ID W5MBE0_LEPOC Unreviewed; 400 AA.
AC W5MBE0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Tripartite motif-containing protein 54 {ECO:0000256|ARBA:ARBA00014725};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000005699.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000005699.1}
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, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm, myofibril, sarcomere, Z
CC line {ECO:0000256|ARBA:ARBA00004216}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHAT01009593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01009594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MBE0; -.
DR STRING; 7918.ENSLOCP00000005699; -.
DR Ensembl; ENSLOCT00000005707.1; ENSLOCP00000005699.1; ENSLOCG00000004733.1.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000156529; -.
DR InParanoid; W5MBE0; -.
DR OMA; NQLEESC; -.
DR Proteomes; UP000018468; Linkage group LG6.
DR Bgee; ENSLOCG00000004733; Expressed in larva and 7 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd19833; Bbox2_MuRF3_C-II; 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; 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; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR PANTHER; PTHR24099:SF32; TRIPARTITE MOTIF CONTAINING 55; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 23..77
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 116..158
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 309..367
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT REGION 368..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 223..279
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 370..393
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 45893 MW; 376879F5294A9551 CRC64;
MDFQSSIIQE SNRMENLEKQ LICPICLEIF SKPVVILPCQ HNLCRKCAND VFQAANPYWT
SRGTNISGGR FRCPSCRHEV VLDRHGVYGL QRNLLVENII DIYKQESSSP RPLKKVDQPM
CLEHEDEKIN IYCVTCQVPT CSMCKVFGAH KNCEVSPLEN VYQHQKRHGF SYQSILESGI
NRKYVVLSVL HASCSDNAVP SSHCILPWQT ELSDGIATLV AGNDRVQAIM NQLEDTCRTI
EENSQRQKQS LSEHFDMLYA ILEERKGEML LKISQEQEEK MSYVRSLIQQ YKEQLDGSSK
LVETAIHSME EPTVATFLMN AKQLLKDMTE ASKQTHIQRT EPGFENMDHF TLNIEHIEAM
LRTMDFGTEA EHDEEYDEEE QEEEEEEGGE EPSEDQTTGI
//
