RNF13_PONAB
ID RNF13_PONAB Reviewed; 381 AA.
AC Q5RCV8;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR858160; CAH90399.1; -; mRNA.
DR RefSeq; NP_001125196.1; NM_001131724.1.
DR AlphaFoldDB; Q5RCV8; -.
DR SMR; Q5RCV8; -.
DR STRING; 9601.ENSPPYP00000015882; -.
DR Ensembl; ENSPPYT00000016511; ENSPPYP00000015882; ENSPPYG00000014202.
DR GeneID; 100172087; -.
DR KEGG; pon:100172087; -.
DR CTD; 11342; -.
DR eggNOG; KOG4628; Eukaryota.
DR GeneTree; ENSGT00940000154942; -.
DR InParanoid; Q5RCV8; -.
DR OrthoDB; 1487241at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Chromosome 3.
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; IEA:Ensembl.
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 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..381
FT /note="E3 ubiquitin-protein ligase RNF13"
FT /id="PRO_0000307368"
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 65..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 320..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..355
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 381 AA; 42814 MW; 4600727D0F197653 CRC64;
MLLSIGMLML SATQVYTILT VQLFAFLNLL PVEADILAYN FENASQTFDD LPARFGYRLP
AEGLKGFLIN SKPENACEPI VPPPVKDNSS GTFIVLIRRL DCNFDIKVLN AQRAGYKAAI
VHNVDSDDLI SMGSNDIEVL KKIDIPSVFI GESSANSLKD EFTYEKGGHL ILVPEFSLPL
EYYLIPFLII VGICLILIVI FMITKFVQDR HRARRNRLRK DQLKKLPVHK FKKGDEYDVC
AICLDEYEDG DKLRILPCSH AYHCKCVDPW LTKTKKTCPV CKQKVVPSQG DSDSDTDSSQ
EENEVTEHTP LLRPLASVSA QSFGALSESR SHQNMTESSD YEEDDNEDTD SSDAENEINE
HDVVVQLQPN GERDYNIANT V
