ID   R152B_XENLA             Reviewed;         203 AA.
AC   Q68EV7;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=E3 ubiquitin-protein ligase rnf152-B {ECO:0000305};
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8N8N0};
DE   AltName: Full=RING finger protein 152-B {ECO:0000250|UniProtKB:Q8N8N0};
DE   AltName: Full=RING-type E3 ubiquitin transferase rnf152-A {ECO:0000305};
GN   Name=rnf152-b {ECO:0000250|UniProtKB:Q8N8N0};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) 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; BC080093; AAH80093.1; -; mRNA.
DR   RefSeq; NP_001087549.1; NM_001094080.1.
DR   RefSeq; XP_018122082.1; XM_018266593.1.
DR   AlphaFoldDB; Q68EV7; -.
DR   SMR; Q68EV7; -.
DR   DNASU; 447373; -.
DR   GeneID; 447373; -.
DR   KEGG; xla:447373; -.
DR   CTD; 447373; -.
DR   Xenbase; XB-GENE-17338332; rnf152.L.
DR   OMA; REIRCPW; -.
DR   OrthoDB; 489543at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 447373; Expressed in lung and 15 other tissues.
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; IEA:InterPro.
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: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   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..203
FT                   /note="E3 ubiquitin-protein ligase rnf152-B"
FT                   /id="PRO_0000405839"
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"
SQ   SEQUENCE   203 AA;  22607 MW;  A3E7D6DD939E8609 CRC64;
     METLSQDSLL ECQICFNYYS PRRRPKLLDC KHTCCSVCLQ QMRASQKDLR CPWCRGVTKL
     PPGYSVSELP DDPDVVAVIA IPHASENTPV FIKLPSNGCY MWPLPVSKER ALLPGDIGCR
     LLPGNQQKPV TVVTMPMEQQ PLHGNIPQDI IEEEHERRGV VKSSTWSGVC TVILVACVLV
     FLLGIVLHNM SCISKRFTVI SCG