RN167_MOUSE
ID RN167_MOUSE Reviewed; 347 AA.
AC Q91XF4; Q3U4S5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=E3 ubiquitin-protein ligase RNF167 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9H6Y7};
DE AltName: Full=RING finger protein 167;
DE Flags: Precursor;
GN Name=Rnf167;
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=NOD; TISSUE=Thymus;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts as a regulator of the
CC TORC1 signaling pathway. Positively regulates the TORC1 signaling
CC pathway independently of arginine levels: acts by catalyzing 'Lys-29'-
CC polyubiquitination and degradation of CASTOR1, releasing the GATOR2
CC complex from CASTOR1. Also negatively regulates the TORC1 signaling
CC pathway in response to leucine deprivation: acts by mediating 'Lys-63'-
CC linked polyubiquitination of SESN2, promoting SESN2-interaction with
CC the GATOR2 complex. Also involved in protein trafficking and
CC localization. Acts as a regulator of synaptic transmission by mediating
CC ubiquitination and degradation of AMPAR receptor GluA2/GRIA2. Does not
CC catalyze ubiquitination of GluA1/GRIA1. Also acts as a regulator of the
CC recycling endosome pathway by mediating ubiquitination of VAMP3.
CC Regulates lysosome positioning by catalyzing ubiquitination and
CC degradation of ARL8B. Plays a role in growth regulation involved in
CC G1/S transition by mediating, possibly by mediating ubiquitination of
CC SLC22A18. Acts with a limited set of E2 enzymes, such as UBE2D1 and
CC UBE2N. {ECO:0000250|UniProtKB:Q9H6Y7}.
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:Q9H6Y7};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9H6Y7}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9H6Y7};
CC Single-pass type I membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q9H6Y7}; Single-pass type I membrane protein
CC {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:Q9H6Y7};
CC Single-pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9H6Y7}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Targeted to cytoplasmic membranes; mainly localizes
CC to lysosomal membrane. A subpopulation localizes to the cell membrane
CC of neurons. {ECO:0000250|UniProtKB:Q9H6Y7}.
CC -!- PTM: Autoubiquitinated in vitro in the presence of UBE2D1 and UBE2E1.
CC {ECO:0000250|UniProtKB:Q9H6Y7}.
CC -!- SIMILARITY: Belongs to the Godzilla family. {ECO:0000305}.
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DR EMBL; AK154071; BAE32356.1; -; mRNA.
DR EMBL; AL596117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010777; AAH10777.1; -; mRNA.
DR CCDS; CCDS24959.1; -.
DR RefSeq; NP_081721.1; NM_027445.2.
DR AlphaFoldDB; Q91XF4; -.
DR SMR; Q91XF4; -.
DR STRING; 10090.ENSMUSP00000036472; -.
DR GlyGen; Q91XF4; 1 site.
DR iPTMnet; Q91XF4; -.
DR PhosphoSitePlus; Q91XF4; -.
DR EPD; Q91XF4; -.
DR MaxQB; Q91XF4; -.
DR PaxDb; Q91XF4; -.
DR PeptideAtlas; Q91XF4; -.
DR PRIDE; Q91XF4; -.
DR ProteomicsDB; 299921; -.
DR Antibodypedia; 23476; 91 antibodies from 20 providers.
DR DNASU; 70510; -.
DR Ensembl; ENSMUST00000037534; ENSMUSP00000036472; ENSMUSG00000040746.
DR GeneID; 70510; -.
DR KEGG; mmu:70510; -.
DR UCSC; uc007jvt.1; mouse.
DR CTD; 26001; -.
DR MGI; MGI:1917760; Rnf167.
DR VEuPathDB; HostDB:ENSMUSG00000040746; -.
DR eggNOG; KOG4628; Eukaryota.
DR GeneTree; ENSGT00940000159547; -.
DR HOGENOM; CLU_035275_1_1_1; -.
DR InParanoid; Q91XF4; -.
DR OMA; RIPTHKF; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q91XF4; -.
DR TreeFam; TF317486; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 70510; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Rnf167; mouse.
DR PRO; PR:Q91XF4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91XF4; protein.
DR Bgee; ENSMUSG00000040746; Expressed in granulocyte and 258 other tissues.
DR ExpressionAtlas; Q91XF4; baseline and differential.
DR Genevisible; Q91XF4; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0036020; C:endolysosome membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1990253; P:cellular response to leucine starvation; ISS:UniProtKB.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISO:MGI.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd02123; PA_C_RZF_like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR044744; ZNRF4/RNF13/RNF167_PA.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Endosome; Glycoprotein; Lysosome; Membrane; Metal-binding;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..347
FT /note="E3 ubiquitin-protein ligase RNF167"
FT /id="PRO_0000245594"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 48..152
FT /note="PA"
FT /evidence="ECO:0000255"
FT ZN_FING 230..272
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 271..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..299
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 343
FT /note="S -> F (in Ref. 1; BAE32356)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 38014 MW; EB2047A7B97817DC CRC64;
MHPAAFPLPV VVATVLWGAA PVRGLIRATS EHNASMDFAD LPALFGATLS DEGLQGFLVE
AHPENACGPI APPPSAPVNG SVFIALLRRF DCNFDLKVLN AQKAGYGAAV VHNVNSNELL
NMVWNSEEIQ QQIWIPSVFI GERSAEYLRA LFVYEKGARV LLVPDNSFPL GYYLIPFTGI
VGLLVLAMGT VLIVRCIQHR KRLQRNRLTK EQLKQIPTHD YQKGDEYDVC AICLDEYEDG
DKLRVLPCAH AYHSRCVDPW LTQTRKTCPI CKQPVHRGPG DEEQEEETQE QEEGDEGEPR
DQPASEWTPL LGSSPTLPTS FGSLAPAPLV FPGPSTDPSP PSSAALA
