RN152_RAT
ID RN152_RAT Reviewed; 203 AA.
AC D4A723;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 66.
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:0000312|RGD:1305251};
DE AltName: Full=RING-type E3 ubiquitin transferase RNF152 {ECO:0000305};
GN Name=Rnf152 {ECO:0000312|RGD:1305251};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-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. Induces apoptosis when overexpressed.
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 -!- SUBUNIT: Interacts with RRAGA (inactive GDP-bound form); stimulated by
CC amino acid starvation. Interacts with SEC16A.
CC {ECO:0000250|UniProtKB:Q8BG47, ECO:0000250|UniProtKB:Q8N8N0}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8N8N0};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q8N8N0}.
CC -!- PTM: Ubiquitinated. Autoubiquitinated in vitro, leading to its
CC degradation by the proteasome. {ECO:0000250|UniProtKB:Q8N8N0}.
CC -!- SIMILARITY: Belongs to the RNF152 family. {ECO:0000305}.
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; CH474000; EDL91732.1; -; Genomic_DNA.
DR RefSeq; NP_001099775.1; NM_001106305.1.
DR RefSeq; XP_017454255.1; XM_017598766.1.
DR RefSeq; XP_017454256.1; XM_017598767.1.
DR RefSeq; XP_017454257.1; XM_017598768.1.
DR RefSeq; XP_017454258.1; XM_017598769.1.
DR RefSeq; XP_017454259.1; XM_017598770.1.
DR AlphaFoldDB; D4A723; -.
DR SMR; D4A723; -.
DR STRING; 10116.ENSRNOP00000019921; -.
DR PaxDb; D4A723; -.
DR Ensembl; ENSRNOT00000019921; ENSRNOP00000019921; ENSRNOG00000014859.
DR Ensembl; ENSRNOT00000102604; ENSRNOP00000093936; ENSRNOG00000014859.
DR Ensembl; ENSRNOT00000105259; ENSRNOP00000091301; ENSRNOG00000014859.
DR Ensembl; ENSRNOT00000105662; ENSRNOP00000097172; ENSRNOG00000014859.
DR Ensembl; ENSRNOT00000107961; ENSRNOP00000095982; ENSRNOG00000014859.
DR Ensembl; ENSRNOT00000119715; ENSRNOP00000093523; ENSRNOG00000014859.
DR GeneID; 293561; -.
DR KEGG; rno:293561; -.
DR UCSC; RGD:1305251; rat.
DR CTD; 220441; -.
DR RGD; 1305251; Rnf152.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00730000111317; -.
DR HOGENOM; CLU_1414689_0_0_1; -.
DR InParanoid; D4A723; -.
DR OMA; REIRCPW; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; D4A723; -.
DR TreeFam; TF331690; -.
DR Reactome; R-RNO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR UniPathway; UPA00143; -.
DR PRO; PR:D4A723; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Proteomes; UP000234681; Chromosome 13.
DR Bgee; ENSRNOG00000014859; Expressed in duodenum and 14 other tissues.
DR Genevisible; D4A723; RN.
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:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
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; 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; PF14634; zf-RING_5; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Apoptosis; Lysosome; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..203
FT /note="E3 ubiquitin-protein ligase RNF152"
FT /id="PRO_0000405835"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 12..55
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 106..165
FT /note="Necessary for interaction with RRAGA"
FT /evidence="ECO:0000250|UniProtKB:Q8N8N0"
FT REGION 140..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 203 AA; 22356 MW; 79BC3DDCDB887DAB CRC64;
METLSQDSLL ECQICFNYYS PRRRPKLLDC KHTCCSVCLQ QMRTSQKDVR CPWCRGITKL
PPGFSVSQLP DDPEVLAVIA IPHTSEHTPV FIKLPSNGCY MLPLPISKER TLLPGDMGCR
LLPGSQQKSL TVVTIPAEQQ PLQGGAPQEA VEEEPDRRGV AKSSTWSGVC TVILVACVLV
FLLGIVLHNM SCISKRFTVI SCG
