TRI54_MOUSE
ID TRI54_MOUSE Reviewed; 366 AA.
AC Q9ERP3;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Tripartite motif-containing protein 54;
DE AltName: Full=Muscle-specific RING finger protein;
DE Short=MuRF;
DE AltName: Full=Muscle-specific RING finger protein 3;
DE Short=MuRF-3;
DE Short=MuRF3;
DE AltName: Full=RING finger protein 30;
GN Name=Trim54; Synonyms=Murf, Rnf30;
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 [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, OLIGOMERIZATION, INTERACTION WITH MICROTUBULES, AND
RP FUNCTION.
RC TISSUE=Heart muscle;
RX PubMed=10953002; DOI=10.1083/jcb.150.4.771;
RA Spencer J.A., Eliazer S., Ilaria R.L. Jr., Richardson J.A., Olson E.N.;
RT "Regulation of microtubule dynamics and myogenic differentiation by MURF, a
RT striated muscle RING-finger protein.";
RL J. Cell Biol. 150:771-784(2000).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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: May bind and stabilize microtubules during myotubes
CC formation. {ECO:0000269|PubMed:10953002}.
CC -!- SUBUNIT: Homooligomer and heterooligomer. Interacts with TRIM63 and
CC probably with TRIM55 (By similarity). Interacts with tubulin.
CC {ECO:0000250, ECO:0000269|PubMed:10953002}.
CC -!- INTERACTION:
CC Q9ERP3; Q14192: FHL2; Xeno; NbExp=2; IntAct=EBI-15626796, EBI-701903;
CC Q9ERP3; Q14315-1: FLNC; Xeno; NbExp=2; IntAct=EBI-15626796, EBI-15532913;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10953002}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:10953002}. Note=Associates with microtubules.
CC Localizes to the Z-lines in skeletal muscles.
CC -!- TISSUE SPECIFICITY: Selectively expressed in heart and skeletal muscle
CC (at protein level). Also detected in lung and brain at much lower
CC level. {ECO:0000269|PubMed:10953002}.
CC -!- DEVELOPMENTAL STAGE: At 8.5 dpc expressed in the developing cardiac
CC region. At 10.5 dpc expression is restricted to the cardiac region and
CC myotome of the somites. Pre-natal expression is muscle-specific.
CC {ECO:0000269|PubMed:10953002}.
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DR EMBL; AF294790; AAG03076.1; -; mRNA.
DR CCDS; CCDS19173.1; -.
DR RefSeq; NP_067422.1; NM_021447.2.
DR AlphaFoldDB; Q9ERP3; -.
DR SMR; Q9ERP3; -.
DR BioGRID; 208426; 3.
DR DIP; DIP-60890N; -.
DR IntAct; Q9ERP3; 2.
DR STRING; 10090.ENSMUSP00000013771; -.
DR iPTMnet; Q9ERP3; -.
DR PhosphoSitePlus; Q9ERP3; -.
DR MaxQB; Q9ERP3; -.
DR PaxDb; Q9ERP3; -.
DR PRIDE; Q9ERP3; -.
DR ProteomicsDB; 298223; -.
DR Antibodypedia; 13583; 381 antibodies from 32 providers.
DR DNASU; 58522; -.
DR Ensembl; ENSMUST00000013771; ENSMUSP00000013771; ENSMUSG00000062077.
DR GeneID; 58522; -.
DR KEGG; mmu:58522; -.
DR UCSC; uc008wxd.2; mouse.
DR CTD; 57159; -.
DR MGI; MGI:1889623; Trim54.
DR VEuPathDB; HostDB:ENSMUSG00000062077; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154004; -.
DR InParanoid; Q9ERP3; -.
DR OMA; DAHSMDS; -.
DR OrthoDB; 824972at2759; -.
DR PhylomeDB; Q9ERP3; -.
DR TreeFam; TF331669; -.
DR BioGRID-ORCS; 58522; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q9ERP3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9ERP3; protein.
DR Bgee; ENSMUSG00000062077; Expressed in hindlimb stylopod muscle and 71 other tissues.
DR ExpressionAtlas; Q9ERP3; baseline and differential.
DR Genevisible; Q9ERP3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd16761; RING-HC_MuRF3; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR033492; TRIM54/TRIM55.
DR InterPro; IPR042752; TRIM54_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 PANTHER; PTHR24103:SF596; PTHR24103:SF596; 1.
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 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Metal-binding; Microtubule; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..366
FT /note="Tripartite motif-containing protein 54"
FT /id="PRO_0000056283"
FT DOMAIN 271..329
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT ZN_FING 26..82
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 121..163
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 168..211
FT /note="Mediates microtubule-binding and
FT homooligomerization"
FT REGION 328..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 194..258
FT /evidence="ECO:0000255"
FT COMPBIAS 332..348
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 366 AA; 41131 MW; 6CD3429162D5BEFA CRC64;
MNFTVGFKPL LGDAHNMDNL EKQLICPICL EMFSKPVVIL PCQHNLCRKC ANDVFQASNP
LWQSRGSTTV SSGGRFRCPS CRHEVVLDRH GVYGLQRNLL VENIIDIYKQ ESSRPLHAKA
EQHLMCEEHE DEKINIYCLS CEVPTCSLCK VFGAHKDCEV APLPTIYKRQ KSELSDGIAM
LVAGNDRVQA VITQMEEVCQ TIEDNSRRQK QLLNQRFETL CAVLEERKGE LLQALAREQE
EKLQRVRGLI RQYGDHLEGS SKLVESAIQS MEEPQMALYL QQAKELINKV GAMSKVELAG
RPEPGYESME QFSVSVEHVA EMLRTIDFQP GAAGDEEDDD MALDGEEGNA GLEEERLDVP
EGSGLH
