TRI55_RAT
ID TRI55_RAT Reviewed; 545 AA.
AC Q5PQN5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Tripartite motif-containing protein 55;
DE AltName: Full=Muscle-specific RING finger protein 2;
DE Short=MuRF-2;
DE Short=MuRF2;
DE AltName: Full=RING finger protein 29;
GN Name=Trim55; Synonyms=Murf2, Rnf29;
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 [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [2]
RP SUBCELLULAR LOCATION.
RC TISSUE=Heart muscle, and Skeletal muscle;
RX PubMed=12414993; DOI=10.1242/jcs.00131;
RA Pizon V., Iakovenko A., van der Ven P.F.M., Kelly R., Fatu C., Fuerst D.O.,
RA Karsenti E., Gautel M.;
RT "Transient association of titin and myosin with microtubules in nascent
RT myofibrils directed by the MURF2 RING-finger protein.";
RL J. Cell Sci. 115:4469-4482(2002).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=15199100; DOI=10.1242/jcs.01158;
RA McElhinny A.S., Perry C.N., Witt C.C., Labeit S., Gregorio C.C.;
RT "Muscle-specific RING finger-2 (MURF-2) is important for microtubule,
RT intermediate filament and sarcomeric M-line maintenance in striated muscle
RT development.";
RL J. Cell Sci. 117:3175-3188(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15802564; DOI=10.1126/science.1110463;
RA Lange S., Xiang F., Yakovenko A., Vihola A., Hackman P., Rostkova E.,
RA Kristensen J., Brandmeier B., Franzen G., Hedberg B., Gunnarsson L.G.,
RA Hughes S.M., Marchand S., Sejersen T., Richard I., Edstroem L., Ehler E.,
RA Udd B., Gautel M.;
RT "The kinase domain of titin controls muscle gene expression and protein
RT turnover.";
RL Science 308:1599-1603(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May regulate gene expression and protein turnover in muscle
CC cells. {ECO:0000269|PubMed:15802564}.
CC -!- SUBUNIT: Homooligomer and heterooligomer (Probable). Interacts with
CC titin/TTN. Interacts with myosins. Interacts with SQSTM1 and NBR1.
CC Probably interacts with TRIM63 and TRIM54 (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nuclear under atrophic
CC conditions and upon mechanical signals. Localizes to the sarcomeric M-
CC band in cardiomyocytes. Colocalizes in part with microtubules.
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DR EMBL; BC087100; AAH87100.1; -; mRNA.
DR RefSeq; NP_001012218.1; NM_001012218.1.
DR AlphaFoldDB; Q5PQN5; -.
DR SMR; Q5PQN5; -.
DR BioGRID; 265529; 1.
DR CORUM; Q5PQN5; -.
DR IntAct; Q5PQN5; 2.
DR STRING; 10116.ENSRNOP00000017125; -.
DR PhosphoSitePlus; Q5PQN5; -.
DR PaxDb; Q5PQN5; -.
DR PRIDE; Q5PQN5; -.
DR GeneID; 365751; -.
DR KEGG; rno:365751; -.
DR UCSC; RGD:1306943; rat.
DR CTD; 84675; -.
DR RGD; 1306943; Trim55.
DR VEuPathDB; HostDB:ENSRNOG00000012723; -.
DR eggNOG; KOG2177; Eukaryota.
DR HOGENOM; CLU_013137_5_3_1; -.
DR InParanoid; Q5PQN5; -.
DR OMA; CDIHEDE; -.
DR OrthoDB; 824972at2759; -.
DR PhylomeDB; Q5PQN5; -.
DR TreeFam; TF331669; -.
DR PRO; PR:Q5PQN5; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000012723; Expressed in heart and 9 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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:0050904; P:diapedesis; ISO:RGD.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISO:RGD.
DR GO; GO:1905517; P:macrophage migration; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR033492; TRIM54/TRIM55.
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; PTHR25462:SF257; PTHR25462:SF257; 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; Metal-binding; Muscle protein; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..545
FT /note="Tripartite motif-containing protein 55"
FT /id="PRO_0000056287"
FT DOMAIN 269..327
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 119..161
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 324..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 219..258
FT /evidence="ECO:0000255"
FT COMPBIAS 327..353
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 545 AA; 59980 MW; 2B884C66708CCB36 CRC64;
MSTSLNYKSF SKEQQTMDNL EKQLICPICL EMFTKPVVIL PCQHNLCRKC ASDIFQASNP
YLPTRGGTTV ASGGRFRCPS CRHEVVLDRH GVYGLQRNLL VENIIDIYKQ ESTRPEKKLD
QPMCEEHEEE RINIYCLNCE VPTCSLCKVF GAHKDCQVAP LTHVFQRQKS ELSDGIAVLV
GSNDRVQGVI SQLEDTCKTI EECCRKQKQD LCEKFDHLYS ILEERKTEMT QAITRTQEEK
LEHVRTLIRK YSDHLENVSK LVESGIQFMD EPEMAVFLQN AKTLLQKITE ASKAFQMEKI
EQGYEIMNNF TVNLNREEKI IREIDFSREE EDEDDEGEVD EEGEGEDAVE VEEAENVQVA
SSGEEETLEK AAEPSELAAE IQAASGPLLA SSPDSVSSLP PAADVLVTQG EVVPTDSQQT
TQSETSGPSA AETADPLFYP SWYKGQSRKM ISNPPHTPGG EGLSQIGPSA AEDSSVQSAE
VAEAAANEQA AVSGKESSST AATSQIGFEA SSPQGQAAAL GSGGGADSEP ARHVFSFSWL
NSLNE
