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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
 
 
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