ID G0WLG4_PIG Unreviewed; 364 AA.
AC G0WLG4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Tripartite motif-containing protein 54 {ECO:0000256|ARBA:ARBA00014725};
GN Name=murf3 {ECO:0000313|EMBL:ADM64314.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:ADM64314.1};
RN [1] {ECO:0000313|EMBL:ADM64314.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21153918; DOI=10.1007/s11033-010-0659-0;
RA Shen H., Zhao S.H., Cao J.H., Li X.Y., Fan B.;
RT "Porcine MuRF2 and MuRF3: molecular cloning, expression and association
RT analysis with muscle production traits.";
RL Mol. Biol. Rep. 38:5115-5123(2011).
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 EMBL; HM449001; ADM64314.1; -; mRNA.
DR RefSeq; NP_001231288.1; NM_001244359.1.
DR AlphaFoldDB; G0WLG4; -.
DR GeneID; 100689265; -.
DR KEGG; ssc:100689265; -.
DR CTD; 57159; -.
DR OrthoDB; 5383069at2759; -.
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 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 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
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 271..329
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT REGION 326..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 364 AA; 40949 MW; 65DCFD68692A22B9 CRC64;
MNFTVGFKPL LGDAHSMDNL EKQLICPICL EMFSKPVVIL PCHHNLCRKC ANDVFQASNP
LWQSRGSTTV SSGGRFRCPS CRHEVVLDRH GVYGLQRNLL VENIIDIYKQ ESSRPLHTKA
EQHLMCEEHE DEKINIYCLS CEVPTCSLCK VFGAHKDCEV APLPTIYKRQ KSELSDGIAM
LVAGNDRVQA VITQMEEVCQ TIEDNSRRQK QLLNQRFEAL CAVLEERKGE LLQALAKVQE
EKLQRVRGLI RQYGDHLEAS SKLVESAIQS MEEPQMALYL QQAKELINKV GTMSKVELAG
RPEPGYESME QFRVSVEHVA EMLRTIDFQP GASGEEEDEE VALDGEEGSA GPEEERPDGP
EGLH
//
