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TRI40_MOUSE
ID   TRI40_MOUSE             Reviewed;         246 AA.
AC   Q3UWA4; B2RVT3;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=E3 ubiquitin ligase TRIM40;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q6P9F5};
DE   AltName: Full=Probable E3 NEDD8-protein ligase;
GN   Name=Trim40; Synonyms=Gm319;
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=Cecum;
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   DISRUPTION PHENOTYPE.
RX   PubMed=29117565; DOI=10.1016/j.celrep.2017.10.020;
RA   Zhao C., Jia M., Song H., Yu Z., Wang W., Li Q., Zhang L., Zhao W., Cao X.;
RT   "The E3 Ubiquitin Ligase TRIM40 Attenuates Antiviral Immune Responses by
RT   Targeting MDA5 and RIG-I.";
RL   Cell Rep. 21:1613-1623(2017).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that plays a role in the
CC       limitation of the innate immune response. Mediates inhibition of the
CC       RLR signaling pathway by ubiquitinating DDX58 and IFIH1 receptors,
CC       leading to their proteasomal degradation. Promotes also the neddylation
CC       of IKBKG/NEMO, stabilizing NFKBIA, and thereby inhibiting of NF-kappa-B
CC       nuclear translocation and activation. {ECO:0000250|UniProtKB:Q6P9F5}.
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:Q6P9F5};
CC   -!- SUBUNIT: Interacts with NEDD8. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: TRIM40 deficiency greatly enhances antiviral
CC       immune responses and interferon-beta production and thus inhibits viral
CC       replication. {ECO:0000269|PubMed:29117565}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR   EMBL; AK136498; BAE23012.1; -; mRNA.
DR   EMBL; BC147336; AAI47337.1; -; mRNA.
DR   EMBL; BC147337; AAI47338.1; -; mRNA.
DR   CCDS; CCDS28727.1; -.
DR   RefSeq; NP_001028407.1; NM_001033235.3.
DR   RefSeq; XP_017172846.1; XM_017317357.1.
DR   AlphaFoldDB; Q3UWA4; -.
DR   BioGRID; 228835; 2.
DR   STRING; 10090.ENSMUSP00000084400; -.
DR   iPTMnet; Q3UWA4; -.
DR   PhosphoSitePlus; Q3UWA4; -.
DR   PaxDb; Q3UWA4; -.
DR   PRIDE; Q3UWA4; -.
DR   ProteomicsDB; 298218; -.
DR   Antibodypedia; 26227; 91 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000087158; ENSMUSP00000084400; ENSMUSG00000073399.
DR   GeneID; 195359; -.
DR   KEGG; mmu:195359; -.
DR   UCSC; uc008clk.2; mouse.
DR   CTD; 135644; -.
DR   MGI; MGI:2684881; Trim40.
DR   VEuPathDB; HostDB:ENSMUSG00000073399; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00710000106875; -.
DR   InParanoid; Q3UWA4; -.
DR   OMA; PEHVSHH; -.
DR   OrthoDB; 1129525at2759; -.
DR   PhylomeDB; Q3UWA4; -.
DR   TreeFam; TF333491; -.
DR   BioGRID-ORCS; 195359; 1 hit in 73 CRISPR screens.
DR   PRO; PR:Q3UWA4; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q3UWA4; protein.
DR   Bgee; ENSMUSG00000073399; Expressed in jejunum and 49 other tissues.
DR   ExpressionAtlas; Q3UWA4; baseline and differential.
DR   Genevisible; Q3UWA4; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008385; C:IkappaB kinase complex; 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; IBA:GO_Central.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:MGI.
DR   GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISO:MGI.
DR   GO; GO:0045116; P:protein neddylation; 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   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Metal-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..246
FT                   /note="E3 ubiquitin ligase TRIM40"
FT                   /id="PRO_0000307823"
FT   ZN_FING         12..55
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         64..105
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   COILED          105..170
FT                   /evidence="ECO:0000255"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ   SEQUENCE   246 AA;  27903 MW;  E2895CFA10159FAB CRC64;
     MGSLDKDNQD ICPICLDPLK EAVSTDCRHL FCRMCLTQHM DKASVSGILS CPVCRKPCSE
     GVLGDNYICH THQKRVRRFC EASGHLLCEE CLQSPEHQSH TELSIENAIS HYKERLNRRS
     RKLRKDLGNL QQLKAQEKKM LQALQVDCEC HRLRTDLQNQ DQTKEQLKAL PWHWLDQEDL
     PEEVAKIFSF SEAVTQLSIL VSGLERMAKD LDASTLKDAS DLLDRSAPQK LEGLLSRVSP
     AGPKLS
 
 
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