TRI56_BOVIN
ID TRI56_BOVIN Reviewed; 732 AA.
AC E1BD59;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM56 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q80VI1};
DE AltName: Full=Tripartite motif-containing protein 56;
GN Name=TRIM56 {ECO:0000303|PubMed:21289118};
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 GENOMIC DNA].
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP FUNCTION, AND INDUCTION BY IFN-ALPHA AND VIRAL INFECTION.
RX PubMed=21289118; DOI=10.1128/jvi.02546-10;
RA Wang J., Liu B., Wang N., Lee Y.M., Liu C., Li K.;
RT "TRIM56 is a virus- and interferon-inducible E3 ubiquitin ligase that
RT restricts pestivirus infection.";
RL J. Virol. 85:3733-3745(2011).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that plays a key role in innate
CC antiviral immunity by mediating ubiquitination of CGAS and STING1
CC (PubMed:21289118). In response to pathogen- and host-derived double-
CC stranded DNA (dsDNA), targets STING1 to 'Lys-63'-linked ubiquitination,
CC thereby promoting its homodimerization, a step required for the
CC production of type I interferon IFN-beta (By similarity). Also mediate
CC monoubiquitination of CGAS, thereby promoting CGAS oligomerization and
CC subsequent activation (By similarity). Independently of its E3
CC ubiquitin ligase activity, positive regulator of TLR3 signaling.
CC Potentiates extracellular double stranded RNA (dsRNA)-induced
CC expression of IFNB1 and interferon-stimulated genes ISG15, IFIT1/ISG56,
CC CXCL10, OASL and CCL5/RANTES (By similarity). Restricts bovine viral
CC diarrhea virus (BVDV) replication (PubMed:21289118).
CC {ECO:0000250|UniProtKB:Q80VI1, ECO:0000250|UniProtKB:Q9BRZ2,
CC ECO:0000269|PubMed:21289118}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9BRZ2};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q80VI1}.
CC -!- SUBUNIT: Interacts with STING1 (By similarity). Interacts with TICAM1
CC (By similarity). {ECO:0000250|UniProtKB:Q80VI1,
CC ECO:0000250|UniProtKB:Q9BRZ2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q80VI1}.
CC -!- INDUCTION: Up-regulated by IFN-alpha. Up-regulated in response to viral
CC infection, including Sendai virus and bovine viral diarrhea virus.
CC {ECO:0000269|PubMed:21289118}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AAFC03118057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BD59; -.
DR SMR; E1BD59; -.
DR STRING; 9913.ENSBTAP00000015969; -.
DR PaxDb; E1BD59; -.
DR PRIDE; E1BD59; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; E1BD59; -.
DR OrthoDB; 489543at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0034340; P:response to type I interferon; ISS:UniProtKB.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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 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; 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 Antiviral defense; Coiled coil; Cytoplasm; Immunity; Innate immunity;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..732
FT /note="E3 ubiquitin-protein ligase TRIM56"
FT /id="PRO_0000404586"
FT ZN_FING 21..60
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 164..205
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 374..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 211..286
FT /evidence="ECO:0000255"
FT COMPBIAS 386..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 402
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRZ2"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRZ2"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRZ2"
SQ SEQUENCE 732 AA; 79152 MW; F10AC1FA60674B40 CRC64;
MVSQGSSPSL LEALSSDFLA CKICLEQLRV PKTLPCLHTY CQDCLAQLAE GSRLRCPECR
ESVPVPPAGV AAFKTNFFVN GLLDLVKARA GGDLRAGKPA CALCPLMGGA SAGGPATARC
LDCADDLCQA CADGHRCTRQ THSHRVVDLV GYRAGWYDEE ARERQAAQCP QHPGEALRFL
CQPCSQLLCR ECRLDPHLDH PCLPLAEAVR ARRPGLEELL AGVDNNLAEL EATRLAEKEA
LARLREQAAK VVTQVEEASE RVLRALLAQK QEVLGQLRAH VEAAEEGARE RLGELEGQEQ
VAREAAAFAR RVLSLGREAE ILSLEGAIAQ RLRQLQGCPW VPGPAPCQLP QLELYPGLLD
KNCHLLRLSF EEQLPQKDSG KDGARSQGGD ATQPQSRDGV QTPNQEDGAK TPKESRAQTP
QEDGGTQARV GSRSNKKRKF KGRLKSVSRE PSPAPGPNLE GSGLLPRPIF FCSFPTRMPG
DKRAPRITGL CPFGSREILV ADEQNRALKR FSLNGDYRGA VPVPEGCSPC SVAALQDTVA
FSAAARLYLI NHNGEVQWRR ALSLCQASHA VAAMPSGDRV AVSVSGHVEV YNMEGSLATR
FIPGGKANRG LRALVFLTTS PQGHFVGSDW QQNSLVVCDG LGQVVGEYRG PGLHGCQPGS
VSVDKKGYIF LTLREVNKVV ILDPKGSLLG DFLTAYHGLE KPRVTTMVDG RYLVVSLSNG
TIHVFRVRPL DS
