TRI26_PANTR
ID TRI26_PANTR Reviewed; 539 AA.
AC Q7YR34; Q1XHU4;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12799463; DOI=10.1073/pnas.1230533100;
RA Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A.,
RA Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y.,
RA Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T., Meyer A.,
RA Ikeo K., Gojobori T., Bahram S., Inoko H.;
RT "Comparative sequencing of human and chimpanzee MHC class I regions unveils
RT insertions/deletions as the major path to genomic divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
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; BA000041; BAC78183.1; -; Genomic_DNA.
DR EMBL; AB210203; BAE92825.1; -; Genomic_DNA.
DR EMBL; AB210204; BAE92826.1; -; Genomic_DNA.
DR RefSeq; NP_001037841.1; NM_001044376.1.
DR RefSeq; XP_009449080.1; XM_009450805.2.
DR RefSeq; XP_009449081.1; XM_009450806.2.
DR RefSeq; XP_009449082.1; XM_009450807.2.
DR RefSeq; XP_009449085.1; XM_009450810.2.
DR AlphaFoldDB; Q7YR34; -.
DR SMR; Q7YR34; -.
DR STRING; 9598.ENSPTRP00000039843; -.
DR PaxDb; Q7YR34; -.
DR Ensembl; ENSPTRT00000048788; ENSPTRP00000039843; ENSPTRG00000024332.
DR GeneID; 462536; -.
DR KEGG; ptr:462536; -.
DR CTD; 7726; -.
DR VGNC; VGNC:12729; TRIM26.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158668; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q7YR34; -.
DR OMA; PFFWLNW; -.
DR OrthoDB; 542578at2759; -.
DR TreeFam; TF342569; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000024332; Expressed in lung and 21 other tissues.
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:0046597; P:negative regulation of viral entry into host cell; IEA:Ensembl.
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 GO; GO:0044790; P:suppression of viral release by host; IEA:Ensembl.
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..539
FT /note="Tripartite motif-containing protein 26"
FT /id="PRO_0000056237"
FT DOMAIN 295..539
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..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 188..227
FT /evidence="ECO:0000255"
FT COMPBIAS 376..435
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 539 AA; 62198 MW; 707B34C54F348852 CRC64;
MATSAPLRSL EEEVTCSICL DYLRDPVTID CGHVFCRSCT TDVRPISGSR PVCPLCKKPF
KKENIRPVWQ LASLVENIER LKVDKGRQPG EVTREQQDAK LCERHREKLH YYCEDDGKLL
CVMCRESREH RPHTAVLMEK AAQPHREKIL NHLSTLRRDR DKIQGFQAKG EADILAALKK
LQDQRQYIVA EFEQGHQFLR EREEHLLEQL AKLEQELTEG REKFKSRGVG ELARLALVIS
ELEGKAQQPA AELMQDTRDF LNRYPRKKFW VGKPIARVVK KKTGEFSDKL LSLQRGLREF
QGKLLRDLEY KTVSVTLDPQ SASGYLQLSE DWKCVTYTSL YKSAYLHPQQ FDCEPGVLGS
KGFTWGKVYW EVEVEREGWS EDEEEGDEEE EGEEEEEEEE AGYGDGYDDW ETDEDEESLG
DEEEEEEEEE EEVLESCMVG VARDSMKRKG DLSLRPEDGV WALRLSSSGI WANTSPEAEL
FPALRPRRVG IALDYEGGTV TFTNAESQEL IYTFTATFTR RLVPFLWLKW PGTRLLLRP
