RNF34_BOVIN
ID RNF34_BOVIN Reviewed; 375 AA.
AC Q5E9J6;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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}.
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DR EMBL; BT020924; AAX08941.1; -; mRNA.
DR RefSeq; NP_001014858.1; NM_001014858.1.
DR AlphaFoldDB; Q5E9J6; -.
DR SMR; Q5E9J6; -.
DR STRING; 9913.ENSBTAP00000002986; -.
DR PaxDb; Q5E9J6; -.
DR PRIDE; Q5E9J6; -.
DR Ensembl; ENSBTAT00000002986; ENSBTAP00000002986; ENSBTAG00000002315.
DR GeneID; 506764; -.
DR KEGG; bta:506764; -.
DR CTD; 80196; -.
DR VEuPathDB; HostDB:ENSBTAG00000002315; -.
DR VGNC; VGNC:34063; RNF34.
DR eggNOG; KOG4275; Eukaryota.
DR GeneTree; ENSGT00390000012719; -.
DR HOGENOM; CLU_041431_1_0_1; -.
DR InParanoid; Q5E9J6; -.
DR OMA; CRICCDA; -.
DR OrthoDB; 1361306at2759; -.
DR TreeFam; TF325195; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000002315; Expressed in oocyte and 108 other tissues.
DR ExpressionAtlas; Q5E9J6; baseline and differential.
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:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0070417; P:cellular response to cold; IEA:Ensembl.
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 Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
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 SMART; SM00184; RING; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF68906; SSF68906; 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..375
FT /note="E3 ubiquitin-protein ligase RNF34"
FT /id="PRO_0000056071"
FT DOMAIN 115..134
FT /note="SAP 1"
FT DOMAIN 267..281
FT /note="SAP 2"
FT ZN_FING 56..107
FT /note="FYVE-type"
FT ZN_FING 328..363
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 202..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..243
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 227..228
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 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969K3"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR6"
SQ SEQUENCE 375 AA; 41788 MW; F3BEEEA02BA3B944 CRC64;
MKAGATSMWA SCCGLLNEVM GTGAVRGQQS GFAGGTGPFR FTPNSDFSAY PPASAEGPNI
VCKACGLSFS VFRKKHVCCD CKKDFCSVCS VLQENLRRCS TCHLLQETAF QRPQLMRLKV
KDLRQYLILR NIPIDTCREK EDLVDLVLCH HRLGSEDDLD TSSLNSSRSQ TSSFFTHSFF
SNYTAPSATA SSFQGELMGG DRTLGSGALA QEPSEIASAN TEDDEDDDDD DDDDDDDDEE
NLEDRTPGLT KKRVRASLSD LSSLEDVEGM SVRQLKEILA RNFVNYSGCC EKWELVEKVN
RLYKENEENQ KSYGERLQLQ DEEDDSLCRI CMDAVIDCVL LECGHMVTCT KCGKRMSECP
ICRQYVVRAV HVFKS
