TRI26_MOUSE
ID TRI26_MOUSE Reviewed; 545 AA.
AC Q99PN3; B8JJ55; Q8C9E9; Q8JZT7; Q99PN2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 155.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RA Reymond A., Meroni G.;
RT "Deciphering the function of the tripartite motif containing proteins.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-394.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=Q99PN3-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q99PN3-2; Sequence=VSP_010812, VSP_010813;
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; AF230395; AAG50174.1; -; mRNA.
DR EMBL; AF230396; AAG50175.1; -; mRNA.
DR EMBL; CR956641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466559; EDL23302.1; -; Genomic_DNA.
DR EMBL; BC037110; AAH37110.1; -; mRNA.
DR EMBL; AK042252; BAC31204.1; -; mRNA.
DR CCDS; CCDS37613.1; -. [Q99PN3-1]
DR RefSeq; NP_001020770.2; NM_001025599.3. [Q99PN3-1]
DR RefSeq; NP_001273655.1; NM_001286726.1. [Q99PN3-1]
DR RefSeq; NP_001273656.1; NM_001286727.1. [Q99PN3-1]
DR RefSeq; XP_006524276.1; XM_006524213.3. [Q99PN3-1]
DR AlphaFoldDB; Q99PN3; -.
DR SMR; Q99PN3; -.
DR BioGRID; 204644; 3.
DR STRING; 10090.ENSMUSP00000060103; -.
DR iPTMnet; Q99PN3; -.
DR PhosphoSitePlus; Q99PN3; -.
DR EPD; Q99PN3; -.
DR MaxQB; Q99PN3; -.
DR PaxDb; Q99PN3; -.
DR PRIDE; Q99PN3; -.
DR ProteomicsDB; 298296; -. [Q99PN3-1]
DR ProteomicsDB; 298297; -. [Q99PN3-2]
DR Antibodypedia; 26253; 138 antibodies from 21 providers.
DR DNASU; 22670; -.
DR Ensembl; ENSMUST00000053434; ENSMUSP00000060103; ENSMUSG00000024457. [Q99PN3-1]
DR Ensembl; ENSMUST00000123715; ENSMUSP00000118438; ENSMUSG00000024457. [Q99PN3-2]
DR Ensembl; ENSMUST00000130367; ENSMUSP00000114896; ENSMUSG00000024457. [Q99PN3-1]
DR GeneID; 22670; -.
DR KEGG; mmu:22670; -.
DR UCSC; uc008clh.2; mouse. [Q99PN3-1]
DR CTD; 7726; -.
DR MGI; MGI:1337056; Trim26.
DR VEuPathDB; HostDB:ENSMUSG00000024457; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158668; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q99PN3; -.
DR OMA; PFFWLNW; -.
DR OrthoDB; 542578at2759; -.
DR PhylomeDB; Q99PN3; -.
DR TreeFam; TF342569; -.
DR BioGRID-ORCS; 22670; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Trim26; mouse.
DR PRO; PR:Q99PN3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q99PN3; protein.
DR Bgee; ENSMUSG00000024457; Expressed in humerus cartilage element and 255 other tissues.
DR ExpressionAtlas; Q99PN3; baseline and differential.
DR Genevisible; Q99PN3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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:MGI.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
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:MGI.
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 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Cytoplasm; Immunity; Innate immunity;
KW Metal-binding; Nucleus; Reference proteome; Transferase; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..545
FT /note="Tripartite motif-containing protein 26"
FT /id="PRO_0000056236"
FT DOMAIN 301..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 382..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 197..243
FT /evidence="ECO:0000255"
FT COMPBIAS 382..441
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"
FT VAR_SEQ 319..326
FT /note="VSVTLDPQ -> DFFCPCKC (in isoform Beta)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010812"
FT VAR_SEQ 327..545
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010813"
FT CONFLICT 73
FT /note="S -> N (in Ref. 1; AAG50174/AAG50175)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="T -> A (in Ref. 1; AAG50174/AAG50175)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="G -> E (in Ref. 1; AAG50174)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 62809 MW; 98B6683E337EE217 CRC64;
MAVSAPLRSL EEEVTCSICL DYLRDPVTID CGHVFCRSCT SDIRPISGNR PVCPLCKKPF
KKENIRPVWQ LASLVENIER LKVDNGRQPG ELAREPQDMK LCERHQEKLH YYCEDDGKLL
CVMCRESREH RPHTAVLVEK AALPHREKIL NHLNTLRRDR DKIQGFQAKG EADILAALTK
LQEQRQYIVA EFKQGHQFLK KREQHLLDQL ATLEQLLTEG REKFKTRGVS ELDRLTLVIS
ELEGKARQPA AELMQDVCTT QDTKDFANKY PRKKFWIGKA IPHMVKRKAG EFSDKLLSLQ
RGLRQFQGKL LRDLEYKTVS VTLDPQSASG YLHLSEDWKC VTYTGQYQSD CLLPQQFDCE
PGVLGSKGFT WGKVYWEVEL EREGWSEDEE EGEEEEEGEE EEEDEEVGYG DGYEDWETDE
EDESLGEEEE EEEEEEEEVQ ESCMVGVAKD SVKRKGDLSL RPEDGVWALR LSPSGIWANT
SPEAQLFPVL RPRRVGIALD YEGGTVTFTN AESQELIYTF TTTFTRRLVP FLWLKWPGAR
LLLRP
