RN152_MOUSE
ID RN152_MOUSE Reviewed; 203 AA.
AC Q8BG47; Q0VF67;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
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|MGI:MGI:2443787};
DE AltName: Full=RING-type E3 ubiquitin transferase RNF152 {ECO:0000305};
GN Name=Rnf152 {ECO:0000312|MGI:MGI:2443787};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25936802; DOI=10.1016/j.molcel.2015.03.033;
RA Deng L., Jiang C., Chen L., Jin J., Wei J., Zhao L., Chen M., Pan W.,
RA Xu Y., Chu H., Wang X., Ge X., Li D., Liao L., Liu M., Li L., Wang P.;
RT "The ubiquitination of RagA GTPase by RNF152 negatively regulates mTORC1
RT activation.";
RL Mol. Cell 58:804-818(2015).
RN [4]
RP INTERACTION WITH SEC16A.
RX PubMed=29300766; DOI=10.1371/journal.pone.0190407;
RA Wu Y., Guo X.P., Kanemoto S., Maeoka Y., Saito A., Asada R., Matsuhisa K.,
RA Ohtake Y., Imaizumi K., Kaneko M.;
RT "Sec16A, a key protein in COPII vesicle formation, regulates the stability
RT and localization of the novel ubiquitin ligase RNF183.";
RL PLoS ONE 13:E0190407-E0190407(2018).
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 (PubMed:25936802). Also mediates
CC 'Lys-48'-linked polyubiquitination of target proteins and their
CC subsequent targeting to the proteasome for degradation. Induces
CC apoptosis when overexpressed (By similarity).
CC {ECO:0000250|UniProtKB:Q8N8N0, ECO:0000269|PubMed:25936802}.
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 (By similarity). Interacts with SEC16A
CC (PubMed:29300766). {ECO:0000250|UniProtKB:Q8N8N0,
CC ECO:0000269|PubMed:29300766}.
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 -!- DISRUPTION PHENOTYPE: Mice lacking Rnf152 do not show overt embryonic
CC development defect. {ECO:0000269|PubMed:25936802}.
CC -!- SIMILARITY: Belongs to the RNF152 family. {ECO:0000305}.
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DR EMBL; AK035832; BAC29205.1; -; mRNA.
DR EMBL; AK044638; BAC32015.1; -; mRNA.
DR EMBL; BC118961; AAI18962.1; -; mRNA.
DR CCDS; CCDS15204.1; -.
DR RefSeq; NP_001153840.1; NM_001160368.1.
DR RefSeq; NP_848894.1; NM_178779.4.
DR RefSeq; XP_006529762.1; XM_006529699.3.
DR RefSeq; XP_017176696.1; XM_017321207.1.
DR AlphaFoldDB; Q8BG47; -.
DR SMR; Q8BG47; -.
DR STRING; 10090.ENSMUSP00000050103; -.
DR PhosphoSitePlus; Q8BG47; -.
DR PaxDb; Q8BG47; -.
DR PRIDE; Q8BG47; -.
DR ProteomicsDB; 300415; -.
DR Antibodypedia; 71070; 10 antibodies from 7 providers.
DR DNASU; 320311; -.
DR Ensembl; ENSMUST00000058688; ENSMUSP00000050103; ENSMUSG00000047496.
DR Ensembl; ENSMUST00000172299; ENSMUSP00000128632; ENSMUSG00000047496.
DR GeneID; 320311; -.
DR KEGG; mmu:320311; -.
DR UCSC; uc011wpy.1; mouse.
DR CTD; 220441; -.
DR MGI; MGI:2443787; Rnf152.
DR VEuPathDB; HostDB:ENSMUSG00000047496; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00730000111317; -.
DR HOGENOM; CLU_1414689_0_0_1; -.
DR InParanoid; Q8BG47; -.
DR OMA; REIRCPW; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q8BG47; -.
DR TreeFam; TF331690; -.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 320311; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Rnf152; mouse.
DR PRO; PR:Q8BG47; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BG47; protein.
DR Bgee; ENSMUSG00000047496; Expressed in pigmented layer of retina and 181 other tissues.
DR Genevisible; Q8BG47; MM.
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:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
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; IDA:UniProtKB.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP: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 1: Evidence at protein level;
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_0000056112"
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 139..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 203 AA; 22353 MW; C8BC2F7F51B37DAA CRC64;
METLSQDSLL ECQICFNYYS PRRRPKLLDC KHTCCSVCLQ QMRTSQKDVR CPWCRGITKL
PPGFSVSQLP DDPEVLAVIA IPHTSEHTPV FIKLPSNGCY MLPLPISKER TLLPGDMGCR
LLPGSQQKSL TVVTIPAEQQ PLQGGAPPEA VEEEPDRRGV VKSSTWSGVC TVILVACVLV
FLLGIVLHNM SCISKRFTVI SCG
