RN149_MOUSE
ID RN149_MOUSE Reviewed; 394 AA.
AC Q3U2C5; E9QAH5; Q14BF0; Q8CGR2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=E3 ubiquitin-protein ligase RNF149;
DE EC=2.3.2.27;
DE AltName: Full=Goliath-related E3 ubiquitin-protein ligase 4;
DE AltName: Full=RING finger protein 149;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF149 {ECO:0000305};
DE Flags: Precursor;
GN Name=Rnf149; Synonyms=Greul4;
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] (ISOFORM 1).
RC STRAIN=NOD;
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] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 113-394.
RC STRAIN=CD-1;
RX PubMed=12435366; DOI=10.1006/dbio.2002.0814;
RA Borchers A.G.M., Hufton A.L., Eldridge A.G., Jackson P.K., Harland R.M.,
RA Baker J.C.;
RT "The E3 ubiquitin ligase GREUL1 anteriorizes ectoderm during Xenopus
RT development.";
RL Dev. Biol. 251:395-408(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341 AND SER-344, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-327, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its
CC proteasomal degradation. {ECO:0000250}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3U2C5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U2C5-2; Sequence=VSP_021734;
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
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DR EMBL; AK155360; BAE33216.1; -; mRNA.
DR EMBL; AC119809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115968; AAI15969.1; -; mRNA.
DR EMBL; AY155439; AAN75220.1; -; mRNA.
DR CCDS; CCDS14907.1; -. [Q3U2C5-1]
DR RefSeq; NP_001028307.2; NM_001033135.3. [Q3U2C5-1]
DR AlphaFoldDB; Q3U2C5; -.
DR SMR; Q3U2C5; -.
DR STRING; 10090.ENSMUSP00000050388; -.
DR GlyGen; Q3U2C5; 3 sites.
DR iPTMnet; Q3U2C5; -.
DR PhosphoSitePlus; Q3U2C5; -.
DR EPD; Q3U2C5; -.
DR jPOST; Q3U2C5; -.
DR MaxQB; Q3U2C5; -.
DR PaxDb; Q3U2C5; -.
DR PeptideAtlas; Q3U2C5; -.
DR PRIDE; Q3U2C5; -.
DR ProteomicsDB; 301614; -. [Q3U2C5-1]
DR ProteomicsDB; 301615; -. [Q3U2C5-2]
DR Antibodypedia; 2559; 181 antibodies from 23 providers.
DR DNASU; 67702; -.
DR Ensembl; ENSMUST00000062525; ENSMUSP00000050388; ENSMUSG00000048234. [Q3U2C5-1]
DR GeneID; 67702; -.
DR KEGG; mmu:67702; -.
DR UCSC; uc007atl.3; mouse. [Q3U2C5-1]
DR CTD; 284996; -.
DR MGI; MGI:2677438; Rnf149.
DR VEuPathDB; HostDB:ENSMUSG00000048234; -.
DR eggNOG; KOG4628; Eukaryota.
DR GeneTree; ENSGT00940000161020; -.
DR HOGENOM; CLU_049885_1_0_1; -.
DR InParanoid; Q3U2C5; -.
DR OMA; NEEHYGN; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q3U2C5; -.
DR TreeFam; TF317486; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 67702; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Rnf149; mouse.
DR PRO; PR:Q3U2C5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3U2C5; protein.
DR Bgee; ENSMUSG00000048234; Expressed in granulocyte and 124 other tissues.
DR ExpressionAtlas; Q3U2C5; baseline and differential.
DR Genevisible; Q3U2C5; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0031647; P:regulation of protein stability; IDA:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16804; RING-H2_RNF149; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR042712; RNF149_RING-H2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02225; PA; 1.
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 Alternative splicing; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..394
FT /note="E3 ubiquitin-protein ligase RNF149"
FT /id="PRO_0000261612"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 66..171
FT /note="PA"
FT ZN_FING 265..306
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 321..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..145
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021734"
FT CONFLICT 115
FT /note="T -> S (in Ref. 1; BAE33216)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="G -> E (in Ref. 1; BAE33216)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 42553 MW; 065F9207CDDDFCE2 CRC64;
MAARRRPAAG VGARDALAVL ALALCTPGVG GGALEWYSAM VSIEYVDPQS NLTVWSVSES
GRFGESSLRE ERQGLVGVPR APAPAEGCAP DTRFVAPGAL GNAPWVALVA RGGCTFKDKV
LAAARRNASA VVVYNLESNG NATEPMSHAG TGNIVVIMIS YPKGREIFDL VQKGIPVKMR
IEIGTRHMQE FISGQSVVFV AIAFITMMII SLAWLIFYYI QRFLYTGSQF GSQNHRKETK
KVIGQLPLHT VKHGEKGIDV DAENCAVCIE NFKVKDVIRI LPCKHIFHRI CIDPWLLDHR
TCPMCKLDVI KALGYWGDPE DTQELPTPEA APGRVSVGNL SVTSQDEERS ESNLPSSSSS
ESGPHRPCLK EDAGEDTALL GAGRSEPQHG GSIC
