TRI54_BOVIN
ID TRI54_BOVIN Reviewed; 366 AA.
AC Q58D15; Q29RH5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Tripartite motif-containing protein 54;
GN Name=TRIM54;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; BT021782; AAX46629.1; -; mRNA.
DR EMBL; BC114171; AAI14172.1; -; mRNA.
DR RefSeq; NP_001017951.1; NM_001017951.1.
DR AlphaFoldDB; Q58D15; -.
DR SMR; Q58D15; -.
DR STRING; 9913.ENSBTAP00000024312; -.
DR PaxDb; Q58D15; -.
DR PRIDE; Q58D15; -.
DR Ensembl; ENSBTAT00000024312; ENSBTAP00000024312; ENSBTAG00000018267.
DR GeneID; 535320; -.
DR KEGG; bta:535320; -.
DR CTD; 57159; -.
DR VEuPathDB; HostDB:ENSBTAG00000018267; -.
DR VGNC; VGNC:36340; TRIM54.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000156529; -.
DR HOGENOM; CLU_013137_5_1_1; -.
DR InParanoid; Q58D15; -.
DR OMA; DAHSMDS; -.
DR OrthoDB; 824972at2759; -.
DR TreeFam; TF331669; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000018267; Expressed in laryngeal cartilage and 45 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
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: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..366
FT /note="Tripartite motif-containing protein 54"
FT /id="PRO_0000056281"
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 326..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 185..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; 41337 MW; 9058297044439497 CRC64;
MNFTVGFKPL LGDAHSMDNL EKQLICPICL EMFSKPVVIL PCQHNLCRKC ANDVFQASNP
LWQSRSSTTV SSGGRFRCPS CRHEVVLDRH GVYGLQRNLL VENIIDIYKQ ESSRPLHSKA
EQHLMCEEHE DEKINIYCLS CEVPTCSLCK VFGAHKDCEV APLPTIYKRQ KSELSDGIAM
LVAGNDRVQA VITQMEEVCQ TIEENSRRQK QLLNQRFEGL CAVLEERKGE LLQALAREQE
EKLQRVRGLI RQYGDHLEAS SKLVESAIQS MEEPQMALYL QQAKELINKV GTMSKVELAG
RPEPGYERMD QFTVSVEHVA EMLRTIDFQP GTSGEEEDEE VAVEGEEGNA GPEEERTDGR
ESTGQH
