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Database: UniProt
Entry: RN152_DANRE
LinkDB: RN152_DANRE
Original site: 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   24-JAN-2024, entry version 109.
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 that acts as a negative regulator
CC       of mTORC1 signaling by mediating ubiquitination of RagA/RRAGA and RHEB.
CC       Catalyzes 'Lys-63'-linked polyubiquitination of RagA/RRAGA in response
CC       to amino acid starvation, thereby regulating mTORC1 signaling. Also
CC       mediates monoubiquitination of RHEB, promoting its association with the
CC       TSC-TBC complex and subsequent inhibition. Also mediates 'Lys-48'-
CC       linked polyubiquitination of target proteins and their subsequent
CC       targeting to the proteasome for degradation.
CC       {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; 7955-ENSDARP00000106876; -.
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; 5356073at2759; -.
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   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0031090; C:organelle membrane; 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   GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR   CDD; cd16548; RING-HC_RNF152; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR033609; RING_RNF152.
DR   InterPro; IPR045744; RNF152_C.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR25464:SF1; E3 UBIQUITIN-PROTEIN LIGASE RNF152; 1.
DR   PANTHER; PTHR25464; TRIPARTITE MOTIF-CONTAINING PROTEIN 2-LIKE PROTEIN; 1.
DR   Pfam; PF19325; RNF152_C; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SUPFAM; SSF57850; RING/U-box; 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
//
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