TRI54_RAT
ID TRI54_RAT Reviewed; 364 AA.
AC Q5XIH6;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Tripartite motif-containing protein 54;
DE AltName: Full=RING finger protein 30;
GN Name=Trim54; Synonyms=Rnf30;
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).
CC -!- FUNCTION: May bind and stabilize microtubules during myotubes
CC formation. {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer and heterooligomer. Interacts with TRIM63 and
CC probably with TRIM55. Interacts with tubulin (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC myofibril, sarcomere, Z line {ECO:0000250}. Note=Associates with
CC microtubules. Localizes to the Z-lines in skeletal muscles (By
CC similarity). {ECO:0000250}.
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DR EMBL; BC083706; AAH83706.1; -; mRNA.
DR RefSeq; NP_001013235.1; NM_001013217.1.
DR AlphaFoldDB; Q5XIH6; -.
DR SMR; Q5XIH6; -.
DR IntAct; Q5XIH6; 1.
DR STRING; 10116.ENSRNOP00000008113; -.
DR PaxDb; Q5XIH6; -.
DR PRIDE; Q5XIH6; -.
DR Ensembl; ENSRNOT00000008113; ENSRNOP00000008113; ENSRNOG00000006146.
DR GeneID; 362708; -.
DR KEGG; rno:362708; -.
DR CTD; 57159; -.
DR RGD; 1306453; Trim54.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154004; -.
DR HOGENOM; CLU_013137_5_1_1; -.
DR InParanoid; Q5XIH6; -.
DR OMA; DAHSMDS; -.
DR OrthoDB; 824972at2759; -.
DR PhylomeDB; Q5XIH6; -.
DR PRO; PR:Q5XIH6; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000006146; Expressed in skeletal muscle tissue and 9 other tissues.
DR Genevisible; Q5XIH6; RN.
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; ISO:RGD.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule 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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISO:RGD.
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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Metal-binding; Microtubule; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..364
FT /note="Tripartite motif-containing protein 54"
FT /id="PRO_0000056285"
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 /evidence="ECO:0000250"
FT REGION 328..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 194..252
FT /evidence="ECO:0000255"
FT COMPBIAS 332..348
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..364
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 364 AA; 41031 MW; 30D0B386B085016C CRC64;
MNFTVGFKPL LGDAHNMDNL EKQLICPICL EMFSKPVVIL PCQHNLCRKC ANDVFQASNP
LWQSRGSTTV SSGGRFRCPS CRHEVVLDRH GVYGLQRNLL VENIIDIYKQ ESSRPLHSKA
EQHLMCEEHE DEKINIYCLS CEVPTCSLCK VFGAHKDCEV APLPTIYKRQ KSELSDGIAM
LVAGNDRVQA VITQMEEVCQ TIEDNSRRQK QLLNQKFETL CAVLEERKGE LLQALARVQE
EKLQRVRSLI RQYGDHLEAS SKLVESAIQS MEEPQMALYL QQAKELINKV GAMSKVELAG
RPEPGYESME QFSVIVEHVA EMLRTIDFQP GASGDEEDDE VTLDGEEGNT GLEEERLDGP
EGLH
