RN115_MOUSE
ID RN115_MOUSE Reviewed; 305 AA.
AC Q9D0C1; Q8R5A1; Q9D885;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=E3 ubiquitin-protein ligase RNF115 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:17462600, ECO:0000269|PubMed:23418353};
DE AltName: Full=RING finger protein 115 {ECO:0000312|MGI:MGI:1915095};
DE AltName: Full=RING-type E3 ubiquitin transferase RNF115 {ECO:0000305};
DE AltName: Full=Rab7-interacting RING finger protein {ECO:0000303|PubMed:12972561};
DE Short=Rabring 7 {ECO:0000303|PubMed:12972561};
DE AltName: Full=Zinc finger protein 364 {ECO:0000250|UniProtKB:Q9Y4L5};
GN Name=Rnf115 {ECO:0000312|MGI:MGI:1915095};
GN Synonyms=Zfp364 {ECO:0000312|MGI:MGI:1915095},
GN Znf364 {ECO:0000250|UniProtKB:Q9Y4L5};
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=Embryo, and Small intestine;
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].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 INTERACTION WITH RAB7A, AND SUBCELLULAR LOCATION.
RX PubMed=12972561; DOI=10.1091/mbc.e02-08-0495;
RA Mizuno K., Kitamura A., Sasaki T.;
RT "Rabring7, a novel Rab7 target protein with a RING finger motif.";
RL Mol. Biol. Cell 14:3741-3752(2003).
RN [4]
RP FUNCTION, PATHWAY, CATALYTIC ACTIVITY, AUTOUBIQUITINATION, AND MUTAGENESIS
RP OF CYS-229.
RX PubMed=17462600; DOI=10.1016/j.bbrc.2007.04.052;
RA Sakane A., Hatakeyama S., Sasaki T.;
RT "Involvement of Rabring7 in EGF receptor degradation as an E3 ligase.";
RL Biochem. Biophys. Res. Commun. 357:1058-1064(2007).
RN [5]
RP FUNCTION, PATHWAY, CATALYTIC ACTIVITY, INTERACTION WITH EGFR AND FLT3, AND
RP MUTAGENESIS OF CYS-22; CYS-25 AND CYS-229.
RX PubMed=23418353; DOI=10.1242/jcs.116129;
RA Smith C.J., Berry D.M., McGlade C.J.;
RT "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of
RT the epidermal growth factor receptor.";
RL J. Cell Sci. 126:1366-1380(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys-
CC 48'- and/or 'Lys-63'-linked polyubiquitination of substrates and may
CC play a role in diverse biological processes. Through their
CC polyubiquitination, may play a role in the endosomal trafficking and
CC degradation of membrane receptors including EGFR, FLT3, MET and CXCR4.
CC {ECO:0000269|PubMed:17462600, ECO:0000303|PubMed:23418353}.
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:0000269|PubMed:17462600,
CC ECO:0000269|PubMed:23418353};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:17462600, ECO:0000269|PubMed:23418353}.
CC -!- SUBUNIT: Interacts with RAB7A. Interacts with EGFR and FLT3.
CC {ECO:0000269|PubMed:12972561, ECO:0000269|PubMed:23418353}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12972561}.
CC Note=The GTP-bound form of RAB7A recruits RNF115 from the cytosol onto
CC late endosomes/lysosomes. {ECO:0000269|PubMed:12972561}.
CC -!- PTM: RING-type zinc finger-dependent and E2-dependent
CC autoubiquitination. {ECO:0000269|PubMed:17462600}.
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DR EMBL; AK008329; BAB25607.1; -; mRNA.
DR EMBL; AK011584; BAB27716.1; -; mRNA.
DR EMBL; BC023113; AAH23113.1; -; mRNA.
DR CCDS; CCDS17647.1; -.
DR RefSeq; NP_080682.3; NM_026406.3.
DR AlphaFoldDB; Q9D0C1; -.
DR SMR; Q9D0C1; -.
DR BioGRID; 212475; 7.
DR IntAct; Q9D0C1; 2.
DR MINT; Q9D0C1; -.
DR STRING; 10090.ENSMUSP00000029740; -.
DR iPTMnet; Q9D0C1; -.
DR PhosphoSitePlus; Q9D0C1; -.
DR MaxQB; Q9D0C1; -.
DR PaxDb; Q9D0C1; -.
DR PRIDE; Q9D0C1; -.
DR ProteomicsDB; 300526; -.
DR Antibodypedia; 74554; 103 antibodies from 24 providers.
DR Ensembl; ENSMUST00000029740; ENSMUSP00000029740; ENSMUSG00000028098.
DR GeneID; 67845; -.
DR KEGG; mmu:67845; -.
DR UCSC; uc008qoe.2; mouse.
DR CTD; 27246; -.
DR MGI; MGI:1915095; Rnf115.
DR VEuPathDB; HostDB:ENSMUSG00000028098; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000157203; -.
DR HOGENOM; CLU_034892_0_2_1; -.
DR InParanoid; Q9D0C1; -.
DR OMA; QDNRTNE; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; Q9D0C1; -.
DR TreeFam; TF317985; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 67845; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Rnf115; mouse.
DR PRO; PR:Q9D0C1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D0C1; protein.
DR Bgee; ENSMUSG00000028098; Expressed in soleus muscle and 255 other tissues.
DR ExpressionAtlas; Q9D0C1; baseline and differential.
DR Genevisible; Q9D0C1; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4L5"
FT CHAIN 2..305
FT /note="E3 ubiquitin-protein ligase RNF115"
FT /id="PRO_0000056315"
FT ZN_FING 229..270
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 100..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4L5"
FT MUTAGEN 22
FT /note="C->A: Loss of interaction with EGFR and FLT3. No
FT effect on E3 ubiquitin protein ligase activity; when
FT associated with A-25."
FT /evidence="ECO:0000269|PubMed:23418353"
FT MUTAGEN 25
FT /note="C->A: Loss of interaction with EGFR and FLT3. No
FT effect on E3 ubiquitin protein ligase activity; when
FT associated with A-22."
FT /evidence="ECO:0000269|PubMed:23418353"
FT MUTAGEN 229
FT /note="C->S: Loss of E3 ubiquitin protein ligase activity."
FT /evidence="ECO:0000269|PubMed:17462600,
FT ECO:0000269|PubMed:23418353"
FT CONFLICT 40
FT /note="R -> G (in Ref. 1; BAB25607)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="E -> G (in Ref. 2; AAH23113)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 33859 MW; DF89F268AFE91625 CRC64;
MAEASAAGAD AGSAVAAHRF FCHFCKGEVN PKLPEYICPR CDSGFIEEVT DDSSFLGGGG
SRTDNSTATH FAELWDHLDH TMFLQDFRPF LSSNPLDQDN RANERGHQTH TDFWGPSRPP
RLPMTRRYRS RGSTRPDRSP AIEGIIQQIF AGFFANSAIP GSPHPFSWSG MLHSNPGDYA
WGQTGLDAIV TQLLGQLENT GPPPADKEKI TSLPTVTVTQ EQVNTGLECP VCKEDYTVEE
KVRQLPCNHF FHSSCIVPWL ELHDTCPVCR KSLNGEDSTR QTQSSEASAS NRFSNDSQLH
DRWTF
