GenomeNet

Database: UniProt
Entry: RN152_CHICK
LinkDB: RN152_CHICK
Original site: 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   08-MAY-2019, entry version 60.
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;
OC   Phasianidae; 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.,
RA   Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E.,
RA   Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W.,
RA   Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C.,
RA   Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E.,
RA   Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J.,
RA   Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M.,
RA   Paton B., Smith J., Morrice D., Daniels L., Tempest H.G.,
RA   Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V.,
RA   Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J.,
RA   van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J.,
RA   Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H.,
RA   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.,
RA   Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J.,
RA   Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H.,
RA   Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C.,
RA   Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C.,
RA   Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P.,
RA   King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S.,
RA   Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S.,
RA   Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S.,
RA   Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z.,
RA   Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J.,
RA   Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z.,
RA   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.,
RA   Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G.,
RA   Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D.,
RA   Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G.,
RA   Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A.,
RA   Mardis E.R., Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide
RT   unique 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
CC       cellular response to amino acid availability. Also mediates 'Lys-
CC       48'-linked polyubiquitination of target proteins and their
CC       subsequent targeting to the proteasome for degradation.
CC       {ECO:0000250|UniProtKB:Q8N8N0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC         protein]-L-lysine.; EC=2.3.2.27;
CC         Evidence={ECO:0000250|UniProtKB:Q8N8N0};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q8N8N0}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane
CC       {ECO:0000250|UniProtKB:Q8N8N0}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q8N8N0}.
CC   -!- SIMILARITY: Belongs to the RNF152 family. {ECO:0000305}.
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   SMR; E1C2W7; -.
DR   STRING; 9031.ENSGALP00000042495; -.
DR   PaxDb; E1C2W7; -.
DR   Ensembl; ENSGALT00000043782; ENSGALP00000042495; ENSGALG00000028822.
DR   GeneID; 420909; -.
DR   KEGG; gga:420909; -.
DR   CTD; 220441; -.
DR   eggNOG; ENOG410ITF4; Eukaryota.
DR   eggNOG; ENOG4111BNB; LUCA.
DR   GeneTree; ENSGT00730000111317; -.
DR   InParanoid; E1C2W7; -.
DR   KO; K15705; -.
DR   OMA; SQKDLRC; -.
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 10 organ(s), highest expression level in kidney.
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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR25464:SF1; PTHR25464:SF1; 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   Complete proteome; Lysosome; Membrane; Metal-binding;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    203       E3 ubiquitin-protein ligase RNF152.
FT                                /FTId=PRO_0000405836.
FT   TRANSMEM    167    187       Helical. {ECO:0000255}.
FT   ZN_FING      12     55       RING-type. {ECO:0000255|PROSITE-
FT                                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
//
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