ID TRI63_MOUSE Reviewed; 350 AA. AC Q38HM4; Q8BWC4; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 22-FEB-2012, entry version 62. DE RecName: Full=E3 ubiquitin-protein ligase TRIM63; DE EC=6.3.2.-; DE AltName: Full=Muscle-specific RING finger protein 1; DE Short=MuRF-1; DE Short=MuRF1; DE Short=Muscle RING finger protein 1; DE AltName: Full=Tripartite motif-containing protein 63; GN Name=Trim63; Synonyms=Murf1, Rf1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS AN E3 UBIQUITIN RP LIGASE, INTERACTION WITH TNNI3, DOMAIN, AND SUBCELLULAR LOCATION. RC STRAIN=C57BL/6; RX PubMed=15601779; DOI=10.1073/pnas.0404341102; RA Kedar V., McDonough H., Arya R., Li H.-H., Rockman H.A., Patterson C.; RT "Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that RT degrades cardiac troponin I."; RL Proc. Natl. Acad. Sci. U.S.A. 101:18135-18140(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Heart; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP PROTEIN SEQUENCE OF 197-212, AND MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [4] RP INDUCTION. RX PubMed=12773310; DOI=10.1152/ajpcell.00129.2003; RA Li Y.-P., Chen Y., Li A.S., Reid M.B.; RT "Hydrogen peroxide stimulates ubiquitin-conjugating activity and RT expression of genes for specific E2 and E3 proteins in skeletal muscle RT myotubes."; RL Am. J. Physiol. 285:C806-C812(2003). RN [5] RP FUNCTION, AND INTERACTION WITH GNB2L1 AND PRKCE. RX PubMed=15596539; DOI=10.1083/jcb.200402033; RA Arya R., Kedar V., Hwang J.R., McDonough H., Li H.-H., Taylor J., RA Patterson C.; RT "Muscle ring finger protein-1 inhibits PKC-epsilon activation and RT prevents cardiomyocyte hypertrophy."; RL J. Cell Biol. 167:1147-1159(2004). CC -!- FUNCTION: E3 ubiquitin ligase. Regulates proteasomal degradation CC of cardiac troponin I/TNNI3 and probably of other sarcomeric- CC associated proteins. May play a role in striated muscle atrophy CC and hypertrophy by regulating an anti-hypertrophic PKC-mediated CC signaling pathway. May regulate the organization of myofibrils CC through TTN in muscle cells. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Homooligomer and heterooligomer. Interacts with SUMO2, CC titin/TTN and GMEB1. Interacts with TRIM54 and probably with CC TRIM55 (By similarity). Interacts with TNNI3. Forms a ternary CC complex with GNB2L1 and PRKCE. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, myofibril, CC sarcomere, M line (By similarity). Cytoplasm, myofibril, CC sarcomere, Z line (By similarity). Note=Localizes to the M- and Z- CC lines in skeletal muscle (By similarity). Colocalizes with TNNI3 CC in myocytes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q38HM4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q38HM4-2; Sequence=VSP_016647, VSP_016648; CC Note=No experimental confirmation available; CC -!- INDUCTION: By hydrogen peroxide. CC -!- DOMAIN: The RING-type zinc finger mediates interaction with SUMO2 CC and localization to the nucleus (By similarity). Also required for CC the E3 ubiquitin ligase activity. CC -!- SIMILARITY: Contains 1 B box-type zinc finger. CC -!- SIMILARITY: Contains 1 COS domain. CC -!- SIMILARITY: Contains 1 RING-type zinc finger. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ229108; ABB16283.1; -; mRNA. DR EMBL; AK052911; BAC35199.1; -; mRNA. DR IPI; IPI00226235; -. DR IPI; IPI00660145; -. DR UniGene; Mm.331961; -. DR ProteinModelPortal; Q38HM4; -. DR SMR; Q38HM4; 9-161. DR STRING; Q38HM4; -. DR PhosphoSite; Q38HM4; -. DR PRIDE; Q38HM4; -. DR UCSC; uc008ves.1; mouse. DR MGI; MGI:2447992; Trim63. DR eggNOG; NOG310224; -. DR HOVERGEN; HBG071242; -. DR OrthoDB; EOG457571; -. DR ArrayExpress; Q38HM4; -. DR CleanEx; MM_TRIM63; -. DR Genevestigator; Q38HM4; -. DR GermOnline; ENSMUSG00000028834; Mus musculus. DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR InterPro; IPR017903; COS_domain. DR InterPro; IPR000315; Znf_B-box. DR InterPro; IPR018957; Znf_C3HC4_RING-type. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1. DR Pfam; PF00643; zf-B_box; 1. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00336; BBOX; 1. DR SMART; SM00184; RING; 1. DR PROSITE; PS51262; COS; 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; Complete proteome; Cytoplasm; KW Direct protein sequencing; Ligase; Metal-binding; Muscle protein; KW Nucleus; Reference proteome; Ubl conjugation pathway; Zinc; KW Zinc-finger. FT CHAIN 1 350 E3 ubiquitin-protein ligase TRIM63. FT /FTId=PRO_0000056291. FT DOMAIN 267 325 COS. FT ZN_FING 23 79 RING-type. FT ZN_FING 117 159 B box-type. FT REGION 74 218 Interaction with TTN (By similarity). FT COILED 207 269 Potential. FT VAR_SEQ 111 151 SRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSLCKVFGAH FT -> RSVCSRTAPPLPQAPPTSRSLQLLSPAQRASTLYRRQN FT LSS (in isoform 2). FT /FTId=VSP_016647. FT VAR_SEQ 152 350 Missing (in isoform 2). FT /FTId=VSP_016648. FT CONFLICT 6 6 G -> S (in Ref. 2; BAC35199). FT CONFLICT 42 42 N -> D (in Ref. 2; BAC35199). SQ SEQUENCE 350 AA; 39491 MW; 1840B7BB2F77DEC1 CRC64; MDYKSGLIPD GNAMENLEKQ LICPICLEMF TKPVVILPCQ HNLCRKCAND IFQAANPYWT NRGGSVSMSG GRFRCPSCRH EVIMDRHGVY GLQRNLLVEN IIDIYKQECS SRPLQKGSHP MCKEHEDEKI NIYCLTCEVP TCSLCKVFGA HQACEVAPLQ SIFQGQKTEL SNCISMLVAG NDRVQTIISQ LVDSCRVTKE NSHQVKEELS QKFDTLYAIL DEKKSELLQR ITQEQEEKLG FIEALILQYR EQLEKSTKLV ETAIQSLDEP GGATFLSSAK QLIKSNVEAS KGCQLGKTEQ GFENMDYFTL DLEHIAEALR AIDFGTDEEE EEFTEEEADE EEGVTTEGHQ //