TRIM6_MOUSE
ID TRIM6_MOUSE Reviewed; 488 AA.
AC Q8BGE7; B2RSQ8; Q99PQ6;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Tripartite motif-containing protein 6;
DE EC=2.3.2.27 {ECO:0000269|PubMed:22328504};
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM6 {ECO:0000305};
GN Name=Trim6;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 55-205.
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MYC.
RX PubMed=22328504; DOI=10.1242/jcs.095273;
RA Sato T., Okumura F., Ariga T., Hatakeyama S.;
RT "TRIM6 interacts with Myc and maintains the pluripotency of mouse embryonic
RT stem cells.";
RL J. Cell Sci. 125:1544-1555(2012).
RN [5]
RP FUNCTION.
RX PubMed=24882218; DOI=10.1016/j.immuni.2014.04.018;
RA Rajsbaum R., Versteeg G.A., Schmid S., Maestre A.M., Belicha-Villanueva A.,
RA Martinez-Romero C., Patel J.R., Morrison J., Pisanelli G., Miorin L.,
RA Laurent-Rolle M., Moulton H.M., Stein D.A., Fernandez-Sesma A.,
RA tenOever B.R., Garcia-Sastre A.;
RT "Unanchored K48-linked polyubiquitin synthesized by the E3-ubiquitin ligase
RT TRIM6 stimulates the interferon-IKKepsilon kinase-mediated antiviral
RT response.";
RL Immunity 40:880-895(2014).
CC -!- FUNCTION: E3 ubiquitin ligase that plays a crucial role in the
CC activation of the IKBKE-dependent branch of the type I interferon
CC signaling pathway (PubMed:24882218). In concert with the ubiquitin-
CC conjugating E2 enzyme UBE2K, synthesizes unanchored 'Lys-48'-linked
CC polyubiquitin chains that promote the oligomerization and
CC autophosphorylation of IKBKE leading to stimulation of an antiviral
CC response (PubMed:24882218). Ubiquitinates also MYC and inhibits its
CC transcription activation activity, maintaining the pluripotency of
CC embryonic stem cells (PubMed:22328504). {ECO:0000269|PubMed:22328504,
CC ECO:0000269|PubMed:24882218}.
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:0000269|PubMed:22328504};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:22328504}.
CC -!- SUBUNIT: Homotrimer. Forms heteromultimers (via B30.2/SPRY domain) with
CC TRIM5 (By similarity). Interacts with MYC (PubMed:22328504). Interacts
CC (via SPRY domain) with IKBKE (By similarity). Interacts with VAMP8;
CC this interaction contributes to the activation of the type I interferon
CC antiviral response (By similarity). {ECO:0000250|UniProtKB:Q9C030,
CC ECO:0000269|PubMed:22328504}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22328504}.
CC -!- DOMAIN: The B-box zinc finger and the linker region between the coiled
CC coil and B30.2/SPRY domains contribute to higher order self-
CC association. {ECO:0000250|UniProtKB:Q9C030}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AK033396; BAC28267.1; -; mRNA.
DR EMBL; AK049238; BAC33629.1; -; mRNA.
DR EMBL; BC138965; AAI38966.1; -; mRNA.
DR EMBL; AF220031; AAG53485.1; -; mRNA.
DR CCDS; CCDS40065.1; -.
DR RefSeq; NP_001013637.1; NM_001013616.2.
DR RefSeq; XP_006508427.1; XM_006508364.2.
DR RefSeq; XP_006508428.1; XM_006508365.3.
DR RefSeq; XP_006508429.1; XM_006508366.3.
DR AlphaFoldDB; Q8BGE7; -.
DR SMR; Q8BGE7; -.
DR STRING; 10090.ENSMUSP00000095782; -.
DR iPTMnet; Q8BGE7; -.
DR PhosphoSitePlus; Q8BGE7; -.
DR PaxDb; Q8BGE7; -.
DR PRIDE; Q8BGE7; -.
DR Antibodypedia; 11069; 115 antibodies from 27 providers.
DR DNASU; 94088; -.
DR Ensembl; ENSMUST00000098180; ENSMUSP00000095782; ENSMUSG00000072244.
DR GeneID; 94088; -.
DR KEGG; mmu:94088; -.
DR UCSC; uc009ivq.1; mouse.
DR CTD; 117854; -.
DR MGI; MGI:2137352; Trim6.
DR VEuPathDB; HostDB:ENSMUSG00000072244; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000163021; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q8BGE7; -.
DR OMA; EPTYCFN; -.
DR OrthoDB; 165920at2759; -.
DR PhylomeDB; Q8BGE7; -.
DR TreeFam; TF338674; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 94088; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Trim6; mouse.
DR PRO; PR:Q8BGE7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BGE7; protein.
DR Bgee; ENSMUSG00000072244; Expressed in ectoplacental cone and 74 other tissues.
DR ExpressionAtlas; Q8BGE7; baseline and differential.
DR Genevisible; Q8BGE7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IMP:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035458; P:cellular response to interferon-beta; ISO:MGI.
DR GO; GO:0098586; P:cellular response to virus; IDA:UniProtKB.
DR GO; GO:0010994; P:free ubiquitin chain polymerization; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; ISO:MGI.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:MGI.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
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 GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
DR CDD; cd15823; SPRY_PRY_TRIM6; 1.
DR Gene3D; 2.60.120.920; -; 1.
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; IPR035828; PRY/SPRY_TRIM6.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 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; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..488
FT /note="Tripartite motif-containing protein 6"
FT /id="PRO_0000056203"
FT DOMAIN 282..488
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 15..60
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 92..133
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 132..223
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 488 AA; 56152 MW; A1FDC42D8DD4A531 CRC64;
MTSTVLVDIR DEVTCPICLE LLTEPLSIDC GHSFCQVCII GNSNNSVFGQ GGRSSCPVCR
TSYQPGNLRP NRHLAAIVKR LREVALCPGK QLEVIFCALH GEKLQLFCKE DGKLICWLCE
RSQEHRGHHT FLMEEVAQEY QDMFQESLKK LRREQQEAEK LKALIQEKRE SWKSQVEPEK
RRIQTEFKQL RSILDREEQR ELKKLEVEER KGLSIIEKAE GDLIHQSQSL KDLISDLEHR
CQGSTVELLQ DVGDVTKRSE FWTLRKPQAL PTKLKSLFRA PDLRKMLKVF RELTDVQSYW
VDVTLNPQTA NLNLVLSKNR RQVRFVGAQL SEPSSLEEHY DCSVLGSQHF SSGKYYWEVD
VSKKTAWILG VCSTPVDPMF SFSQYSSKQG AYSRYQPQCG YWVIGLQCKH EYRAYEDSSP
SLLLSMTVPP RRIGIFLDCE AGTVSFYNVT NHGLPIYTFS KYYFPSALCP YFNPCSCIVP
MTLRRPTS
