RNF13_MOUSE
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 03-AUG-2022, entry version 145.
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}.
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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 GlyGen; O54965; 1 site.
DR iPTMnet; O54965; -.
DR PhosphoSitePlus; O54965; -.
DR MaxQB; O54965; -.
DR PaxDb; O54965; -.
DR PeptideAtlas; O54965; -.
DR PRIDE; O54965; -.
DR ProteomicsDB; 300553; -. [O54965-1]
DR ProteomicsDB; 300554; -. [O54965-2]
DR Antibodypedia; 2251; 137 antibodies from 28 providers.
DR DNASU; 24017; -.
DR Ensembl; ENSMUST00000041826; ENSMUSP00000049331; ENSMUSG00000036503. [O54965-1]
DR Ensembl; ENSMUST00000199041; ENSMUSP00000142335; ENSMUSG00000036503. [O54965-2]
DR GeneID; 24017; -.
DR KEGG; mmu:24017; -.
DR UCSC; uc008phj.3; mouse. [O54965-1]
DR CTD; 11342; -.
DR MGI; MGI:1346341; Rnf13.
DR VEuPathDB; HostDB:ENSMUSG00000036503; -.
DR eggNOG; KOG4628; Eukaryota.
DR GeneTree; ENSGT00940000154942; -.
DR InParanoid; O54965; -.
DR OMA; FMIVRCI; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; O54965; -.
DR TreeFam; TF317486; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 24017; 2 hits in 58 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 255 other tissues.
DR ExpressionAtlas; O54965; baseline and differential.
DR Genevisible; O54965; MM.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:Ensembl.
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 Gene3D; 3.30.40.10; -; 1.
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 Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
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
