RNF13_CHICK
ID RNF13_CHICK Reviewed; 381 AA.
AC Q90972; Q533M4;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=E3 ubiquitin-protein ligase RNF13;
DE EC=2.3.2.27;
DE AltName: Full=C-RZF {ECO:0000303|PubMed:8610176};
DE AltName: Full=RING finger protein 13;
DE Flags: Precursor;
GN Name=RNF13 {ECO:0000303|PubMed:20015074};
GN Synonyms=RZF {ECO:0000303|PubMed:8610176};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=8610176; DOI=10.1073/pnas.93.7.3105;
RA Tranque P., Crossin K.L., Cirelli C., Edelman G.M., Mauro V.P.;
RT "Identification and characterization of a RING zinc finger gene (C-RZF)
RT expressed in chicken embryo cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:3105-3109(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wang K., Zhang Q., Yang W., Zhu D., Yu F., Zhang Y., Chen Y.;
RT "Myostatin inhibits myoblasts proliferation by up-regulating cRNF E3
RT ubiquitin ligase.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY.
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, INDUCTION BY MSTN, AND MUTAGENESIS OF CYS-258; HIS-260 AND TRP-270.
RX PubMed=20015074; DOI=10.1111/j.1742-4658.2009.07498.x;
RA Zhang Q., Wang K., Zhang Y., Meng J., Yu F., Chen Y., Zhu D.;
RT "The myostatin-induced E3 ubiquitin ligase RNF13 negatively regulates the
RT proliferation of chicken myoblasts.";
RL FEBS J. 277:466-476(2010).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that regulates cell proliferation
CC (PubMed:20015074). Involved in apoptosis regulation. Mediates ER
CC stress-induced activation of JNK signaling pathway and apoptosis by
CC promoting ERN1 activation and splicing of XBP1 mRNA (By similarity).
CC {ECO:0000250|UniProtKB:O43567, ECO:0000269|PubMed:20015074}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {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:0000305|PubMed:8610176};
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 -!- TISSUE SPECIFICITY: Widely expressed (at protein level). Lowest levels
CC in the liver, moderate levels in the heart, intestine and spleen, and
CC high levels in skeletal muscle, kidney, proventriculus and brain. Also
CC expressed in inner ear after noise exposure.
CC {ECO:0000269|PubMed:20015074, ECO:0000269|PubMed:8610176,
CC ECO:0000269|Ref.3}.
CC -!- DEVELOPMENTAL STAGE: Expressed in skeletal muscle tissue during
CC embryonic development and for 2 weeks after hatching; becomes
CC undetectable 3 weeks after hatching (at protein level).
CC {ECO:0000269|PubMed:20015074}.
CC -!- INDUCTION: By myostatin. {ECO:0000269|PubMed:20015074}.
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}.
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DR EMBL; X95455; CAA64725.1; -; mRNA.
DR EMBL; AY787020; AAX14391.1; -; Genomic_DNA.
DR RefSeq; NP_990686.1; NM_205355.1.
DR AlphaFoldDB; Q90972; -.
DR SMR; Q90972; -.
DR BioGRID; 676561; 1.
DR STRING; 9031.ENSGALP00000038118; -.
DR PaxDb; Q90972; -.
DR Ensembl; ENSGALT00000038908; ENSGALP00000038118; ENSGALG00000010411.
DR Ensembl; ENSGALT00000085254; ENSGALP00000059828; ENSGALG00000010411.
DR GeneID; 396303; -.
DR KEGG; gga:396303; -.
DR CTD; 11342; -.
DR VEuPathDB; HostDB:geneid_396303; -.
DR eggNOG; KOG4628; Eukaryota.
DR GeneTree; ENSGT00940000154942; -.
DR HOGENOM; CLU_035275_1_1_1; -.
DR InParanoid; Q90972; -.
DR OMA; FMIVRCI; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q90972; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q90972; -.
DR Proteomes; UP000000539; Chromosome 9.
DR Bgee; ENSGALG00000010411; Expressed in lung and 13 other tissues.
DR ExpressionAtlas; Q90972; baseline and differential.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Lysosome; Membrane;
KW Metal-binding; Nucleus; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..381
FT /note="E3 ubiquitin-protein ligase RNF13"
FT /id="PRO_0000056056"
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..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..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 MUTAGEN 258
FT /note="C->A: Decrease in E3 ligase activity. Complete loss
FT of myoblast growth suppression activity; when associated
FT with A-260."
FT /evidence="ECO:0000269|PubMed:20015074"
FT MUTAGEN 260
FT /note="H->A: Decrease in E3 ligase activity. Loss of
FT myoblast growth suppression activity; when associated with
FT A-258."
FT /evidence="ECO:0000269|PubMed:20015074"
FT MUTAGEN 270
FT /note="W->A: Decrease in E3 ligase activity. Loss of
FT myoblast growth suppression activity."
FT /evidence="ECO:0000269|PubMed:20015074"
SQ SEQUENCE 381 AA; 42820 MW; 6816145C40343C6A CRC64;
MLLSIGMLML SATQIYTIVT VQLFAFLNLL PVEADILAYN FENGTQTFDD LPARFGYRLP
AEGLKGFLIN SKPENACEPI APPPLRDNSS TAFIVLIRRL ECNFDIKVLN AQRAGYKAAI
VHNVDSDDLI SMGSNDIEIL KKIDIPSVFI GEASANSLKE EFTYEKGGHV VLIPEFSLPL
EYYLIPFLII VGICLILIVI FMITKFVQDR HRARRNRLRK DQLKKLPVHK FKKGDEYDVC
AICLDEYEDG DKLRILPCSH AYHCKCVDPW LTKTKKTCPV CKQKVVPSQG DSDSETDSSQ
EENEVSENTP LLRPLASVST QSFGALSESH SHQNMTESSE YEEDDNDNID SSDAESGVNE
ESVVVQLQPN DERDYRVTNT V
