TRI63_RAT
ID TRI63_RAT Reviewed; 351 AA.
AC Q91Z63;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM63;
DE EC=2.3.2.27;
DE AltName: Full=Muscle-specific RING finger protein 1;
DE Short=MuRF-1;
DE Short=MuRF1;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM63 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 63;
GN Name=Trim63; Synonyms=Murf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, AND FUNCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=11679633; DOI=10.1126/science.1065874;
RA Bodine S.C., Latres E., Baumhueter S., Lai V.K.-M., Nunez L., Clarke B.A.,
RA Poueymirou W.T., Panaro F.J., Na E., Dharmarajan K., Pan Z.-Q.,
RA Valenzuela D.M., DeChiara T.M., Stitt T.N., Yancopoulos G.D., Glass D.J.;
RT "Identification of ubiquitin ligases required for skeletal muscle
RT atrophy.";
RL Science 294:1704-1708(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 SUBCELLULAR LOCATION.
RX PubMed=11927605; DOI=10.1083/jcb.200108089;
RA McElhinny A.S., Kakinuma K., Sorimachi H., Labeit S., Gregorio C.C.;
RT "Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric
RT M-line and thick filament structure and may have nuclear functions via its
RT interaction with glucocorticoid modulatory element binding protein-1.";
RL J. Cell Biol. 157:125-136(2002).
RN [4]
RP INDUCTION.
RX PubMed=12782319; DOI=10.1016/s0014-5793(03)00505-2;
RA Dehoux M.J.M., van Beneden R.P., Fernandez-Celemin L., Lause P.L.,
RA Thissen J.-P.M.;
RT "Induction of MafBx and Murf ubiquitin ligase mRNAs in rat skeletal muscle
RT after LPS injection.";
RL FEBS Lett. 544:214-217(2003).
RN [5]
RP INDUCTION.
RX PubMed=12672461; DOI=10.1016/s1357-2725(02)00341-2;
RA Wray C.J., Mammen J.M.V., Hershko D.D., Hasselgren P.-O.;
RT "Sepsis upregulates the gene expression of multiple ubiquitin ligases in
RT skeletal muscle.";
RL Int. J. Biochem. Cell Biol. 35:698-705(2003).
RN [6]
RP INDUCTION.
RX PubMed=14718385; DOI=10.1096/fj.03-0610com;
RA Lecker S.H., Jagoe R.T., Gilbert A., Gomes M., Baracos V., Bailey J.,
RA Price S.R., Mitch W.E., Goldberg A.L.;
RT "Multiple types of skeletal muscle atrophy involve a common program of
RT changes in gene expression.";
RL FASEB J. 18:39-51(2004).
RN [7]
RP FUNCTION.
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 prevents
RT cardiomyocyte hypertrophy.";
RL J. Cell Biol. 167:1147-1159(2004).
RN [8]
RP INDUCTION.
RX PubMed=15827064; DOI=10.1152/ajpendo.00591.2004;
RA Hong-Brown L.Q., Pruznak A.M., Frost R.A., Vary T.C., Lang C.H.;
RT "Indinavir alters regulators of protein anabolism and catabolism in
RT skeletal muscle.";
RL Am. J. Physiol. 289:E382-E390(2005).
RN [9]
RP INDUCTION.
RX PubMed=15963672; DOI=10.1016/j.exger.2005.04.005;
RA DeRuisseau K.C., Kavazis A.N., Powers S.K.;
RT "Selective downregulation of ubiquitin conjugation cascade mRNA occurs in
RT the senescent rat soleus muscle.";
RL Exp. Gerontol. 40:526-531(2005).
CC -!- FUNCTION: E3 ubiquitin ligase. Mediates the ubiquitination and
CC subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates
CC the proteasomal degradation of muscle proteins under amino acid
CC starvation, where muscle protein is catabolized to provide other organs
CC with amino acids. Inhibits de novo skeletal muscle protein synthesis
CC under amino acid starvation. Regulates proteasomal degradation of
CC cardiac troponin I/TNNI3 and probably of other sarcomeric-associated
CC proteins. May play a role in striated muscle atrophy and hypertrophy by
CC regulating an anti-hypertrophic PKC-mediated signaling pathway. May
CC regulate the organization of myofibrils through TTN in muscle cells.
CC {ECO:0000269|PubMed:11679633, ECO:0000269|PubMed:15596539}.
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 -!- SUBUNIT: Homodimer. Homooligomer and heterooligomer. Interacts with
CC SUMO2, titin/TTN and GMEB1. Interacts with TRIM54 and probably with
CC TRIM55 and TNNI3. Forms a ternary complex with RACK1 and PRKCE.
CC Interacts with CKM (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasm, myofibril, sarcomere, M line {ECO:0000250}. Cytoplasm,
CC myofibril, sarcomere, Z line {ECO:0000269|PubMed:11927605}.
CC Note=Colocalizes with TNNI3 in myocytes. Localizes to the M- and Z-
CC lines in skeletal muscle (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Muscle specific. Selectively expressed in heart and
CC skeletal muscle. {ECO:0000269|PubMed:11679633}.
CC -!- INDUCTION: By interleukin-1, dexamethasone, lipolysaccharide and
CC indinavir. Up-regulated upon muscle denervation, immobilization and
CC unweighting and more generally upon muscle atrophy. Up-regulated upon
CC sepsis. Down-regulated upon aging. {ECO:0000269|PubMed:11679633,
CC ECO:0000269|PubMed:12672461, ECO:0000269|PubMed:12782319,
CC ECO:0000269|PubMed:14718385, ECO:0000269|PubMed:15827064,
CC ECO:0000269|PubMed:15963672}.
CC -!- DOMAIN: The RING-type zinc finger mediates interaction with SUMO2 and
CC localization to the nucleus. Also required for the E3 ubiquitin ligase
CC activity (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The B box-type zinc finger mediates homodimerization.
CC {ECO:0000250}.
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DR EMBL; AY059627; AAL16405.1; -; mRNA.
DR EMBL; BC061824; AAH61824.1; -; mRNA.
DR RefSeq; NP_543179.1; NM_080903.1.
DR AlphaFoldDB; Q91Z63; -.
DR SMR; Q91Z63; -.
DR BioGRID; 250873; 8.
DR IntAct; Q91Z63; 1.
DR STRING; 10116.ENSRNOP00000058869; -.
DR PaxDb; Q91Z63; -.
DR DNASU; 140939; -.
DR Ensembl; ENSRNOT00000067524; ENSRNOP00000058869; ENSRNOG00000016543.
DR GeneID; 140939; -.
DR KEGG; rno:140939; -.
DR UCSC; RGD:619964; rat.
DR CTD; 84676; -.
DR RGD; 619964; Trim63.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000156529; -.
DR HOGENOM; CLU_013137_5_1_1; -.
DR InParanoid; Q91Z63; -.
DR OMA; EASKGCH; -.
DR OrthoDB; 824972at2759; -.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q91Z63; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000016543; Expressed in skeletal muscle tissue and 16 other tissues.
DR Genevisible; Q91Z63; RN.
DR GO; GO:0043292; C:contractile fiber; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; NAS:BHF-UCL.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0031432; F:titin binding; ISO:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; ISO:RGD.
DR GO; GO:0006936; P:muscle contraction; IDA:MGI.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IMP:BHF-UCL.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0006513; P:protein monoubiquitination; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; ISO:RGD.
DR GO; GO:0014878; P:response to electrical stimulus involved in regulation of muscle adaptation; IDA:UniProtKB.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
DR GO; GO:0014732; P:skeletal muscle atrophy; IEP:RGD.
DR CDD; cd16759; RING-HC_MuRF1; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR042667; TRIM63_RING-HC.
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; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Metal-binding; Muscle protein; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..351
FT /note="E3 ubiquitin-protein ligase TRIM63"
FT /id="PRO_0000056292"
FT DOMAIN 267..325
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT ZN_FING 23..79
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 117..159
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 74..218
FT /note="Interaction with TTN"
FT /evidence="ECO:0000250"
FT REGION 326..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 189..269
FT /evidence="ECO:0000255"
FT COMPBIAS 327..344
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 351 AA; 39723 MW; BF906A21340C4D97 CRC64;
MDYKSGLIPD GNAMENLEKQ LICPICLEMF TKPVVILPCQ HNLCRKCAND IFQAANPYWT
NRGGSVSMSG GRFRCPSCRH EVIMDRHGVY GLQRNLLVEN IIDIYKQECS SRPLQKGSHP
MCKEHEDEKI NIYCLTCEVP TCSLCKVFGA HQACEVAPLQ SIFQGQKTEL SNCISMLVAG
NDRVQTIISQ LEDSCRVTKE NSHQVKEELS HKFDALYAIL DEKKSELLQR ITQEQEEKLD
FIEALILQYR EQLEKSTKLV ETAIQSLDEP GGATFLLSAK PLIKSIVEAS KGCQLGKTEQ
GFENMDYFTL NLEHIAEALR AIDFGTDEEE EFTEEEEEED QEEGVSTEGH Q
