RN152_DANRE
ID RN152_DANRE Reviewed; 198 AA.
AC Q58EC8;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=E3 ubiquitin-protein ligase rnf152 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8N8N0};
DE AltName: Full=RING finger protein 152 {ECO:0000250|UniProtKB:Q8N8N0};
DE AltName: Full=RING-type E3 ubiquitin transferase rnf152 {ECO:0000305};
GN Name=rnf152 {ECO:0000250|UniProtKB:Q8N8N0};
GN ORFNames=zgc:110537 {ECO:0000312|EMBL:AAH91974.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase mediating 'Lys-63'-linked
CC polyubiquitination of RRAGA in response to amino acid starvation.
CC Thereby, regulates mTORC1 signaling and plays a role in the cellular
CC response to amino acid availability. Also mediates 'Lys-48'-linked
CC polyubiquitination of target proteins and their subsequent targeting to
CC the proteasome for degradation. {ECO:0000250|UniProtKB:Q8N8N0}.
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:Q8N8N0};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q8N8N0}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8N8N0};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q8N8N0}.
CC -!- SIMILARITY: Belongs to the RNF152 family. {ECO:0000305}.
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DR EMBL; BC091974; AAH91974.1; -; mRNA.
DR RefSeq; NP_001014380.1; NM_001014358.1.
DR AlphaFoldDB; Q58EC8; -.
DR SMR; Q58EC8; -.
DR STRING; 7955.ENSDARP00000106876; -.
DR PaxDb; Q58EC8; -.
DR GeneID; 541544; -.
DR KEGG; dre:541544; -.
DR CTD; 220441; -.
DR ZFIN; ZDB-GENE-050327-84; rnf152.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q58EC8; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q58EC8; -.
DR Reactome; R-DRE-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q58EC8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0031301; C:integral component of organelle membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; 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:0006915; P:apoptotic process; IEA:InterPro.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
DR GO; GO:0001654; P:eye development; IMP:ZFIN.
DR GO; GO:0030902; P:hindbrain development; IMP:ZFIN.
DR GO; GO:0030917; P:midbrain-hindbrain boundary development; IMP:ZFIN.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; ISS:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR033609; RNF152.
DR InterPro; IPR045744; RNF152_C.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR25464:SF1; PTHR25464:SF1; 1.
DR Pfam; PF19325; RNF152_C; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Lysosome; Membrane; Metal-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..198
FT /note="E3 ubiquitin-protein ligase rnf152"
FT /id="PRO_0000405837"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 12..55
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 198 AA; 21736 MW; 20BFF60AB6756979 CRC64;
MDSLSQSSRL ECQICFNYFS QRRLPKLLHC QHTCCSVCLS QMRLSQREIR CPWCRCVTQI
PIGLSVSHLP DDPEVLSVIS VSQSSEHTPI FIHLPNNGCY LLPVSLDTDG TPLPGQPTCH
VGPKSIGVFD VSDGQNHVLG HDGLGDGMEE EEVVVVKTTA WTGVCTVLLV AFILIFLLGI
VLHNMSCVSK RFTIISCG
