RN157_MOUSE
ID RN157_MOUSE Reviewed; 685 AA.
AC Q3TEL6; Q80T75;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=E3 ubiquitin ligase Rnf157 {ECO:0000303|PubMed:25342469};
DE EC=2.3.2.27 {ECO:0000269|PubMed:25342469};
DE AltName: Full=RING finger protein 157;
DE AltName: Full=RING-type E3 ubiquitin transferase Rnf157 {ECO:0000305};
GN Name=Rnf157; Synonyms=Kiaa1917;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 193-685 (ISOFORM 1).
RC STRAIN=C57BL/6J; 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-685 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH APBB1.
RX PubMed=25342469; DOI=10.1038/cdd.2014.163;
RA Matz A., Lee S.J., Schwedhelm-Domeyer N., Zanini D., Holubowska A.,
RA Kannan M., Farnworth M., Jahn O., Goepfert M.C., Stegmueller J.;
RT "Regulation of neuronal survival and morphology by the E3 ubiquitin ligase
RT RNF157.";
RL Cell Death Differ. 22:626-642(2015).
CC -!- FUNCTION: E3 ubiquitin ligase that ubiquitinates APBB1 for its
CC degradation by the proteasome and thus prevents apoptosis and promotes
CC survival of neurons (PubMed:25342469). Has a dual role in neurons as it
CC is also required for dendrite growth and maintenance for which its
CC ligase activity is not critical (PubMed:25342469). May act as a
CC scaffold molecule to regulate this process (PubMed:25342469). Acts as a
CC downstream effector of the interconnected PI3K and MAPK signaling
CC pathways and thus participates in the regulation of the cell cycle (By
CC similarity). {ECO:0000250|UniProtKB:Q96PX1,
CC ECO:0000269|PubMed:25342469}.
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:25342469};
CC -!- SUBUNIT: Interacts with APBB1 (PubMed:25342469). Interacts with CHD1;
CC CHD1-binding controls RNF157 stability (By similarity). Interacts also
CC with ATRN, MEGF8, TECR, MSI2, PLRG1, BYSL, MTERF3, PSMA1, MRPS18B,
CC PRPF4, FASTKD2, SLC25A1, SMU1, CNOT9, MRPS2, MAGT1, FXR2, EMD, PSMD8,
CC HDAC1, RAN, HSD17B12, TXNDC5 AND MRPL19 (By similarity).
CC {ECO:0000250|UniProtKB:Q96PX1, ECO:0000269|PubMed:25342469}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:M0R5D6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TEL6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TEL6-2; Sequence=VSP_021736, VSP_021737;
CC -!- DOMAIN: The D-box motifs play a key role in RNF157 stabilization (By
CC similarity). {ECO:0000250|UniProtKB:M0R5D6}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE41232.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL645861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK169566; BAE41232.1; ALT_INIT; mRNA.
DR EMBL; AK122571; BAC65853.1; -; mRNA.
DR CCDS; CCDS48984.1; -. [Q3TEL6-2]
DR AlphaFoldDB; Q3TEL6; -.
DR STRING; 10090.ENSMUSP00000097776; -.
DR iPTMnet; Q3TEL6; -.
DR PhosphoSitePlus; Q3TEL6; -.
DR MaxQB; Q3TEL6; -.
DR PaxDb; Q3TEL6; -.
DR PRIDE; Q3TEL6; -.
DR ProteomicsDB; 301616; -. [Q3TEL6-1]
DR ProteomicsDB; 301617; -. [Q3TEL6-2]
DR UCSC; uc007mkz.1; mouse. [Q3TEL6-1]
DR MGI; MGI:2442484; Rnf157.
DR eggNOG; KOG4265; Eukaryota.
DR InParanoid; Q3TEL6; -.
DR PhylomeDB; Q3TEL6; -.
DR ChiTaRS; Rnf157; mouse.
DR PRO; PR:Q3TEL6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3TEL6; protein.
DR GO; GO:0044297; C:cell body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR CDD; cd16789; mRING-HC-C3HC5_MGRN1_like---blasttree; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR045195; MGRN1/RNF157_mRING_C3HC5.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996; PTHR22996; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Lipoprotein; Metal-binding; Myristate;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..685
FT /note="E3 ubiquitin ligase Rnf157"
FT /id="PRO_0000261615"
FT ZN_FING 276..315
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 339..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 329..332
FT /note="D-box 1"
FT /evidence="ECO:0000250|UniProtKB:Q96PX1"
FT MOTIF 657..660
FT /note="D-box 2"
FT /evidence="ECO:0000250|UniProtKB:Q96PX1"
FT COMPBIAS 442..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 592
FT /note="I -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_021736"
FT VAR_SEQ 642..685
FT /note="EWQCAEHELGGRRPSARPRSPRGGLGKEASAFRIETVALPGTYV -> TWQH
FT EDNTVNCRHTQRRRLSSSSLEDPEENRPCVWDPMAV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_021737"
SQ SEQUENCE 685 AA; 74534 MW; 22B9382ECBA0E334 CRC64;
MGALTSRQHA GVEEVDIPSN SVYRYPPKSG SYFASHFIMG GEKFDSTHPE GYLFGENSDL
NFLGNRPVAF PYAAPPPQEP VKTLRSLINI RKDTLRLVKC AEEVKSHGEE AGKAKVHYNV
EFTFDTDARV AITIYYQATE EFQNGIASYI PKDNSLQSET VHYKRGVFQQ FCLPSHTVDP
SEWAEEELGF DLDREVYPLV VHAVVDEGDE YFGHCHVLLG TFEKHPDGTF CVKPLKQKQV
VDGVSYLLQE IYGIENKYNT QDSKVAEDDV SDNSAECVVC LSDVRDTLIL PCRHLCLCNT
CADTLRYQAN NCPICRLPFR ALLQIRAMRK KLGPLSPSSF NPIISSQTSD SEEHSSSENI
PPGYEVVSLL EALNGPLTSS PAVPPLHVLG DGHLSGMLPS YGSDGYLPPV RTLSPLDRLS
DCNNQGLKLK KSLSKSISQN SSVLHEEEDE RSCSESDTQL SQRLSVQHPE EGPDVTPESE
NLTLSSSGAV DQSSCTGTPL SSTISSPEDP ASSSLAQSVM SMASSQISTD TVSSMSGSYI
APGTEEEGEA LPSPRAASRA PSEGEETPAE SPDSNFAGLP AGEQDAEGND IIEEEDRSPV
REDGQRTCAF LGMECDNNND FDVASVKALD NKLCSEVCLP GEWQCAEHEL GGRRPSARPR
SPRGGLGKEA SAFRIETVAL PGTYV
