RN152_CHICK
ID RN152_CHICK Reviewed; 203 AA.
AC E1C2W7;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 69.
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};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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; AC145926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001291963.1; NM_001305034.1.
DR RefSeq; XP_015137664.1; XM_015282178.1.
DR RefSeq; XP_015137666.1; XM_015282180.1.
DR RefSeq; XP_015137667.1; XM_015282181.1.
DR AlphaFoldDB; E1C2W7; -.
DR STRING; 9031.ENSGALP00000042495; -.
DR PaxDb; E1C2W7; -.
DR Ensembl; ENSGALT00000043782; ENSGALP00000042495; ENSGALG00000028822.
DR GeneID; 420909; -.
DR KEGG; gga:420909; -.
DR CTD; 220441; -.
DR VEuPathDB; HostDB:geneid_420909; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00730000111317; -.
DR HOGENOM; CLU_1414689_0_0_1; -.
DR InParanoid; E1C2W7; -.
DR OMA; REIRCPW; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; E1C2W7; -.
DR TreeFam; TF331690; -.
DR Reactome; R-GGA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR UniPathway; UPA00143; -.
DR PRO; PR:E1C2W7; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000028822; Expressed in kidney and 13 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:0031267; F:small GTPase binding; IEA:Ensembl.
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: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 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"
FT /id="PRO_0000405836"
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; 22239 MW; E28E355B28C3BCF4 CRC64;
METLSQDSLL ECQICFNYYS PRRRPKLLDC KHTCCSVCLQ QMRTSQKDLR CPWCRGITKL
PPGYSVSQLP DDPEVIAVIA IPHTSEHTPV FIKLPSNGCY MLPLPLSKER AMLPGDIGCR
LLPGSQQKSL AVVTIPAEQQ PLQGGLPAEA GAEEPDRRGV VKSSTWSGVC TVILVACVLV
FLLGIVLHNM SCISKRFTVI SCG
