TRI26_RAT
ID TRI26_RAT Reviewed; 542 AA.
AC P62603; Q6MFZ0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
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; BX883051; CAE84057.1; -; Genomic_DNA.
DR RefSeq; NP_001011665.1; NM_001011665.2.
DR AlphaFoldDB; P62603; -.
DR SMR; P62603; -.
DR STRING; 10116.ENSRNOP00000001019; -.
DR jPOST; P62603; -.
DR PaxDb; P62603; -.
DR PRIDE; P62603; -.
DR Ensembl; ENSRNOT00000001019; ENSRNOP00000001019; ENSRNOG00000032930.
DR GeneID; 309586; -.
DR KEGG; rno:309586; -.
DR UCSC; RGD:1359126; rat.
DR CTD; 7726; -.
DR RGD; 1359126; Trim26.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158668; -.
DR InParanoid; P62603; -.
DR PRO; PR:P62603; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000032930; Expressed in liver and 18 other tissues.
DR ExpressionAtlas; P62603; baseline and differential.
DR Genevisible; P62603; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:RGD.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0044790; P:suppression of viral release by host; ISO:RGD.
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; 1.
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..542
FT /note="Tripartite motif-containing protein 26"
FT /id="PRO_0000056239"
FT DOMAIN 298..542
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 379..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 197..243
FT /evidence="ECO:0000255"
FT COILED 411..440
FT /evidence="ECO:0000255"
FT COMPBIAS 379..438
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 542 AA; 62631 MW; 88C87B17F9E57BA6 CRC64;
MAVSAPLRSL EEEVTCSICL DYLRDPVTID CGHVFCRSCT SDIRPISGNR PVCPLCKKPF
KKENIRPVWQ LASLVENIER LKVDNGKQPG ELAREPQDMK LCERHQEKLH YYCEDDGKLL
CVMCRESREH RPHTAVLVEK AALPHREKIL NHLNTLRRDR DKIQGFQAKG EADILAALTK
LQEQRQYIVA EFKQGHQFLK KREQHLLDQL ATLEQLLTEG REKFKTRGVS ELDRLTLVIS
ELEGKARQPA AELMQLSDRL SCLSLRYPRK KFWIGKAIPH MVKRKAGEFS DKLLSLQRGL
RQFQGKLLRD LEYKTVSVTL DPQSASGYLQ LSEDWKCITY TGQYQSDCLL PQQFDCEPGV
LGSKGFTWGK VYWEVELERE GWSEDEEEGE EEEEGEEEEE DEEPGYGDRY EDWETDEEDE
SLGEEEEEEE EEEEEVQESC MVGVAKDSVK RKGNLSLRPE DGVWALRLSP SGIWANTSPE
AQLFPVLRPR RVGIALDYEG GTVTFTNAES QELIYTFTTT FTRRLVPFLW LKWPEARLLL
RP
