TRI14_MOUSE
ID TRI14_MOUSE Reviewed; 440 AA.
AC Q8BVW3; B1AVH3; Q6A0C3; Q762I6; Q9D3G8;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Tripartite motif-containing protein 14;
DE AltName: Full=PU.1-binding protein;
GN Name=Trim14; Synonyms=Kiaa0129, Pub;
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] (ISOFORM 1), FUNCTION, INTERACTION WITH SPI1,
RP MUTAGENESIS OF HIS-51, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=14592421; DOI=10.1016/j.bbrc.2003.09.212;
RA Hirose S., Nishizumi H., Sakano H.;
RT "Pub, a novel PU.1 binding protein, regulates the transcriptional activity
RT of PU.1.";
RL Biochem. Biophys. Res. Commun. 311:351-360(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Skin;
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).
RN [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27666593; DOI=10.1016/j.molcel.2016.08.025;
RA Chen M., Meng Q., Qin Y., Liang P., Tan P., He L., Zhou Y., Chen Y.,
RA Huang J., Wang R.F., Cui J.;
RT "TRIM14 inhibits cGAS degradation mediated by selective autophagy receptor
RT p62 to promote innate immune responses.";
RL Mol. Cell 64:105-119(2016).
CC -!- FUNCTION: Plays a role in the innate immune defense against viruses.
CC Facilitates the type I IFN response by interacting with MAVS at the
CC outer mitochondria membrane and thereby recruiting NF-kappa-B essential
CC modulator IKBKG/NEMO to the MAVS signalosome, leading to the activation
CC of both the IFN regulatory factor 3/IRF3 and NF-kappa-B pathways.
CC Positively regulates the CGAS-induced type I interferon signaling
CC pathway by stabilizing CGAS and inhibiting its autophagic degradation
CC (PubMed:27666593). Inhibits the transcriptional activity of SPI1 in a
CC dose-dependent manner (PubMed:14592421). {ECO:0000250|UniProtKB:Q14142,
CC ECO:0000269|PubMed:14592421, ECO:0000269|PubMed:27666593}.
CC -!- FUNCTION: Plays an essential role in the innate immune defense against
CC viruses and bacteria. Facilitates the type I IFN response by
CC interacting with MAVS at the outer mitochondria membrane and thereby
CC recruiting NF-kappa-B essential modulator IKBKG/NEMO to the MAVS
CC signalosome, leading to the activation of both the IFN regulatory
CC factor 3/IRF3 and NF-kappa-B pathways. Positively regulates the CGAS-
CC induced type I interferon signaling pathway by stabilizing CGAS and
CC inhibiting its autophagic degradation (PubMed:27666593). Acts as a
CC scaffold between TBK1 and STAT3 to promote phosphorylation of STAT3 and
CC resolve interferon-stimulated gene (ISG) expression. Inhibits the
CC transcriptional activity of SPI1 in a dose-dependent manner
CC (PubMed:14592421). {ECO:0000250|UniProtKB:Q14142,
CC ECO:0000269|PubMed:14592421, ECO:0000269|PubMed:27666593}.
CC -!- SUBUNIT: Interacts with MAVS. Interacts with WRNIP1 and PPP6C; these
CC interactions positively regulate the RIG-I/DDX58 signaling pathway.
CC Interacts with CGAS; this interaction stabilizes CGAS and promotes type
CC I interferon production. Interacts with USP14; this interaction
CC mediates the cleavage of 'Lys-48'-linked ubiquitination of CGAS (By
CC similarity). Interacts with TBK1 (By similarity). Interacts with SPI1
CC (PubMed:14592421). {ECO:0000250|UniProtKB:Q14142,
CC ECO:0000269|PubMed:14592421}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q14142}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:Q14142}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BVW3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BVW3-2; Sequence=VSP_012055, VSP_012056;
CC Name=3;
CC IsoId=Q8BVW3-3; Sequence=VSP_012053, VSP_012054;
CC -!- TISSUE SPECIFICITY: Expressed with high level in spleen, thymus, liver
CC and testis. Expressed with low level in the brain, kidney, and skeletal
CC muscle. Expressed in various differentiation stages of B-lymphocytes.
CC {ECO:0000269|PubMed:14592421}.
CC -!- DOMAIN: The B-box zinc finger is responsible for inhibition of SPI1-
CC mediated transcriptional activation.
CC -!- PTM: Ubiquitinated. Undergoes 'Lys-63'-linked polyubiquitination; this
CC modification allows IKBKG/NEMO recruitment to MAVS. Undergoes 'Lys-48'-
CC linked polyubiquitination by RNF125; this modification mediates its
CC degradation via the ubiquitin-proteasome pathway.
CC {ECO:0000250|UniProtKB:Q14142}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice have an impaired herpes simplex
CC virus type 1 (HSV-1)-triggered antiviral responses and become highly
CC susceptible to lethal HSV-1 infection. {ECO:0000269|PubMed:27666593}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32173.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB117644; BAD02394.1; -; mRNA.
DR EMBL; AK172895; BAD32173.1; ALT_INIT; mRNA.
DR EMBL; AK017887; BAB30988.1; -; mRNA.
DR EMBL; AK076277; BAC36286.1; -; mRNA.
DR EMBL; AL683884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18153.1; -. [Q8BVW3-1]
DR RefSeq; NP_083353.1; NM_029077.4. [Q8BVW3-1]
DR AlphaFoldDB; Q8BVW3; -.
DR SMR; Q8BVW3; -.
DR BioGRID; 216982; 3.
DR STRING; 10090.ENSMUSP00000038719; -.
DR iPTMnet; Q8BVW3; -.
DR PhosphoSitePlus; Q8BVW3; -.
DR EPD; Q8BVW3; -.
DR jPOST; Q8BVW3; -.
DR MaxQB; Q8BVW3; -.
DR PaxDb; Q8BVW3; -.
DR PeptideAtlas; Q8BVW3; -.
DR PRIDE; Q8BVW3; -.
DR ProteomicsDB; 298292; -. [Q8BVW3-1]
DR ProteomicsDB; 298293; -. [Q8BVW3-2]
DR ProteomicsDB; 298294; -. [Q8BVW3-3]
DR Antibodypedia; 14448; 138 antibodies from 24 providers.
DR DNASU; 74735; -.
DR Ensembl; ENSMUST00000046897; ENSMUSP00000038719; ENSMUSG00000039853. [Q8BVW3-1]
DR Ensembl; ENSMUST00000102924; ENSMUSP00000099988; ENSMUSG00000039853. [Q8BVW3-2]
DR Ensembl; ENSMUST00000184112; ENSMUSP00000138876; ENSMUSG00000039853. [Q8BVW3-3]
DR GeneID; 74735; -.
DR KEGG; mmu:74735; -.
DR UCSC; uc008stw.2; mouse. [Q8BVW3-1]
DR UCSC; uc008sty.2; mouse. [Q8BVW3-2]
DR CTD; 9830; -.
DR MGI; MGI:1921985; Trim14.
DR VEuPathDB; HostDB:ENSMUSG00000039853; -.
DR eggNOG; ENOG502QTZS; Eukaryota.
DR GeneTree; ENSGT00940000161010; -.
DR HOGENOM; CLU_013137_1_0_1; -.
DR InParanoid; Q8BVW3; -.
DR OMA; ARDCFAA; -.
DR PhylomeDB; Q8BVW3; -.
DR TreeFam; TF351014; -.
DR BioGRID-ORCS; 74735; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Trim14; mouse.
DR PRO; PR:Q8BVW3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BVW3; protein.
DR Bgee; ENSMUSG00000039853; Expressed in ureteric bud trunk and 59 other tissues.
DR ExpressionAtlas; Q8BVW3; baseline and differential.
DR Genevisible; Q8BVW3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
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:0032897; P:negative regulation of viral transcription; ISO:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; 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:0032880; P:regulation of protein localization; IBA:GO_Central.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central.
DR CDD; cd13738; SPRY_PRY_TRIM14; 1.
DR Gene3D; 2.60.120.920; -; 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; IPR044116; SPRY_PRY_TRIM14.
DR InterPro; IPR000315; Znf_B-box.
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; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Immunity; Innate immunity;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..440
FT /note="Tripartite motif-containing protein 14"
FT /id="PRO_0000220371"
FT DOMAIN 247..440
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 17..59
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 178
FT /note="A -> T (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012053"
FT VAR_SEQ 179..440
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012054"
FT VAR_SEQ 263..283
FT /note="YARTPTLDPDTMHARLRLSPD -> CETGEWEREVGWEQRWMGARK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012055"
FT VAR_SEQ 284..440
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012056"
FT MUTAGEN 51
FT /note="H->N: Loss of inhibition of SPI1-mediated
FT transcriptional activation."
FT /evidence="ECO:0000269|PubMed:14592421"
FT CONFLICT 43
FT /note="A -> T (in Ref. 3; BAB30988)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="H -> P (in Ref. 3; BAC36286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 49641 MW; 0B4A01FEAE79EF15 CRC64;
MASETTEARA PFQPDGAYGW RCPEHSERPA ELFCRRCGRC VCALCPVLGA HRGHPVGLAE
EEAVRVQKLI QDCLECLATK KRQHADNIAH LEDAGERLKV YADSSKAWLT QKFTELRLLL
DEEEVLAKKF IDKSTQLTLQ VYREQAETCG KQIEVMDDFS TRVWGIGQEP NPVQLLQAYI
ATKTEMGQQM SPSELSHPVP LSFEPVKNFF KEFVEAIGNT LQTPMDTRLK ENINCQLSNS
SSTKPGALLK TSPSPERALF LKYARTPTLD PDTMHARLRL SPDGLTVRCS LLGRLGPRPA
PRFDALRQVL GRDGFAAGRH YWEVDVQEAG VGWWVGAAYP SLRRRGASAA ARLGCNRESW
CVKRYDLEYW AFHDGQRSRL RPRRDPHRLG VFLDYEAGIL AFYDVAGGMS HLHTFHAAFQ
EPLYPALRLW EGPISIPRLP
