RN152_AILME
ID RN152_AILME Reviewed; 203 AA.
AC D2H6Z0;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 55.
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=PANDA_005868 {ECO:0000312|EMBL:EFB24541.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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. {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}.
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DR EMBL; GL192540; EFB24541.1; -; Genomic_DNA.
DR RefSeq; XP_019653372.1; XM_019797813.1.
DR AlphaFoldDB; D2H6Z0; -.
DR SMR; D2H6Z0; -.
DR STRING; 9646.ENSAMEP00000020126; -.
DR Ensembl; ENSAMET00000020895; ENSAMEP00000020126; ENSAMEG00000019059.
DR GeneID; 100463900; -.
DR CTD; 220441; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00730000111317; -.
DR HOGENOM; CLU_1414689_0_0_1; -.
DR InParanoid; D2H6Z0; -.
DR OMA; REIRCPW; -.
DR OrthoDB; 489543at2759; -.
DR TreeFam; TF331690; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
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_0000405834"
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"
SQ SEQUENCE 203 AA; 22280 MW; 23708C5611B41D3E CRC64;
METLSQDSLL ECQICFNYYS PRRRPKLLDC KHTCCSVCLQ QMRTSQKDVR CPWCRGITKL
PPGFSVAQLP DDPEVLAVIA IPHASEHTPV FIKLPSNGCY MLPLPISKER ALLPGDMGCR
LLPGSQQKSV TVVTVPAEQR PLQGGAPQEA VEEEPDRRGV AKSSTWSGVC TVILVACVLV
FLLGIVLHNM SCISKRFTVI SCG
