ID RNF13_MOUSE Reviewed; 381 AA. AC O54965; O54966; Q6PEA8; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 27-MAR-2024, entry version 154. DE RecName: Full=E3 ubiquitin-protein ligase RNF13; DE EC=2.3.2.27 {ECO:0000269|PubMed:19292867}; DE AltName: Full=RING finger protein 13; DE Flags: Precursor; GN Name=Rnf13; Synonyms=Rzf {ECO:0000303|Ref.1}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RA Lomax M.I., Warner S.J., Bersirli C.G., Gong T.-W.L.; RT "The gene for a RING zinc finger protein is expressed in the inner chick RT ear after noise exposure."; RL Prim. Sens. Neuron 2:305-316(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Inner ear; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TOPOGRAPHY, RP TISSUE SPECIFICITY, AUTOUBIQUITINATION, GLYCOSYLATION, AND MUTAGENESIS OF RP CYS-266. RX PubMed=19292867; DOI=10.1111/j.1742-4658.2009.06913.x; RA Bocock J.P., Carmicle S., Chhotani S., Ruffolo M.R., Chu H., Erickson A.H.; RT "The PA-TM-RING protein RING finger protein 13 is an endosomal integral RT membrane E3 ubiquitin ligase whose RING finger domain is released to the RT cytoplasm by proteolysis."; RL FEBS J. 276:1860-1877(2009). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=20230530; DOI=10.1111/j.1600-0854.2010.01060.x; RA Bocock J.P., Carmicle S., Madamba E., Erickson A.H.; RT "Nuclear targeting of an endosomal E3 ubiquitin ligase."; RL Traffic 11:756-766(2010). CC -!- FUNCTION: E3 ubiquitin-protein ligase that regulates cell proliferation CC (PubMed:19292867). Involved in apoptosis regulation (By similarity). CC Mediates ER stress-induced activation of JNK signaling pathway and CC apoptosis by promoting ERN1 activation and splicing of XBP1 mRNA (By CC similarity). Also involved in protein trafficking and localization (By CC similarity). {ECO:0000250|UniProtKB:O43567, CC ECO:0000269|PubMed:19292867}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:19292867}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:19292867}. CC -!- SUBUNIT: Interacts with ERN1. {ECO:0000250|UniProtKB:O43567}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:O43567}; Single-pass type I membrane protein CC {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:19292867}; CC Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane CC {ECO:0000269|PubMed:19292867}; Single-pass type I membrane protein CC {ECO:0000255}. Nucleus inner membrane {ECO:0000269|PubMed:20230530}; CC Single-pass type I membrane protein {ECO:0000255}. Note=The mature CC protein is subjected to extensive proteolysis that leads to the CC shedding of the ectodomain into the lumen of vesicles and the release CC of the C-terminal fragment into the cytosol (PubMed:20230530). Not CC detected in early endosomes (PubMed:20230530). Treatment of the cells CC with either PMA or ionomycin stabilizes the full-length protein which CC relocalizes to recycling endosomes and to the inner nuclear membrane CC (PubMed:20230530). {ECO:0000269|PubMed:20230530}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O54965-1; Sequence=Displayed; CC Name=2; CC IsoId=O54965-2; Sequence=VSP_005749, VSP_005750; CC -!- TISSUE SPECIFICITY: Expressed in the brain, heart, kidney, liver and CC spleen. Higher expression in adult tissues compared to the embryonic CC counterparts. {ECO:0000269|PubMed:19292867}. CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase CC activity and for promoting ER stress-induced JNK activation and CC apoptosis. {ECO:0000250|UniProtKB:O43567}. CC -!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:19292867}. CC -!- PTM: N-glycosylated and also modified with chondroitin sulfate. CC {ECO:0000269|PubMed:19292867}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF037205; AAC03770.1; -; mRNA. DR EMBL; AF037206; AAC03771.1; -; mRNA. DR EMBL; AK158046; BAE34334.1; -; mRNA. DR EMBL; CH466530; EDL35322.1; -; Genomic_DNA. DR EMBL; CH466530; EDL35326.1; -; Genomic_DNA. DR EMBL; BC058182; AAH58182.1; -; mRNA. DR CCDS; CCDS50913.1; -. [O54965-1] DR CCDS; CCDS79910.1; -. [O54965-2] DR RefSeq; NP_001106884.1; NM_001113413.2. [O54965-1] DR RefSeq; NP_036013.1; NM_011883.4. [O54965-2] DR RefSeq; XP_006501520.1; XM_006501457.3. DR AlphaFoldDB; O54965; -. DR SMR; O54965; -. DR STRING; 10090.ENSMUSP00000049331; -. DR GlyCosmos; O54965; 1 site, No reported glycans. DR GlyGen; O54965; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; O54965; -. DR PhosphoSitePlus; O54965; -. DR MaxQB; O54965; -. DR PaxDb; 10090-ENSMUSP00000049331; -. DR PeptideAtlas; O54965; -. DR ProteomicsDB; 300553; -. [O54965-1] DR ProteomicsDB; 300554; -. [O54965-2] DR Pumba; O54965; -. DR Antibodypedia; 2251; 164 antibodies from 28 providers. DR DNASU; 24017; -. DR Ensembl; ENSMUST00000041826.14; ENSMUSP00000049331.10; ENSMUSG00000036503.14. [O54965-1] DR Ensembl; ENSMUST00000199041.2; ENSMUSP00000142335.2; ENSMUSG00000036503.14. [O54965-2] DR GeneID; 24017; -. DR KEGG; mmu:24017; -. DR UCSC; uc008phj.3; mouse. [O54965-1] DR AGR; MGI:1346341; -. DR CTD; 11342; -. DR MGI; MGI:1346341; Rnf13. DR VEuPathDB; HostDB:ENSMUSG00000036503; -. DR eggNOG; KOG4628; Eukaryota. DR GeneTree; ENSGT00940000154942; -. DR InParanoid; O54965; -. DR OMA; GHIVLIP; -. DR OrthoDB; 5474929at2759; -. DR PhylomeDB; O54965; -. DR TreeFam; TF317486; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 24017; 2 hits in 61 CRISPR screens. DR ChiTaRS; Rnf13; mouse. DR PRO; PR:O54965; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; O54965; Protein. DR Bgee; ENSMUSG00000036503; Expressed in pigmented layer of retina and 258 other cell types or tissues. DR ExpressionAtlas; O54965; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005768; C:endosome; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0008432; F:JUN kinase binding; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0051640; P:organelle localization; ISO:MGI. DR GO; GO:0070304; P:positive regulation of stress-activated protein kinase signaling cascade; ISS:UniProtKB. DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR CDD; cd02123; PA_C_RZF_like; 1. DR CDD; cd16796; RING-H2_RNF13; 1. DR Gene3D; 3.50.30.30; -; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR046450; PA_dom_sf. DR InterPro; IPR003137; PA_domain. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR044744; ZNRF4/RNF13/RNF167_PA. DR PANTHER; PTHR46539; E3 UBIQUITIN-PROTEIN LIGASE ATL42; 1. DR PANTHER; PTHR46539:SF25; RING FINGER PROTEIN 150; 1. DR Pfam; PF02225; PA; 1. DR Pfam; PF13639; zf-RING_2; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF52025; PA domain; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; O54965; MM. PE 1: Evidence at protein level; KW Alternative splicing; Endoplasmic reticulum; Endosome; Glycoprotein; KW Lysosome; Membrane; Metal-binding; Nucleus; Reference proteome; Signal; KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT SIGNAL 1..34 FT /evidence="ECO:0000255" FT CHAIN 35..381 FT /note="E3 ubiquitin-protein ligase RNF13" FT /id="PRO_0000056055" FT TOPO_DOM 35..182 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 183..203 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 204..381 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 64..160 FT /note="PA" FT ZN_FING 240..282 FT /note="RING-type; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT REGION 285..381 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 303..332 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 340..354 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 358..381 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 88 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 261..268 FT /note="AYHCKCVD -> GMSTHTVL (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_005749" FT VAR_SEQ 269..381 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_005750" FT MUTAGEN 266 FT /note="C->A: Loss of E3 ligase activity." FT /evidence="ECO:0000269|PubMed:19292867" FT CONFLICT 362 FT /note="S -> I (in Ref. 1; AAC03770)" FT /evidence="ECO:0000305" SQ SEQUENCE 381 AA; 42732 MW; 1E0EF4801A2C6FE8 CRC64; MLLSIGMLML SATQVYTILT VQLFAFLNLL PVEADILAYN FENASQTFED LPARFGYRLP AEGLKGFLIN SKPENACEPI VPPPLKDNSS GTFIVLIRRL DCNFDIKVLN AQRAGYKAAI VHNVDSDDLI SMGSNDIDTL KKIDIPSVFI GESSANSLKD EFTYEKGGHI ILVPELSLPL EYYLIPFLII VGICLILIVI FMITKFVQDR HRNRRNRLRK DQLKKLPVHK FKKGDEYDVC AICLEEYEDG DKLRILPCSH AYHCKCVDPW LTKTKKTCPV CKQKVVPSQG DSDSDTDSSQ EENQVSEHTP LLPPSASART QSFGSLSESH SHHNMTESSD YEDDDNEETD SSDADNEITD HSVVVQLQPN GEQDYNIANT V //