TRI26_PIG
ID TRI26_PIG Reviewed; 545 AA.
AC O77666;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Tripartite motif-containing protein 26;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q12899};
DE AltName: Full=Zinc finger protein 173;
GN Name=TRIM26; Synonyms=ZNF173;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Large white;
RX PubMed=11685460; DOI=10.1007/s002510100348;
RA Renard C., Vaiman M., Chiannilkulchai N., Cattolico L., Robert C.,
RA Chardon P.;
RT "Sequence of the pig major histocompatibility region containing the
RT classical class I genes.";
RL Immunogenetics 53:490-500(2001).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which regulates the IFN-beta
CC production and antiviral response downstream of various DNA-encoded
CC pattern-recognition receptors (PRRs). Promotes nuclear IRF3
CC ubiquitination and proteasomal degradation. Bridges together TBK1 and
CC NEMO during the innate response to viral infection leading to the
CC activation of TBK1. {ECO:0000250|UniProtKB:Q12899}.
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:Q12899};
CC -!- SUBUNIT: Interacts with TBK1; this interaction bridges together TBK1
CC and NEMO in order to activate TBK1. Interacts with INCA1.
CC {ECO:0000250|UniProtKB:Q12899}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12899}. Nucleus
CC {ECO:0000250|UniProtKB:Q12899}. Note=Viral infection mediates TRIM26
CC nuclear translocation. {ECO:0000250|UniProtKB:Q12899}.
CC -!- PTM: Autoubiquitinates upon viral infection. In turn, autoubiquitinated
CC TRIM26 recruits NEMO and bridges TBK1-NEMO interaction.
CC {ECO:0000250|UniProtKB:Q12899}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AJ251829; CAB63934.1; -; Genomic_DNA.
DR RefSeq; NP_001116681.1; NM_001123209.1.
DR AlphaFoldDB; O77666; -.
DR SMR; O77666; -.
DR STRING; 9823.ENSSSCP00000001310; -.
DR PaxDb; O77666; -.
DR PeptideAtlas; O77666; -.
DR PRIDE; O77666; -.
DR GeneID; 100144460; -.
DR KEGG; ssc:100144460; -.
DR CTD; 7726; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; O77666; -.
DR OrthoDB; 542578at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR Gene3D; 2.60.120.920; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Immunity; Innate immunity; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..545
FT /note="Tripartite motif-containing protein 26"
FT /id="PRO_0000056238"
FT DOMAIN 295..545
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 97..138
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 376..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 172..226
FT /evidence="ECO:0000255"
FT COMPBIAS 376..402
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..440
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 545 AA; 62778 MW; AF4E233309232C7E CRC64;
MATSAPLRSL EEEVTCSICL DYLRDPVTID CGHVFCRSCT TDIHPVSGGR PVCPLCKKPF
TKENIRPVWQ LASLVENIER LKVDTGRQPG EVAREQQDTR LCERHQEKLH YYCEDDGKLL
CVMCRESREH RPHMAVLVEK AAQPHREKIL NHLSTLRRDR DKIQGFQAKG EADILAELKK
LQDQRQRILA AFEQGHQFLW EREQHLLDQL AKLEQEVTEG REKYKTRGDG ELARLAQVIS
ELEGKAQQPA AELMQDTRDF LTRYPRKKFW IGKPIARVVK KRTGEFSDKL LSLQRGLREF
QGKLLRDLEY KTVSVTLDPQ SASGYLQLSE DWKCVTYSGL YQSSYLHPQQ FECEPGVLGS
KGFTWGKVYW EVEVEREGWS EDEEEGDEEE EGEEEEEEEE AGYGAGFGYG DGYDDWGTDE
DEESLGDEEE EEEEEEEEVL ESCMVGVARD SVKRKGDLSL RPEDGVWALR LSSSGIWANT
RPEAELFPAQ RPRRVGIALD YEGGTVTFTN AESQELIYTF KATFTRRLLP FLWLRWPGTR
LLLRP
