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E3 ubiquitin/ISG15 ligase TRIM25 (EC 6.3.2.n3) (Estrogen-responsive finger protein) (RING-type E3 ubiquitin transferase) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM25) (Tripartite motif-containing protein 25) (Ubiquitin/ISG15-conjugating enzyme TRIM25) (Zinc finger protein 147)

 TRI25_MOUSE             Reviewed;         634 AA.
Q61510; Q5SU70;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
25-OCT-2017, entry version 156.
RecName: Full=E3 ubiquitin/ISG15 ligase TRIM25;
EC=6.3.2.n3 {ECO:0000250|UniProtKB:Q14258};
AltName: Full=Estrogen-responsive finger protein;
AltName: Full=RING-type E3 ubiquitin transferase;
EC=2.3.2.27 {ECO:0000250|UniProtKB:Q14258};
AltName: Full=RING-type E3 ubiquitin transferase TRIM25 {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 25;
AltName: Full=Ubiquitin/ISG15-conjugating enzyme TRIM25;
AltName: Full=Zinc finger protein 147;
Name=Trim25; Synonyms=Efp, Zfp147, Znf147;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Ovary, Placenta, and Uterus;
PubMed=7592654; DOI=10.1074/jbc.270.41.24406;
Orimo A., Inoue S., Ikeda K., Noji S., Muramatsu M.;
"Molecular cloning, structure, and expression of mouse estrogen-
responsive finger protein Efp. Co-localization with estrogen receptor
mRNA in target organs.";
J. Biol. Chem. 270:24406-24413(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, Lung, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Functions as a ubiquitin E3 ligase and as an ISG15 E3
ligase. Involved in innate immune defense against viruses by
mediating ubiquitination of DDX58. Mediates 'Lys-63'-linked
polyubiquitination of the DDX58 N-terminal CARD-like region which
is crucial for triggering the cytosolic signal transduction that
leads to the production of interferons in response to viral
infection. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter
protein implicated in the regulation of a large spectrum signaling
pathway. Mediates estrogen action in various target organs.
Mediates the ubiquitination and subsequent proteasomal degradation
of ZFHX3. {ECO:0000250|UniProtKB:Q14258}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000250|UniProtKB:Q14258}.
-!- CATALYTIC ACTIVITY: ATP + [ISG15] + [protein]-lysine = AMP +
diphosphate + [protein]-N-ISGyllysine.
{ECO:0000250|UniProtKB:Q14258}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts (via SPRY domain) with DDX58 (via CARD domain).
Interacts with ZFHX3. {ECO:0000250|UniProtKB:Q14258}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14258}.
Note=Colocalized with DDX58 at cytoplasmic perinuclear bodies.
{ECO:0000250|UniProtKB:Q14258}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7592654}.
-!- DOMAIN: The RING-type zinc finger is important for ISG15 E3 ligase
activity and autoISGylation. AutoISGylation negatively regulates
ISG15 E3 ligase activity. {ECO:0000250|UniProtKB:Q14258}.
-!- DOMAIN: The C-terminal B30.2/SPRY domain interacts with the first
N-terminal CARD domain of DDX58. {ECO:0000250|UniProtKB:Q14258}.
-!- PTM: Auto-ISGylated. {ECO:0000250|UniProtKB:Q14258}.
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EMBL; D63902; BAA09941.1; -; mRNA.
EMBL; AK169562; BAE41230.1; -; mRNA.
EMBL; AL646096; CAI24266.1; -; Genomic_DNA.
CCDS; CCDS36278.1; -.
PIR; I49642; I49642.
RefSeq; NP_033572.2; NM_009546.2.
UniGene; Mm.248445; -.
PDB; 4B8E; X-ray; 1.78 A; A/B=440-634.
PDBsum; 4B8E; -.
ProteinModelPortal; Q61510; -.
SMR; Q61510; -.
BioGrid; 229840; 4.
IntAct; Q61510; 3.
MINT; MINT-240797; -.
STRING; 10090.ENSMUSP00000103528; -.
iPTMnet; Q61510; -.
PhosphoSitePlus; Q61510; -.
EPD; Q61510; -.
MaxQB; Q61510; -.
PaxDb; Q61510; -.
PeptideAtlas; Q61510; -.
PRIDE; Q61510; -.
Ensembl; ENSMUST00000107896; ENSMUSP00000103528; ENSMUSG00000000275.
GeneID; 217069; -.
KEGG; mmu:217069; -.
UCSC; uc007kwc.1; mouse.
CTD; 7706; -.
MGI; MGI:102749; Trim25.
eggNOG; ENOG410ITFP; Eukaryota.
eggNOG; ENOG410XQS1; LUCA.
GeneTree; ENSGT00760000118995; -.
HOGENOM; HOG000132974; -.
HOVERGEN; HBG101063; -.
InParanoid; Q61510; -.
KO; K10652; -.
OMA; SPAFQDH; -.
OrthoDB; EOG091G05F6; -.
TreeFam; TF351086; -.
Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
UniPathway; UPA00143; -.
PRO; PR:Q61510; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000000275; -.
CleanEx; MM_TRIM25; -.
ExpressionAtlas; Q61510; baseline and differential.
Genevisible; Q61510; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:1904264; F:ubiquitin protein ligase activity involved in ERAD pathway; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0036503; P:ERAD pathway; ISO:MGI.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
GO; GO:1902187; P:negative regulation of viral release from host cell; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISO:MGI.
GO; GO:0006513; P:protein monoubiquitination; ISO:MGI.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0046596; P:regulation of viral entry into host cell; ISO:MGI.
GO; GO:1902186; P:regulation of viral release from host cell; ISO:MGI.
GO; GO:0043627; P:response to estrogen; ISO:MGI.
GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR003879; Butyrophylin_SPRY.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR006574; PRY.
InterPro; IPR003877; SPRY_dom.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF13765; PRY; 1.
Pfam; PF00622; SPRY; 1.
PRINTS; PR01407; BUTYPHLNCDUF.
SMART; SM00589; PRY; 1.
SMART; SM00184; RING; 1.
SMART; SM00449; SPRY; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS50188; B302_SPRY; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Antiviral defense; Coiled coil;
Complete proteome; Cytoplasm; Immunity; Innate immunity;
Isopeptide bond; Ligase; Metal-binding; Phosphoprotein;
Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 634 E3 ubiquitin/ISG15 ligase TRIM25.
/FTId=PRO_0000056234.
DOMAIN 444 634 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
ZN_FING 13 54 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
COILED 215 305 {ECO:0000255}.
MOD_RES 90 90 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14258}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000250|UniProtKB:Q14258}.
MOD_RES 272 272 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q14258}.
MOD_RES 277 277 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q14258}.
MOD_RES 572 572 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q14258}.
CROSSLNK 116 116 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15).
{ECO:0000250|UniProtKB:Q14258}.
CONFLICT 34 34 M -> T (in Ref. 1; BAA09941).
{ECO:0000305}.
CONFLICT 165 165 L -> F (in Ref. 1; BAA09941).
{ECO:0000305}.
CONFLICT 261 261 K -> R (in Ref. 1; BAA09941).
{ECO:0000305}.
CONFLICT 439 439 V -> I (in Ref. 1; BAA09941).
{ECO:0000305}.
HELIX 441 450 {ECO:0000244|PDB:4B8E}.
HELIX 454 457 {ECO:0000244|PDB:4B8E}.
HELIX 458 460 {ECO:0000244|PDB:4B8E}.
TURN 468 470 {ECO:0000244|PDB:4B8E}.
STRAND 475 478 {ECO:0000244|PDB:4B8E}.
TURN 479 482 {ECO:0000244|PDB:4B8E}.
STRAND 483 486 {ECO:0000244|PDB:4B8E}.
STRAND 501 509 {ECO:0000244|PDB:4B8E}.
STRAND 514 523 {ECO:0000244|PDB:4B8E}.
STRAND 528 535 {ECO:0000244|PDB:4B8E}.
STRAND 540 542 {ECO:0000244|PDB:4B8E}.
HELIX 543 545 {ECO:0000244|PDB:4B8E}.
STRAND 553 559 {ECO:0000244|PDB:4B8E}.
STRAND 562 567 {ECO:0000244|PDB:4B8E}.
STRAND 570 574 {ECO:0000244|PDB:4B8E}.
STRAND 581 587 {ECO:0000244|PDB:4B8E}.
TURN 588 591 {ECO:0000244|PDB:4B8E}.
STRAND 592 609 {ECO:0000244|PDB:4B8E}.
STRAND 616 624 {ECO:0000244|PDB:4B8E}.
STRAND 628 631 {ECO:0000244|PDB:4B8E}.
SEQUENCE 634 AA; 71726 MW; 3B764531AAE8582E CRC64;
MAELNPLAEE LSCSVCLELF KEPVTTPCGH NFCMSCLDET WVVQGPPYRC PQCRKVYQVR
PQLQKNTVMC AVVEQFLQAE QARTPVDDWT PPARFSASSA ATQVACDHCL TEIAVKTCLV
CMASFCQEHL RPHFDSPAFQ DHPLQSPIRD LLRRKCTQHN RLRELFCPEH GECICHICLV
EHKTCSPTTL SQASADLEYK LRNKLTIMHS HINGATKALE DVRSKQQCVQ DSMKRKMEQL
RQEYMEMKAV IDAAETSSLR KLKEEEKRVY GKFDTIYQVL VKKKSEMQKL KAEVELIMDK
GDEFEFLEKA AKLQGESTKP VYIPKIDLDH DLIMGIYQGA ADLKSELKHS IKKLQKKSEE
HNGSGNKGDQ TQSTFKPVQP SKKTIQEKKT KKTPVAPGPP SHFSPNKLPT FGAPGQSLDS
KATSPDAAPK ASAAQPDSVG VKAKVLENFL TKSRTELLEY FVKVIFDYNT AHNKVSLSNK
YTTASVSDGL QHYRSHPQRF TYCSQVLGLH CYKNGIHYWE VELQKNNFCG VGICYGSMER
QGPESRLGRN PNSWCVEWFN NKISAWHNNV EKTLPSTKAT RVGVLLNCDH GFVIFFAVTE
KVHLMYKFKV DFTEALYPAF WVFSAGTTLS ICSK


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