RNF13_RAT
ID RNF13_RAT Reviewed; 380 AA.
AC Q66HG0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=E3 ubiquitin-protein ligase RNF13;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 13;
DE Flags: Precursor;
GN Name=Rnf13;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that regulates cell
CC proliferation. Involved in apoptosis regulation. Mediates ER stress-
CC induced activation of JNK signaling pathway and apoptosis by promoting
CC ERN1 activation and splicing of XBP1 mRNA. Also involved in protein
CC trafficking and localization. {ECO:0000250|UniProtKB:O43567}.
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:0000250|UniProtKB:O43567};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:O43567}.
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:0000250|UniProtKB:O54965};
CC Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane
CC {ECO:0000250|UniProtKB:O43567}; Single-pass type I membrane protein
CC {ECO:0000255}. Nucleus inner membrane {ECO:0000250|UniProtKB:O54965};
CC Single-pass type I membrane protein {ECO:0000255}. Note=Under certain
CC conditions, relocalizes to recycling endosomes and to the inner nuclear
CC membrane. {ECO:0000250|UniProtKB:O54965}.
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:0000250|UniProtKB:O43567}.
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DR EMBL; BC081881; AAH81881.1; -; mRNA.
DR RefSeq; NP_001102914.1; NM_001109444.2.
DR AlphaFoldDB; Q66HG0; -.
DR SMR; Q66HG0; -.
DR BioGRID; 596506; 1.
DR STRING; 10116.ENSRNOP00000060441; -.
DR GlyGen; Q66HG0; 1 site.
DR PaxDb; Q66HG0; -.
DR Ensembl; ENSRNOT00000118325; ENSRNOP00000093374; ENSRNOG00000029209.
DR GeneID; 681578; -.
DR KEGG; rno:681578; -.
DR UCSC; RGD:1594062; rat.
DR CTD; 11342; -.
DR RGD; 1594062; Rnf13.
DR eggNOG; KOG4628; Eukaryota.
DR GeneTree; ENSGT00940000154942; -.
DR HOGENOM; CLU_035275_1_1_1; -.
DR InParanoid; Q66HG0; -.
DR OMA; FMIVRCI; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q66HG0; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q66HG0; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000029209; Expressed in lung and 20 other tissues.
DR Genevisible; Q66HG0; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS: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; ISS: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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Lysosome; Membrane;
KW Metal-binding; Nucleus; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..380
FT /note="E3 ubiquitin-protein ligase RNF13"
FT /id="PRO_0000307369"
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..380
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..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 380 AA; 42585 MW; 1BC463BCB34C4309 CRC64;
MLLSIGMLML SATQVYTILT VQLFAFLNLL PVEADILAYN FENASQTFED LPARFGYRLP
AEGLKGFLIN SKPENACEPI VPPPLKDNSS GTFIVLIRRL DCNFDIKVLN AQRAGYKAAI
VHNVDSDDLI SMGSNDIDIL KKIDIPSVFI GESSANSLKD EFTYEKGGHV ILVPELSLPL
EYYLIPFLII VGICLILIVI FMITKFVQDR HRNRRNRLRK DQLKKLPVHK FKKGDEYDVC
AICLEEYEDG DKLRILPCSH AYHCKCVDPW LTKTKKTCPV CKQKVVPSQG DSDSDTDSSQ
EENQVSEHTP LLPPSASART QSFGSLSESH SHHMTESSDY EDDDNEETDS SDADNEITDH
SVVVQLQPNG EPDYNIANTV
