ID RNF41_PONAB Reviewed; 317 AA.
AC Q5R7T5;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=E3 ubiquitin-protein ligase NRDP1;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 41;
DE AltName: Full=RING-type E3 ubiquitin transferase NRDP1 {ECO:0000305};
GN Name=RNF41; Synonyms=NRDP1;
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=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as E3 ubiquitin-protein ligase and regulates the
CC degradation of target proteins. Polyubiquitinates MYD88. Negatively
CC regulates MYD88-dependent production of pro-inflammatory cytokines. Can
CC promote TRIF-dependent production of type I interferon and inhibits
CC infection with vesicular stomatitis virus. Promotes also activation of
CC TBK1 and IRF3. Involved in the ubiquitination of erythropoietin (EPO)
CC and interleukin-3 (IL-3) receptors. Thus, through maintaining basal
CC levels of cytokine receptors, RNF41 is involved in the control of
CC hematopoietic progenitor cell differentiation into myeloerythroid
CC lineages. Contributes to the maintenance of steady-state ERBB3 levels
CC by mediating its growth factor-independent degradation. Involved in the
CC degradation of the inhibitor of apoptosis BIRC6 and thus is an
CC important regulator of cell death by promoting apoptosis. Acts also as
CC a PRKN modifier that accelerates its degradation, resulting in a
CC reduction of PRKN activity, influencing the balance of intracellular
CC redox state. The RNF41-PRKN pathway regulates autophagosome-lysosome
CC fusion during late mitophagy. Mitophagy is a selective form of
CC autophagy necessary for mitochondrial quality control.
CC {ECO:0000250|UniProtKB:Q9H4P4}.
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 -!- SUBUNIT: Interacts with USP8, ERBB3, PRKN, BIRC6, CSF2RB, EPOR, IL3RA,
CC MYD88 and TBK1. Interacts with CLEC16A. {ECO:0000250|UniProtKB:Q8BH75,
CC ECO:0000250|UniProtKB:Q9H4P4}.
CC -!- PTM: Autoubiquitinated. Autoubiquitination leads to proteasomal
CC degradation. Deubiquitinated by USP8 to get stabilized which induces
CC apoptosis. {ECO:0000250}.
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DR EMBL; CR860024; CAH92175.1; -; mRNA.
DR RefSeq; NP_001126274.1; NM_001132802.1.
DR RefSeq; XP_009246169.1; XM_009247894.1.
DR RefSeq; XP_009246170.1; XM_009247895.1.
DR AlphaFoldDB; Q5R7T5; -.
DR SMR; Q5R7T5; -.
DR STRING; 9601.ENSPPYP00000005297; -.
DR Ensembl; ENSPPYT00000005505.2; ENSPPYP00000005297.1; ENSPPYG00000004649.2.
DR GeneID; 100173246; -.
DR KEGG; pon:100173246; -.
DR CTD; 10193; -.
DR eggNOG; KOG0297; Eukaryota.
DR GeneTree; ENSGT00530000063647; -.
DR HOGENOM; CLU_076732_0_0_1; -.
DR InParanoid; Q5R7T5; -.
DR OMA; ENYVCKR; -.
DR OrthoDB; 5490637at2759; -.
DR TreeFam; TF351947; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Chromosome 12.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005128; F:erythropoietin receptor binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005135; F:interleukin-3 receptor binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:1901525; P:negative regulation of mitophagy; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0045619; P:regulation of lymphocyte differentiation; IEA:Ensembl.
DR GO; GO:0043408; P:regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0045637; P:regulation of myeloid cell differentiation; IEA:Ensembl.
DR GO; GO:0051896; P:regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR CDD; cd16634; mRING-HC-C3HC3D_Nrdp1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR015036; NRDP1.
DR InterPro; IPR037255; NRDP1_C.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR15315:SF74; E3 UBIQUITIN-PROTEIN LIGASE NRDP1; 1.
DR PANTHER; PTHR15315; RING FINGER PROTEIN 41, 151; 1.
DR Pfam; PF08941; USP8_interact; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF160088; NRDP1 C-terminal domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Autophagy; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..317
FT /note="E3 ubiquitin-protein ligase NRDP1"
FT /id="PRO_0000290007"
FT ZN_FING 18..57
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 78..138
FT /note="SIAH-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
SQ SEQUENCE 317 AA; 35905 MW; 46AE87AF8BE1A369 CRC64;
MGYDVTRFQG DVDEDLICPI CSGVLEEPVQ APHCEHAFCN ACITQWFSQQ QTCPVDRSVV
TVAHLRPVPR IMRNMLSKLQ IACDNAVFGC SAVVRLDNLM SHLSDCEHNP KRPVTCEQGC
GLEMPKDELP NHNCIKHLRS VVQQQQTRIA ELEKTSAEHK HQLAEQKRDI QLLKAYMRAI
RSVNPNLQNL EETIEYNEIL EWVNSLQPAR VTRWGGMIST PDAVLQAVIK RSLVESGCPA
SIVNELIENA HERSWPQGLA TLETRQMNRR YYENYVAKRI PGKQAVVVMA CENQHMGDDM
VQEPGLVMIF AHGVEEI
//
