TRI47_MOUSE
ID TRI47_MOUSE Reviewed; 641 AA.
AC Q8C0E3; A2A862; Q6P249; Q811J7; Q8BVZ8; Q8R1K0; Q8R3Y1;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM47 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305|PubMed:29291351};
DE AltName: Full=Tripartite motif-containing protein 47;
GN Name=Trim47 {ECO:0000312|MGI:MGI:1917374};
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 5-641 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 198-641 (ISOFORMS 1 AND 2).
RC STRAIN=C3H/He; TISSUE=Kidney, Mammary gland, and Osteoblast;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72 AND SER-393, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Lung, Spleen, and Testis;
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 TISSUE SPECIFICITY.
RX PubMed=29291351; DOI=10.1038/nm.4461;
RA Ji Y.X., Huang Z., Yang X., Wang X., Zhao L.P., Wang P.X., Zhang X.J.,
RA Alves-Bezerra M., Cai L., Zhang P., Lu Y.X., Bai L., Gao M.M., Zhao H.,
RA Tian S., Wang Y., Huang Z.X., Zhu X.Y., Zhang Y., Gong J., She Z.G., Li F.,
RA Cohen D.E., Li H.;
RT "The deubiquitinating enzyme cylindromatosis mitigates nonalcoholic
RT steatohepatitis.";
RL Nat. Med. 24:213-223(2018).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates the ubiquitination
CC and proteasomal degradation of CYLD. {ECO:0000269|PubMed:29291351}.
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:0000305|PubMed:29291351};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000305|PubMed:29291351}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96LD4}. Nucleus
CC {ECO:0000250|UniProtKB:Q96LD4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C0E3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C0E3-2; Sequence=VSP_011988;
CC -!- TISSUE SPECIFICITY: Expressed in hepatocytes, expression is increased
CC in fatty livers. {ECO:0000269|PubMed:29291351}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27457.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC35997.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL607108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK031572; BAC27457.1; ALT_INIT; mRNA.
DR EMBL; AK075838; BAC35997.1; ALT_INIT; mRNA.
DR EMBL; BC023393; AAH23393.1; -; mRNA.
DR EMBL; BC024468; AAH24468.1; -; mRNA.
DR EMBL; BC043714; AAH43714.1; -; mRNA.
DR EMBL; BC064728; AAH64728.1; -; mRNA.
DR CCDS; CCDS56822.1; -. [Q8C0E3-1]
DR CCDS; CCDS56823.1; -. [Q8C0E3-2]
DR RefSeq; NP_766158.3; NM_172570.5. [Q8C0E3-1]
DR AlphaFoldDB; Q8C0E3; -.
DR SMR; Q8C0E3; -.
DR BioGRID; 229890; 4.
DR STRING; 10090.ENSMUSP00000021120; -.
DR iPTMnet; Q8C0E3; -.
DR PhosphoSitePlus; Q8C0E3; -.
DR jPOST; Q8C0E3; -.
DR MaxQB; Q8C0E3; -.
DR PaxDb; Q8C0E3; -.
DR PRIDE; Q8C0E3; -.
DR ProteomicsDB; 298221; -. [Q8C0E3-1]
DR ProteomicsDB; 298222; -. [Q8C0E3-2]
DR Antibodypedia; 32298; 109 antibodies from 21 providers.
DR DNASU; 217333; -.
DR Ensembl; ENSMUST00000021120; ENSMUSP00000021120; ENSMUSG00000020773. [Q8C0E3-2]
DR Ensembl; ENSMUST00000106441; ENSMUSP00000102049; ENSMUSG00000020773. [Q8C0E3-1]
DR GeneID; 217333; -.
DR KEGG; mmu:217333; -.
DR UCSC; uc007mjw.2; mouse. [Q8C0E3-1]
DR UCSC; uc007mjy.2; mouse. [Q8C0E3-2]
DR CTD; 91107; -.
DR MGI; MGI:1917374; Trim47.
DR VEuPathDB; HostDB:ENSMUSG00000020773; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154334; -.
DR HOGENOM; CLU_013137_0_2_1; -.
DR InParanoid; Q8C0E3; -.
DR OMA; CLESRDY; -.
DR TreeFam; TF351086; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 217333; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Trim47; mouse.
DR PRO; PR:Q8C0E3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C0E3; protein.
DR Bgee; ENSMUSG00000020773; Expressed in right kidney and 159 other tissues.
DR Genevisible; Q8C0E3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
DR CDD; cd15808; SPRY_PRY_TRIM47; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR042780; TRIM47_SPRY_PRY.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..641
FT /note="E3 ubiquitin-protein ligase TRIM47"
FT /id="PRO_0000056271"
FT DOMAIN 413..634
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 9..58
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 181..221
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 81..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 305..325
FT /evidence="ECO:0000255"
FT COMPBIAS 88..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..120
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96LD4"
FT MOD_RES 585
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96LD4"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96LD4"
FT VAR_SEQ 404
FT /note="E -> EA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011988"
FT CONFLICT 297
FT /note="E -> D (in Ref. 3; AAH64728)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 69912 MW; 2D499BB07B03AD80 CRC64;
MDGSGPFSCP ICLEPLREPV TLPCGHNFCL ACLGALWPHR SAGGTGGSGG PARCPLCQEP
FPDGLQLRKN HTLSELLQLR QGSVPGPMSA PASGSTRGAT PEPSAPSAPP PAPEPSAPCA
PEQWPAGEEP VRCDACPEGA ALPAALSCLS CLASFCSAHL APHERSPALR GHRLVPPLRR
LEESLCPRHL RPLERYCRVE RVCLCEACAT QDHRGHELVP LEQERALQEV EQSKVLSAAE
DRMDELGAGI AQSRRTVALI KSAAVAERER VSQMFAEATA TLQSFQNEVM GFIEEGEATM
LGRSQGDLRR QEEQRSRLSK ARHNLGQVPE ADSVSFLQEL LALRLALEEG CGPGPGPPRE
LSFTKSSQVV KAVRDTLISA CASQWEQLRG LGSNEDGLQK LGSEDVESQD PDSTSLLESE
APRDYFLKFA YIVDLDSDTA DKFLQLFGTK GVKRVLCPIN YPESPTRFTH CEQVLGEGAL
DRGTYYWEVE IIEGWVSVGV MAEGFSPQEP YDRGRLGRNA HSCCLQWNGR GFSVWFCGLE
APLPHAFSPT VGVCLEYADH ALAFYAVRDG KLSLLRRLKA SRPRRSGALA SPTDPFQSRL
DSHFSGLFNH RLKPAFFLES VDAHLQIGPL KKSCITVLKR R
