TRI54_PONAB
ID TRI54_PONAB Reviewed; 358 AA.
AC Q5REJ9;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Tripartite motif-containing protein 54;
GN Name=TRIM54;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR857526; CAH89808.1; -; mRNA.
DR RefSeq; NP_001124836.1; NM_001131364.1.
DR AlphaFoldDB; Q5REJ9; -.
DR SMR; Q5REJ9; -.
DR STRING; 9601.ENSPPYP00000014021; -.
DR Ensembl; ENSPPYT00000062312; ENSPPYP00000026265; ENSPPYG00000031097.
DR GeneID; 100171694; -.
DR KEGG; pon:100171694; -.
DR CTD; 57159; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154004; -.
DR InParanoid; Q5REJ9; -.
DR Proteomes; UP000001595; Chromosome 2A.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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..358
FT /note="Tripartite motif-containing protein 54"
FT /id="PRO_0000056284"
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..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 194..258
FT /evidence="ECO:0000255"
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 358 AA; 40263 MW; 801A5DB8D12130C3 CRC64;
MNFTVGFKPL LGDAHSMDNL EKQLICPICL EMFSKPVVIL PCQHNLCRKC ANDVFQASNP
LWQSRGSTTV SSGGRFRCPS CRHEVVLDRH GVYGLQRNLL VENIIDIYKQ ESSRPLHSKA
EQHLMCEEHE EEKINIYCLS CEVPTCSLCK VFGAHKDCEV APLPTIYKRQ KSELSDGIAM
LVAGNDRVQA VITQMEEVCQ TIEDNSRRQK QLLNQRFESL CAVLEERKGE LLQALAREQE
EKLQRVRGLI RQYGDHLEAS SKLVETAIQS MEEPQMALYL QQAKELINKV GAMSKVELAG
RPEPGYESME QFTVSVEHVA EMLRTIDFQP GASGEEEEVA PDGDEGSAGQ EEERPDGP