ID RNF34_PONAB Reviewed; 372 AA.
AC Q5NVC7; Q5NVI7; Q5R509;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 24-JAN-2024, entry version 112.
DE RecName: Full=E3 ubiquitin-protein ligase RNF34 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q969K3};
DE AltName: Full=RING finger protein 34;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF34 {ECO:0000305};
GN Name=RNF34;
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: E3 ubiquitin-protein ligase that regulates several biological
CC processes through the ubiquitin-mediated proteasomal degradation of
CC various target proteins. Ubiquitinates the caspases CASP8 and CASP10,
CC promoting their proteasomal degradation, to negatively regulate cell
CC death downstream of death domain receptors in the extrinsic pathway of
CC apoptosis. May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and
CC its subsequent proteasomal degradation thereby indirectly regulating
CC the tumor necrosis factor-mediated signaling pathway. Negatively
CC regulates p53/TP53 through its direct ubiquitination and targeting to
CC proteasomal degradation. Indirectly, may also negatively regulate
CC p53/TP53 through ubiquitination and degradation of SFN. Mediates
CC PPARGC1A proteasomal degradation probably through ubiquitination
CC thereby indirectly regulating the metabolism of brown fat cells.
CC Possibly involved in innate immunity, through 'Lys-48'-linked
CC polyubiquitination of NOD1 and its subsequent proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q969K3}.
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:Q969K3};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q969K3}.
CC -!- SUBUNIT: Interacts with CASP8 and CASP10. Interacts with p53/TP53;
CC involved in p53/TP53 ubiquitination. Interacts (via RING-type zinc
CC finger) with MDM2; the interaction stabilizes MDM2. Interacts (via
CC RING-type zinc finger) with PPARGC1A. Interacts with NOD1.
CC {ECO:0000250|UniProtKB:Q969K3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q969K3};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q969K3}.
CC Endomembrane system {ECO:0000250|UniProtKB:Q6AYH3}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q6AYH3}. Nucleus
CC {ECO:0000250|UniProtKB:Q969K3}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q969K3}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q969K3}.
CC -!- DOMAIN: The RING-type zinc finger is required for the ubiquitination of
CC target proteins. {ECO:0000250|UniProtKB:Q969K3}.
CC -!- DOMAIN: The FYVE-type zinc finger domain is required for localization
CC and may confer affinity for cellular compartments enriched in
CC phosphatidylinositol 5-phosphate and phosphatidylinositol 3-phosphate
CC phospholipids. {ECO:0000250|UniProtKB:Q969K3}.
CC -!- PTM: Autoubiquitinated (in vitro). {ECO:0000250|UniProtKB:Q6AYH3}.
CC -!- PTM: Proteolytically cleaved by caspases upon induction of apoptosis by
CC TNF. {ECO:0000250|UniProtKB:Q969K3}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR861076; CAH93157.1; -; mRNA.
DR EMBL; CR926111; CAI29736.1; -; mRNA.
DR EMBL; CR926044; CAI29676.1; -; mRNA.
DR RefSeq; NP_001126862.1; NM_001133390.1.
DR RefSeq; NP_001128919.1; NM_001135447.1.
DR AlphaFoldDB; Q5NVC7; -.
DR SMR; Q5NVC7; -.
DR STRING; 9601.ENSPPYP00000005752; -.
DR GeneID; 100173871; -.
DR GeneID; 100189867; -.
DR KEGG; pon:100173871; -.
DR CTD; 80196; -.
DR eggNOG; KOG4275; Eukaryota.
DR InParanoid; Q5NVC7; -.
DR OrthoDB; 383715at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:2001271; P:negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; ISS:UniProtKB.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISS:UniProtKB.
DR GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:2000374; P:regulation of oxygen metabolic process; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd15769; FYVE_CARP1; 1.
DR CDD; cd16706; RING-HC_CARP1; 1.
DR Gene3D; 1.10.720.140; -; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR049320; CARP1_2_FYVE.
DR InterPro; IPR049323; CARP1_FYVE.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14879; CASPASE REGULATOR, RING FINGER DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR14879:SF3; E3 UBIQUITIN-PROTEIN LIGASE RNF34; 1.
DR Pfam; PF21272; FYVE_CARP1-2; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cell membrane; Cytoplasm; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..372
FT /note="E3 ubiquitin-protein ligase RNF34"
FT /id="PRO_0000056074"
FT DOMAIN 115..134
FT /note="SAP 1"
FT DOMAIN 264..278
FT /note="SAP 2"
FT ZN_FING 56..107
FT /note="FYVE-type"
FT ZN_FING 325..360
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 194..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..240
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 231..232
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:Q969K3"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969K3"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969K3"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR6"
FT CONFLICT 1
FT /note="M -> MR (in Ref. 1; CAH93157)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="V -> A (in Ref. 1; CAI29676)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="K -> R (in Ref. 1; CAI29736)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 41587 MW; 8354C4DA530741C1 CRC64;
MKAGATSMWA SCCGLLNEVM GTGAVRGQQS GFAGATGPFR FTPNPEFSTY PPAATEGPNI
VCKACGLSFS VFRKKHVCCD CKKDFCSVCS VLQENLRRCS TCHLLQETAF QRPQLMRLKV
KDLRQYLILR NIPTDTCREK EDLVDLVLCH HGLGSEDDMD TSSLNSSRSQ TSSFFTRSFF
SNYTAPSATM SSFQGELMDG DQTSRSGVPA QVQSEITSAN TEDDDDDDDE DDDDEEENAE
DQNPGLSKER VRASLSDLSS LDDVEGMSVR QLKEILARNF VNYSGCCEKW ELVEKVNRLY
KENEENQKSY GERLQLQDEE DDSLCRICMD AVIDCVLLEC GHMVTCTKCG KRMSECPICR
QYVVRAVHVF KS
//
