ID F6YCB8_CALJA Unreviewed; 401 AA.
AC F6YCB8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Tripartite motif-containing protein 54 {ECO:0000256|ARBA:ARBA00014725};
GN Name=TRIM54 {ECO:0000313|Ensembl:ENSCJAP00000001903.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000001903.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000001903.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000001903.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: May bind and stabilize microtubules during myotubes
CC formation. {ECO:0000256|ARBA:ARBA00003888}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000256|ARBA:ARBA00004216}.
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DR AlphaFoldDB; F6YCB8; -.
DR STRING; 9483.ENSCJAP00000001903; -.
DR Ensembl; ENSCJAT00000002017.4; ENSCJAP00000001903.3; ENSCJAG00000001102.5.
DR GeneTree; ENSGT00940000154004; -.
DR HOGENOM; CLU_1197176_0_0_1; -.
DR InParanoid; F6YCB8; -.
DR OMA; MEDICRT; -.
DR Proteomes; UP000008225; Chromosome 14.
DR Bgee; ENSCJAG00000001102; Expressed in heart and 4 other cell types or tissues.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl.
DR CDD; cd19833; Bbox2_MuRF3_C-II; 1.
DR CDD; cd16761; RING-HC_MuRF3; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR033492; Trim54_Bbox2_Zfn.
DR InterPro; IPR042752; TRIM54_RING-HC.
DR InterPro; IPR027370; Znf-RING_euk.
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; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF596; TRIPARTITE MOTIF-CONTAINING PROTEIN 54; 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 SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 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 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 26..82
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 121..163
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 312..370
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT REGION 368..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 262..293
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 373..388
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 44747 MW; 5A9519A3CCFF3DD6 CRC64;
MNFTVGFKPL LGDAHSMDNL EKQLICPICL EMFSKPVVIL PCQHNLCRKC ANDVFQASNP
LWQSRGSTTV SSGGRFRCPS CRHEVVLDRH GVYGLQRNLL VENIIDIYKQ ESSRPLHSKA
EQHLMCEEHE EEKINIYCLS CEVPTCSLCK VFGAHKDCEV APLPTIYKRQ KRELTLLPRL
EGSGTHMTYC SLDLLDSSDP PILASQNASI TGSELSDGIA MLVAGNDRVQ AVITQMEEVC
QTIEDNSRRQ KQLLNQKFES LCAVLEERKG ELLQALAREQ EEKLQRVRGL IRQYGDHLEA
SSKLVESAIQ SMEEPQMALY LQQAKELINK VGAMSKVELA GRPEPGYESM EPFTVSVEHV
AEMLRTIDFQ PGTSGEEEDE EVALDGDEGT AGPEEGRPDG P
//
