
<CrossReference>
<Database>PROSITE</Database>
<ID>PS50089</ID>
</CrossReference>
</CrossReferences>
<Function>E3 ubiquitin-protein ligase that regulates cell proliferation (PubMed:19292867). Involved in apoptosis regulation (By similarity). Mediates ER stress-induced activation of JNK signaling pathway and apoptosis by promoting ERN1 activation and splicing of XBP1 mRNA (By similarity). Also involved in protein trafficking and localization (By similarity). {ECO:0000250|UniProtKB:O43567, ECO:0000269|PubMed:19292867}.</Function>
<OntologyTerms>
<Ontology>GO:0005829</Ontology>
<Ontology>GO:0005783</Ontology>
<Ontology>GO:0005789</Ontology>
<Ontology>GO:0005768</Ontology>
<Ontology>GO:0016021</Ontology>
<Ontology>GO:0043231</Ontology>
<Ontology>GO:0031902</Ontology>
<Ontology>GO:0005765</Ontology>
<Ontology>GO:0005637</Ontology>
<Ontology>GO:0005654</Ontology>
<Ontology>GO:0008432</Ontology>
<Ontology>GO:0046872</Ontology>
<Ontology>GO:0061630</Ontology>
<Ontology>GO:0004842</Ontology>
<Ontology>GO:0051640</Ontology>
<Ontology>GO:0070304</Ontology>
<Ontology>GO:0051865</Ontology>
<Ontology>GO:0006511</Ontology>
</OntologyTerms>
<Topology>
        <Type>Transmembrane</Type>
        <Source>UniProt</Source>
        <Annotation>Sequence Analysis {ECO:0000255}</Annotation>
        </Topology>
<Sequence>MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFEDLPARFGYRLPAEGLKGFLINSKPENACEPIVPPPLKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIDTLKKIDIPSVFIGESSANSLKDEFTYEKGGHIILVPELSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRNRRNRLRKDQLKKLPVHKFKKGDEYDVCAICLEEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENQVSEHTPLLPPSASARTQSFGSLSESHSHHNMTESSDYEDDDNEETDSSDADNEITDHSVVVQLQPNGEQDYNIANTV</Sequence>
        <SequenceLength>381</SequenceLength>
        </Entry>