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Endoribonuclease Dicer (EC 3.1.26.3) (Helicase with RNase motif) (Helicase MOI)

 DICER_HUMAN             Reviewed;        1922 AA.
Q9UPY3; A7E2D3; B3KRG4; E0AD28; O95943; Q9UQ02;
25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
01-SEP-2009, sequence version 3.
27-SEP-2017, entry version 170.
RecName: Full=Endoribonuclease Dicer;
EC=3.1.26.3;
AltName: Full=Helicase with RNase motif;
Short=Helicase MOI;
Name=DICER1; Synonyms=DICER, HERNA, KIAA0928;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10786632; DOI=10.1016/S0167-4781(99)00221-3;
Matsuda S., Ichigotani Y., Okuda T., Irimura T., Nakatsugawa S.,
Hamaguchi M.;
"Molecular cloning and characterization of a novel human gene (HERNA)
which encodes a putative RNA-helicase.";
Biochim. Biophys. Acta 1490:163-169(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
TISSUE=Neuroblastoma;
PubMed=20615407; DOI=10.1016/j.febslet.2010.06.045;
Potenza N., Papa U., Scaruffi P., Mosca N., Tonini G.P., Russo A.;
"A novel splice variant of the human dicer gene is expressed in
neuroblastoma cells.";
FEBS Lett. 584:3452-3457(2010).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lung;
Provost P., Dishart D., Doucet D., Hermansson A., Frendewey D.,
Samuelsson B., Radmark O.;
"RNA binding and processing by recombinant human Dicer.";
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10231032; DOI=10.1093/dnares/6.1.63;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:63-70(1999).
[5]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1248-1922 (ISOFORM 1).
TISSUE=Lung;
PubMed=10051563; DOI=10.1073/pnas.96.5.1881;
Provost P., Samuelsson B., Radmark O.;
"Interaction of 5-lipoxygenase with cellular proteins.";
Proc. Natl. Acad. Sci. U.S.A. 96:1881-1885(1999).
[11]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-1313; ASP-1320;
GLU-1340; GLU-1444; GLN-1702; ASP-1709; PRO-1729 AND GLU-1813.
PubMed=15242644; DOI=10.1016/j.cell.2004.06.017;
Zhang H., Kolb F.A., Jaskiewicz L., Westhof E., Filipowicz W.;
"Single processing center models for human Dicer and bacterial RNase
III.";
Cell 118:57-68(2004).
[12]
INTERACTION WITH PIWIL1.
PubMed=14749716; DOI=10.1038/sj.embor.7400070;
Tahbaz N., Kolb F.A., Zhang H., Jaronczyk K., Filipowicz W.,
Hobman T.C.;
"Characterization of the interactions between mammalian PAZ PIWI
domain proteins and Dicer.";
EMBO Rep. 5:189-194(2004).
[13]
FUNCTION, AND INTERACTION WITH AGO2 AND TARBP2.
PubMed=16271387; DOI=10.1016/j.cell.2005.10.022;
Gregory R.I., Chendrimada T.P., Cooch N., Shiekhattar R.;
"Human RISC couples microRNA biogenesis and posttranscriptional gene
silencing.";
Cell 123:631-640(2005).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH
AGO1 AND AGO2.
PubMed=16289642; DOI=10.1016/j.cub.2005.10.048;
Meister G., Landthaler M., Peters L., Chen P.Y., Urlaub H.,
Luehrmann R., Tuschl T.;
"Identification of novel argonaute-associated proteins.";
Curr. Biol. 15:2149-2155(2005).
[15]
FUNCTION, AND INTERACTION WITH TARBP2.
PubMed=16142218; DOI=10.1038/sj.embor.7400509;
Haase A.D., Jaskiewicz L., Zhang H., Laine S., Sack R., Gatignol A.,
Filipowicz W.;
"TRBP, a regulator of cellular PKR and HIV-1 virus expression,
interacts with Dicer and functions in RNA silencing.";
EMBO Rep. 6:961-967(2005).
[16]
FUNCTION, AND INTERACTION WITH AGO2.
PubMed=16357216; DOI=10.1101/gad.1384005;
Maniataki E., Mourelatos Z.;
"A human, ATP-independent, RISC assembly machine fueled by pre-
miRNA.";
Genes Dev. 19:2979-2990(2005).
[17]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH
AGO2 AND TARBP2.
PubMed=15973356; DOI=10.1038/nature03868;
Chendrimada T.P., Gregory R.I., Kumaraswamy E., Norman J., Cooch N.,
Nishikura K., Shiekhattar R.;
"TRBP recruits the Dicer complex to Ago2 for microRNA processing and
gene silencing.";
Nature 436:740-744(2005).
[18]
FUNCTION, INTERACTION WITH PRKRA AND TARBP2, AND SUBCELLULAR LOCATION.
PubMed=16424907; DOI=10.1038/sj.emboj.7600942;
Lee Y., Hur I., Park S.-Y., Kim Y.-K., Suh M.R., Kim V.N.;
"The role of PACT in the RNA silencing pathway.";
EMBO J. 25:522-532(2006).
[19]
FUNCTION, AND INTERACTION WITH PRKRA AND TARBP2.
PubMed=17452327; DOI=10.1074/jbc.M611768200;
Kok K.H., Ng M.-H., Ching Y.-P., Jin D.-Y.;
"Human TRBP and PACT directly interact with each other and associate
with dicer to facilitate the production of small interfering RNA.";
J. Biol. Chem. 282:17649-17657(2007).
[20]
INTERACTION WITH DHX9.
PubMed=17531811; DOI=10.1016/j.molcel.2007.04.016;
Robb G.B., Rana T.M.;
"RNA helicase A interacts with RISC in human cells and functions in
RISC loading.";
Mol. Cell 26:523-537(2007).
[21]
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH AGO2; EIF6;
MOV10; RPL7A AND TARBP2, AND ASSOCIATION WITH THE 60S RIBOSOME.
PubMed=17507929; DOI=10.1038/nature05841;
Chendrimada T.P., Finn K.J., Ji X., Baillat D., Gregory R.I.,
Liebhaber S.A., Pasquinelli A.E., Shiekhattar R.;
"MicroRNA silencing through RISC recruitment of eIF6.";
Nature 447:823-828(2007).
[22]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH AGO2.
PubMed=18690212; DOI=10.1038/nature07186;
Qi H.H., Ongusaha P.P., Myllyharju J., Cheng D., Pakkanen O., Shi Y.,
Lee S.W., Peng J., Shi Y.;
"Prolyl 4-hydroxylation regulates Argonaute 2 stability.";
Nature 455:421-424(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH
AGO2 AND TARBP2.
PubMed=18178619; DOI=10.1073/pnas.0710869105;
MacRae I.J., Ma E., Zhou M., Robinson C.V., Doudna J.A.;
"In vitro reconstitution of the human RISC-loading complex.";
Proc. Natl. Acad. Sci. U.S.A. 105:512-517(2008).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[26]
FUNCTION.
PubMed=19219043; DOI=10.1038/ng.317;
Melo S.A., Ropero S., Moutinho C., Aaltonen L.A., Yamamoto H.,
Calin G.A., Rossi S., Fernandez A.F., Carneiro F., Oliveira C.,
Ferreira B., Liu C.-G., Villanueva A., Capella G., Schwartz S. Jr.,
Shiekhattar R., Esteller M.;
"A TARBP2 mutation in human cancer impairs microRNA processing and
DICER1 function.";
Nat. Genet. 41:365-370(2009).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
INVOLVEMENT IN RMSE2.
PubMed=21882293; DOI=10.1002/humu.21600;
Foulkes W.D., Bahubeshi A., Hamel N., Pasini B., Asioli S., Baynam G.,
Choong C.S., Charles A., Frieder R.P., Dishop M.K., Graf N., Ekim M.,
Bouron-Dal Soglio D., Arseneau J., Young R.H., Sabbaghian N.,
Srivastava A., Tischkowitz M.D., Priest J.R.;
"Extending the phenotypes associated with DICER1 mutations.";
Hum. Mutat. 32:1381-1384(2011).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-415, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[30]
INTERACTION WITH BCDIN3D.
PubMed=23063121; DOI=10.1016/j.cell.2012.08.041;
Xhemalce B., Robson S.C., Kouzarides T.;
"Human RNA methyltransferase BCDIN3D regulates microRNA processing.";
Cell 151:278-288(2012).
[31]
INVOLVEMENT IN NON-EPITHELIAL OVARIAN TUMORS, VARIANTS LYS-1705;
ASN-1709; GLU-1709; GLY-1709; HIS-1810; TYR-1810; ASN-1810; GLN-1813;
GLY-1813 AND LYS-1813, AND CHARACTERIZATION OF VARIANTS LYS-1705;
ASN-1709 AND GLU-1709.
PubMed=22187960; DOI=10.1056/NEJMoa1102903;
Heravi-Moussavi A., Anglesio M.S., Cheng S.W., Senz J., Yang W.,
Prentice L., Fejes A.P., Chow C., Tone A., Kalloger S.E., Hamel N.,
Roth A., Ha G., Wan A.N., Maines-Bandiera S., Salamanca C., Pasini B.,
Clarke B.A., Lee A.F., Lee C.H., Zhao C., Young R.H., Aparicio S.A.,
Sorensen P.H., Woo M.M., Boyd N., Jones S.J., Hirst M., Marra M.A.,
Gilks B., Shah S.P., Foulkes W.D., Morin G.B., Huntsman D.G.;
"Recurrent somatic DICER1 mutations in nonepithelial ovarian
cancers.";
N. Engl. J. Med. 366:234-242(2012).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160; SER-1460; SER-1470
AND SER-1868, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[34]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1660-1852, CATALYTIC
ACTIVITY, COFACTOR, AND SUBUNIT.
PubMed=17920623; DOI=10.1016/j.jmb.2007.08.069;
Takeshita D., Zenno S., Lee W.C., Nagata K., Saigo K., Tanokura M.;
"Homodimeric structure and double-stranded RNA cleavage activity of
the C-terminal RNase III domain of human dicer.";
J. Mol. Biol. 374:106-120(2007).
[35]
VARIANT PPB ARG-1583.
PubMed=19556464; DOI=10.1126/science.1174334;
Hill D.A., Ivanovich J., Priest J.R., Gurnett C.A., Dehner L.P.,
Desruisseau D., Jarzembowski J.A., Wikenheiser-Brokamp K.A.,
Suarez B.K., Whelan A.J., Williams G., Bracamontes D., Messinger Y.,
Goodfellow P.J.;
"DICER1 mutations in familial pleuropulmonary blastoma.";
Science 325:965-965(2009).
[36]
VARIANT MNG1 PHE-839.
PubMed=21205968; DOI=10.1001/jama.2010.1910;
Rio Frio T., Bahubeshi A., Kanellopoulou C., Hamel N., Niedziela M.,
Sabbaghian N., Pouchet C., Gilbert L., O'Brien P.K., Serfas K.,
Broderick P., Houlston R.S., Lesueur F., Bonora E., Muljo S.,
Schimke R.N., Bouron-Dal Soglio D., Arseneau J., Schultz K.A.,
Priest J.R., Nguyen V.H., Harach H.R., Livingston D.M., Foulkes W.D.,
Tischkowitz M.;
"DICER1 mutations in familial multinodular goiter with and without
ovarian Sertoli-Leydig cell tumors.";
JAMA 305:68-77(2011).
-!- FUNCTION: Double-stranded RNA (dsRNA) endoribonuclease playing a
central role in short dsRNA-mediated post-transcriptional gene
silencing. Cleaves naturally occurring long dsRNAs and short
hairpin pre-microRNAs (miRNA) into fragments of twenty-one to
twenty-three nucleotides with 3' overhang of two nucleotides,
producing respectively short interfering RNAs (siRNA) and mature
microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-
induced silencing complex (RISC) to complementary RNAs to degrade
them or prevent their translation. Gene silencing mediated by
siRNAs, also called RNA interference, controls the elimination of
transcripts from mobile and repetitive DNA elements of the genome
but also the degradation of exogenous RNA of viral origin for
instance. The miRNA pathway on the other side is a mean to
specifically regulate the expression of target genes.
{ECO:0000269|PubMed:15242644, ECO:0000269|PubMed:15973356,
ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387,
ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16357216,
ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:17452327,
ECO:0000269|PubMed:18178619, ECO:0000269|PubMed:19219043}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000269|PubMed:15242644,
ECO:0000269|PubMed:17920623}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000305|PubMed:17920623};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000305|PubMed:17920623};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000305|PubMed:17920623};
-!- SUBUNIT: Component of the RISC loading complex (RLC), or micro-RNA
(miRNA) loading complex (miRLC), which is composed of DICER1, AGO2
and TARBP2; DICER1 and TARBP2 are required to process precursor
miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2.
Note that the trimeric RLC/miRLC is also referred to as RISC.
Interacts with DHX9, AGO1, PIWIL1 and PRKRA. Associates with the
60S ribosome. Interacts with BCDIN3D. Interacts with AGO2, TARBP2,
EIF6, MOV10 and RPL7A (60S ribosome subunit); they form a large
RNA-induced silencing complex (RISC) (PubMed:17507929).
{ECO:0000269|PubMed:14749716, ECO:0000269|PubMed:15973356,
ECO:0000269|PubMed:16142218, ECO:0000269|PubMed:16271387,
ECO:0000269|PubMed:16289642, ECO:0000269|PubMed:16357216,
ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:17452327,
ECO:0000269|PubMed:17507929, ECO:0000269|PubMed:17531811,
ECO:0000269|PubMed:17920623, ECO:0000269|PubMed:18178619,
ECO:0000269|PubMed:18690212, ECO:0000269|PubMed:23063121}.
-!- INTERACTION:
P0C205:- (xeno); NbExp=7; IntAct=EBI-395506, EBI-8332963;
P55265-1:ADAR; NbExp=4; IntAct=EBI-395506, EBI-6913056;
P55265-5:ADAR; NbExp=8; IntAct=EBI-395506, EBI-6913210;
Q9UL18:AGO1; NbExp=5; IntAct=EBI-395506, EBI-527363;
Q9UKV8:AGO2; NbExp=19; IntAct=EBI-395506, EBI-528269;
Q8CJG0:Ago2 (xeno); NbExp=2; IntAct=EBI-395506, EBI-528299;
Q96C10:DHX58; NbExp=2; IntAct=EBI-395506, EBI-744193;
P19525:EIF2AK2; NbExp=2; IntAct=EBI-395506, EBI-640775;
Q96J94:PIWIL1; NbExp=2; IntAct=EBI-395506, EBI-527417;
O75569:PRKRA; NbExp=7; IntAct=EBI-395506, EBI-713955;
Q15633:TARBP2; NbExp=21; IntAct=EBI-395506, EBI-978581;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16424907}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9UPY3-1; Sequence=Displayed;
Name=2; Synonyms=t-Dicer;
IsoId=Q9UPY3-2; Sequence=VSP_042832;
Name=3;
IsoId=Q9UPY3-3; Sequence=VSP_055341, VSP_055342;
Note=No experimental confirmation available.;
-!- DISEASE: Pleuropulmonary blastoma (PPB) [MIM:601200]: A rare
pediatric intrathoracic neoplasm. The tumor arises from the lung,
pleura, or both, and appears to be purely mesenchymal in
phenotype. It lacks malignant epithelial elements, a feature that
distinguishes it from the classic adult-type pulmonary blastoma.
It arises during fetal lung development and is often part of an
inherited cancer syndrome. The tumor contain both epithelial and
mesenchymal cells. Early in tumorigenesis, cysts form in lung
airspaces, and these cysts are lined with benign-appearing
epithelium. Mesenchymal cells susceptible to malignant
transformation reside within the cyst walls and form a dense layer
beneath the epithelial lining. In a subset of patients, overgrowth
of the mesenchymal cells produces a sarcoma, a transition that is
associated with a poorer prognosis. Some patients have
multilocular cystic nephroma, a benign kidney tumor.
{ECO:0000269|PubMed:19556464}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Goiter multinodular 1, with or without Sertoli-Leydig
cell tumors (MNG1) [MIM:138800]: A common disorder characterized
by nodular overgrowth of the thyroid gland. Some individuals may
also develop Sertoli-Leydig cell tumors, usually of the ovary.
{ECO:0000269|PubMed:21205968}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Rhabdomyosarcoma, embryonal, 2 (RMSE2) [MIM:180295]: A
form of rhabdomyosarcoma, a highly malignant tumor of striated
muscle derived from primitive mesenchymal cells and exhibiting
differentiation along rhabdomyoblastic lines. Rhabdomyosarcoma is
one of the most frequently occurring soft tissue sarcomas and the
most common in children. It occurs in four forms: alveolar,
pleomorphic, embryonal and botryoidal rhabdomyosarcomas.
{ECO:0000269|PubMed:21882293}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=DICER1 mutations have been found in uterine cervix
embryonal rhabdomyosarcoma, primitive neuroectodermal tumor, Wilms
tumor, pulmonary sequestration and juvenile intestinal polyp
(PubMed:21882293). Somatic missense mutations affecting the RNase
IIIb domain of DICER1 are common in non-epithelial ovarian tumors.
These mutations do not abolish DICER1 function but alter it in
specific cell types, a novel mechanism through which perturbation
of microRNA processing may be oncogenic (PubMed:22187960).
{ECO:0000269|PubMed:21882293, ECO:0000269|PubMed:22187960}.
-!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00657}.
-!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB38857.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The dark side of RNA
- Issue 87 of October 2007;
URL="http://web.expasy.org/spotlight/back_issues/087";
-----------------------------------------------------------------------
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EMBL; AB028449; BAA78691.1; -; mRNA.
EMBL; HM595745; ADK25182.1; -; mRNA.
EMBL; AJ132261; CAB38857.2; ALT_INIT; mRNA.
EMBL; AB023145; BAA76772.2; -; mRNA.
EMBL; AK091513; BAG52376.1; -; mRNA.
EMBL; AL356017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL390254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW81596.1; -; Genomic_DNA.
EMBL; BC150287; AAI50288.1; -; mRNA.
CCDS; CCDS55941.1; -. [Q9UPY3-2]
CCDS; CCDS9931.1; -. [Q9UPY3-1]
RefSeq; NP_001182502.1; NM_001195573.1. [Q9UPY3-2]
RefSeq; NP_001258211.1; NM_001271282.2. [Q9UPY3-1]
RefSeq; NP_001278557.1; NM_001291628.1. [Q9UPY3-1]
RefSeq; NP_085124.2; NM_030621.4. [Q9UPY3-1]
RefSeq; NP_803187.1; NM_177438.2. [Q9UPY3-1]
RefSeq; XP_011534901.1; XM_011536599.1. [Q9UPY3-1]
RefSeq; XP_011534902.1; XM_011536600.2. [Q9UPY3-1]
RefSeq; XP_011534903.1; XM_011536601.2. [Q9UPY3-1]
RefSeq; XP_011534904.1; XM_011536602.2. [Q9UPY3-1]
RefSeq; XP_016876609.1; XM_017021120.1. [Q9UPY3-1]
RefSeq; XP_016876610.1; XM_017021121.1. [Q9UPY3-1]
UniGene; Hs.738957; -.
UniGene; Hs.87889; -.
PDB; 2EB1; X-ray; 2.00 A; A/B/C=1660-1852.
PDB; 4NGB; X-ray; 2.25 A; A=765-1065.
PDB; 4NGC; X-ray; 2.10 A; A=765-1065.
PDB; 4NGD; X-ray; 1.96 A; A=765-1065.
PDB; 4NGF; X-ray; 3.10 A; A/B/C/D=765-1065.
PDB; 4NGG; X-ray; 2.60 A; A=765-1065.
PDB; 4NH3; X-ray; 2.62 A; A=765-1065.
PDB; 4NH5; X-ray; 2.55 A; A=765-1065.
PDB; 4NH6; X-ray; 2.55 A; A=765-1065.
PDB; 4NHA; X-ray; 3.40 A; A=765-1065.
PDB; 4WYQ; X-ray; 3.20 A; A/D=267-389.
PDBsum; 2EB1; -.
PDBsum; 4NGB; -.
PDBsum; 4NGC; -.
PDBsum; 4NGD; -.
PDBsum; 4NGF; -.
PDBsum; 4NGG; -.
PDBsum; 4NH3; -.
PDBsum; 4NH5; -.
PDBsum; 4NH6; -.
PDBsum; 4NHA; -.
PDBsum; 4WYQ; -.
ProteinModelPortal; Q9UPY3; -.
SMR; Q9UPY3; -.
BioGrid; 116978; 83.
CORUM; Q9UPY3; -.
DIP; DIP-29664N; -.
IntAct; Q9UPY3; 37.
MINT; MINT-1957525; -.
STRING; 9606.ENSP00000343745; -.
ChEMBL; CHEMBL2311232; -.
iPTMnet; Q9UPY3; -.
PhosphoSitePlus; Q9UPY3; -.
BioMuta; DICER1; -.
DMDM; 257051056; -.
EPD; Q9UPY3; -.
PaxDb; Q9UPY3; -.
PeptideAtlas; Q9UPY3; -.
PRIDE; Q9UPY3; -.
Ensembl; ENST00000343455; ENSP00000343745; ENSG00000100697. [Q9UPY3-1]
Ensembl; ENST00000393063; ENSP00000376783; ENSG00000100697. [Q9UPY3-1]
Ensembl; ENST00000526495; ENSP00000437256; ENSG00000100697. [Q9UPY3-1]
Ensembl; ENST00000527414; ENSP00000435681; ENSG00000100697. [Q9UPY3-1]
Ensembl; ENST00000541352; ENSP00000444719; ENSG00000100697. [Q9UPY3-2]
Ensembl; ENST00000556045; ENSP00000451041; ENSG00000100697. [Q9UPY3-3]
GeneID; 23405; -.
KEGG; hsa:23405; -.
UCSC; uc001ydv.4; human. [Q9UPY3-1]
CTD; 23405; -.
DisGeNET; 23405; -.
EuPathDB; HostDB:ENSG00000100697.14; -.
GeneCards; DICER1; -.
HGNC; HGNC:17098; DICER1.
HPA; CAB068185; -.
HPA; HPA000694; -.
MalaCards; DICER1; -.
MIM; 138800; phenotype.
MIM; 180295; phenotype.
MIM; 601200; phenotype.
MIM; 606241; gene.
neXtProt; NX_Q9UPY3; -.
OpenTargets; ENSG00000100697; -.
Orphanet; 276399; Familial multinodular goiter.
Orphanet; 404476; Global developmental delay-lung cysts-overgrowth-Wilms tumor syndrome.
Orphanet; 99914; Gynandroblastoma.
Orphanet; 99915; Maligant granulosa cell tumor of ovary.
Orphanet; 99916; Malignant Sertoli-Leydig cell tumor of ovary.
Orphanet; 284343; Pleuropulmonary blastoma family tumor susceptibility syndrome.
PharmGKB; PA38437; -.
eggNOG; KOG0701; Eukaryota.
eggNOG; COG0571; LUCA.
eggNOG; COG1111; LUCA.
GeneTree; ENSGT00510000046789; -.
HOGENOM; HOG000001567; -.
HOVERGEN; HBG107811; -.
InParanoid; Q9UPY3; -.
KO; K11592; -.
OMA; GPWCADK; -.
OrthoDB; EOG091G00M8; -.
PhylomeDB; Q9UPY3; -.
TreeFam; TF330258; -.
BRENDA; 3.1.26.3; 2681.
Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
Reactome; R-HSA-426486; Small interfering RNA (siRNA) biogenesis.
SIGNOR; Q9UPY3; -.
ChiTaRS; DICER1; human.
EvolutionaryTrace; Q9UPY3; -.
GeneWiki; DICER1; -.
GenomeRNAi; 23405; -.
PRO; PR:Q9UPY3; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100697; -.
CleanEx; HS_DICER1; -.
ExpressionAtlas; Q9UPY3; baseline and differential.
Genevisible; Q9UPY3; HS.
GO; GO:0033167; C:ARC complex; IC:BHF-UCL.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:BHF-UCL.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0070578; C:RISC-loading complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004530; F:deoxyribonuclease I activity; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
GO; GO:0004521; F:endoribonuclease activity; IDA:BHF-UCL.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070883; F:pre-miRNA binding; IDA:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
GO; GO:0004525; F:ribonuclease III activity; IDA:BHF-UCL.
GO; GO:0035197; F:siRNA binding; IDA:BHF-UCL.
GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
GO; GO:0036404; P:conversion of ds siRNA to ss siRNA; IMP:AgBase.
GO; GO:0033168; P:conversion of ds siRNA to ss siRNA involved in RNA interference; IMP:BHF-UCL.
GO; GO:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0010586; P:miRNA metabolic process; TAS:Reactome.
GO; GO:0010626; P:negative regulation of Schwann cell proliferation; ISS:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0021675; P:nerve development; ISS:BHF-UCL.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:BHF-UCL.
GO; GO:0032290; P:peripheral nervous system myelin formation; ISS:BHF-UCL.
GO; GO:0031643; P:positive regulation of myelination; ISS:BHF-UCL.
GO; GO:0014040; P:positive regulation of Schwann cell differentiation; ISS:BHF-UCL.
GO; GO:0031054; P:pre-miRNA processing; IDA:UniProtKB.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IDA:UniProtKB.
GO; GO:0030422; P:production of siRNA involved in RNA interference; IDA:UniProtKB.
GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:BHF-UCL.
GO; GO:0035087; P:siRNA loading onto RISC involved in RNA interference; IDA:BHF-UCL.
GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; IMP:UniProtKB.
CDD; cd00593; RIBOc; 2.
Gene3D; 1.10.1520.10; -; 2.
InterPro; IPR005034; Dicer_dimerisation_dom.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR006935; Helicase/UvrB_N.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR003100; PAZ_dom.
InterPro; IPR000999; RNase_III_dom.
Pfam; PF03368; Dicer_dimer; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF02170; PAZ; 1.
Pfam; PF04851; ResIII; 1.
Pfam; PF00636; Ribonuclease_3; 2.
SMART; SM00487; DEXDc; 1.
SMART; SM00358; DSRM; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00949; PAZ; 1.
SMART; SM00535; RIBOc; 2.
SUPFAM; SSF101690; SSF101690; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF69065; SSF69065; 4.
PROSITE; PS51327; DICER_DSRBF; 1.
PROSITE; PS50137; DS_RBD; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50821; PAZ; 1.
PROSITE; PS00517; RNASE_3_1; 1.
PROSITE; PS50142; RNASE_3_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Disease mutation; Endonuclease; Helicase; Hydrolase;
Magnesium; Manganese; Metal-binding; Nuclease; Nucleotide-binding;
Phosphoprotein; Reference proteome; Repeat; RNA-binding;
RNA-mediated gene silencing.
CHAIN 1 1922 Endoribonuclease Dicer.
/FTId=PRO_0000180470.
DOMAIN 51 227 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 433 602 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 630 722 Dicer dsRNA-binding fold.
{ECO:0000255|PROSITE-ProRule:PRU00657}.
DOMAIN 891 1042 PAZ. {ECO:0000255|PROSITE-
ProRule:PRU00142}.
DOMAIN 1276 1403 RNase III 1. {ECO:0000255|PROSITE-
ProRule:PRU00177}.
DOMAIN 1666 1824 RNase III 2. {ECO:0000255|PROSITE-
ProRule:PRU00177}.
DOMAIN 1849 1914 DRBM. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
NP_BIND 64 71 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 256 595 Required for interaction with PRKRA and
TARBP2.
MOTIF 175 178 DECH box.
METAL 1316 1316 Magnesium or manganese 1. {ECO:0000250}.
METAL 1395 1395 Magnesium or manganese 1. {ECO:0000250}.
METAL 1398 1398 Magnesium or manganese 1. {ECO:0000250}.
METAL 1705 1705 Magnesium or manganese 2.
{ECO:0000244|PDB:2EB1,
ECO:0000269|PubMed:17920623}.
METAL 1810 1810 Magnesium or manganese 2.
{ECO:0000244|PDB:2EB1,
ECO:0000269|PubMed:17920623}.
METAL 1813 1813 Magnesium or manganese 2.
{ECO:0000244|PDB:2EB1,
ECO:0000269|PubMed:17920623}.
SITE 1806 1806 Important for activity.
{ECO:0000250|UniProtKB:Q8R418}.
MOD_RES 413 413 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 415 415 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1016 1016 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1160 1160 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1460 1460 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1468 1468 Phosphoserine.
{ECO:0000250|UniProtKB:Q8R418}.
MOD_RES 1470 1470 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1868 1868 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 13 MKSPALQPLSMAG -> MLAWESDHFLRIL (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055341.
VAR_SEQ 14 1115 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055342.
VAR_SEQ 1789 1922 LRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLET
VWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPA
ERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRS
LKANQPQVPNS -> KSFLQMYPVPLCENCLKWNQKLPNLA
RLRELTTGRSESLWK (in isoform 2).
{ECO:0000303|PubMed:20615407}.
/FTId=VSP_042832.
VARIANT 839 839 S -> F (in MNG1; dbSNP:rs387906934).
{ECO:0000269|PubMed:21205968}.
/FTId=VAR_065301.
VARIANT 1583 1583 L -> R (in PPB; dbSNP:rs137852976).
{ECO:0000269|PubMed:19556464}.
/FTId=VAR_063150.
VARIANT 1705 1705 E -> K (in non-epithelial ovarian tumor;
somatic mutation; results in reduced
RNase IIIb activity but retention of
RNase IIIa activity).
{ECO:0000269|PubMed:22187960}.
/FTId=VAR_067091.
VARIANT 1709 1709 D -> E (in non-epithelial ovarian tumor;
somatic mutation; results in reduced
RNase IIIb activity but retention of
RNase IIIa activity).
{ECO:0000269|PubMed:22187960}.
/FTId=VAR_067092.
VARIANT 1709 1709 D -> G (in non-epithelial ovarian tumor;
somatic mutation).
{ECO:0000269|PubMed:22187960}.
/FTId=VAR_067093.
VARIANT 1709 1709 D -> N (in non-epithelial ovarian tumor;
somatic mutation; results in reduced
RNase IIIb activity but retention of
RNase IIIa activity).
{ECO:0000269|PubMed:22187960}.
/FTId=VAR_067094.
VARIANT 1810 1810 D -> H (in non-epithelial ovarian tumor;
somatic mutation).
{ECO:0000269|PubMed:22187960}.
/FTId=VAR_067095.
VARIANT 1810 1810 D -> N (in non-epithelial ovarian tumor;
somatic mutation; dbSNP:rs775912475).
{ECO:0000269|PubMed:22187960}.
/FTId=VAR_067096.
VARIANT 1810 1810 D -> Y (in non-epithelial ovarian tumor;
somatic mutation).
{ECO:0000269|PubMed:22187960}.
/FTId=VAR_067097.
VARIANT 1813 1813 E -> G (in non-epithelial ovarian tumor;
somatic mutation).
{ECO:0000269|PubMed:22187960}.
/FTId=VAR_067098.
VARIANT 1813 1813 E -> K (in non-epithelial ovarian tumor;
somatic mutation).
{ECO:0000269|PubMed:22187960}.
/FTId=VAR_067099.
VARIANT 1813 1813 E -> Q (in non-epithelial ovarian tumor;
somatic mutation).
{ECO:0000269|PubMed:22187960}.
/FTId=VAR_067100.
MUTAGEN 960 960 F->A: 2-fold decrease in activity.
MUTAGEN 971 971 Y->A: 10-fold decrease in activity; when
associated with Y-972.
MUTAGEN 972 972 Y->A: 10-fold decrease in activity; when
associated with Y-971.
MUTAGEN 1036 1036 E->A: 5-fold decrease in activity.
MUTAGEN 1313 1313 E->A: No effect on activity.
{ECO:0000269|PubMed:15242644}.
MUTAGEN 1320 1320 D->A: Decreased activity. Loss of
activity; when associated with D-1709.
{ECO:0000269|PubMed:15242644}.
MUTAGEN 1340 1340 E->A: No effect on activity.
{ECO:0000269|PubMed:15242644}.
MUTAGEN 1444 1444 E->A: Decreased activity. Loss of
activity; when associated with E-1813.
{ECO:0000269|PubMed:15242644}.
MUTAGEN 1702 1702 Q->A: No effect on activity.
{ECO:0000269|PubMed:15242644}.
MUTAGEN 1709 1709 D->A: Decreased activity. Loss of
activity; when associated with D-1320.
{ECO:0000269|PubMed:15242644}.
MUTAGEN 1729 1729 P->E: No effect on activity.
{ECO:0000269|PubMed:15242644}.
MUTAGEN 1813 1813 E->A: Decreased activity. Loss of
activity; when associated with E-1444.
{ECO:0000269|PubMed:15242644}.
CONFLICT 75 90 VLLTKELSYQIRGDFS -> STTLLKSCLYLDLGETSA
(in Ref. 1; BAA78691). {ECO:0000305}.
CONFLICT 189 189 I -> F (in Ref. 1; BAA78691).
{ECO:0000305}.
CONFLICT 195 195 N -> I (in Ref. 1; BAA78691).
{ECO:0000305}.
CONFLICT 214 214 C -> W (in Ref. 1; BAA78691).
{ECO:0000305}.
CONFLICT 218 218 E -> D (in Ref. 1; BAA78691).
{ECO:0000305}.
CONFLICT 223 223 I -> F (in Ref. 1; BAA78691).
{ECO:0000305}.
CONFLICT 393 394 QQ -> HS (in Ref. 1; BAA78691).
{ECO:0000305}.
CONFLICT 492 493 KQ -> NT (in Ref. 1; BAA78691).
{ECO:0000305}.
CONFLICT 609 609 D -> H (in Ref. 1; BAA78691).
{ECO:0000305}.
HELIX 268 282 {ECO:0000244|PDB:4WYQ}.
HELIX 297 313 {ECO:0000244|PDB:4WYQ}.
HELIX 315 335 {ECO:0000244|PDB:4WYQ}.
HELIX 339 361 {ECO:0000244|PDB:4WYQ}.
STRAND 363 367 {ECO:0000244|PDB:4WYQ}.
HELIX 375 385 {ECO:0000244|PDB:4WYQ}.
STRAND 768 780 {ECO:0000244|PDB:4NGD}.
HELIX 783 785 {ECO:0000244|PDB:4NGD}.
HELIX 795 797 {ECO:0000244|PDB:4NGD}.
STRAND 801 808 {ECO:0000244|PDB:4NGD}.
STRAND 816 820 {ECO:0000244|PDB:4NGD}.
STRAND 823 836 {ECO:0000244|PDB:4NGD}.
HELIX 840 855 {ECO:0000244|PDB:4NGD}.
STRAND 877 883 {ECO:0000244|PDB:4NGD}.
STRAND 890 892 {ECO:0000244|PDB:4NGD}.
HELIX 894 902 {ECO:0000244|PDB:4NGD}.
STRAND 906 908 {ECO:0000244|PDB:4NGD}.
STRAND 916 918 {ECO:0000244|PDB:4NGD}.
HELIX 924 927 {ECO:0000244|PDB:4NGD}.
STRAND 931 937 {ECO:0000244|PDB:4NGD}.
STRAND 939 941 {ECO:0000244|PDB:4NGD}.
STRAND 945 951 {ECO:0000244|PDB:4NGD}.
HELIX 968 976 {ECO:0000244|PDB:4NGD}.
STRAND 987 992 {ECO:0000244|PDB:4NGD}.
HELIX 1016 1030 {ECO:0000244|PDB:4NGD}.
HELIX 1035 1037 {ECO:0000244|PDB:4NGD}.
STRAND 1038 1040 {ECO:0000244|PDB:4NGD}.
HELIX 1045 1051 {ECO:0000244|PDB:4NGD}.
HELIX 1054 1061 {ECO:0000244|PDB:4NGD}.
TURN 1662 1665 {ECO:0000244|PDB:2EB1}.
HELIX 1666 1673 {ECO:0000244|PDB:2EB1}.
HELIX 1680 1687 {ECO:0000244|PDB:2EB1}.
HELIX 1702 1722 {ECO:0000244|PDB:2EB1}.
HELIX 1729 1739 {ECO:0000244|PDB:2EB1}.
HELIX 1742 1751 {ECO:0000244|PDB:2EB1}.
HELIX 1754 1756 {ECO:0000244|PDB:2EB1}.
HELIX 1763 1778 {ECO:0000244|PDB:2EB1}.
HELIX 1806 1822 {ECO:0000244|PDB:2EB1}.
HELIX 1827 1847 {ECO:0000244|PDB:2EB1}.
SEQUENCE 1922 AA; 218682 MW; 9452B96A601D4551 CRC64;
MKSPALQPLS MAGLQLMTPA SSPMGPFFGL PWQQEAIHDN IYTPRKYQVE LLEAALDHNT
IVCLNTGSGK TFIAVLLTKE LSYQIRGDFS RNGKRTVFLV NSANQVAQQV SAVRTHSDLK
VGEYSNLEVN ASWTKERWNQ EFTKHQVLIM TCYVALNVLK NGYLSLSDIN LLVFDECHLA
ILDHPYREIM KLCENCPSCP RILGLTASIL NGKCDPEELE EKIQKLEKIL KSNAETATDL
VVLDRYTSQP CEIVVDCGPF TDRSGLYERL LMELEEALNF INDCNISVHS KERDSTLISK
QILSDCRAVL VVLGPWCADK VAGMMVRELQ KYIKHEQEEL HRKFLLFTDT FLRKIHALCE
EHFSPASLDL KFVTPKVIKL LEILRKYKPY ERQQFESVEW YNNRNQDNYV SWSDSEDDDE
DEEIEEKEKP ETNFPSPFTN ILCGIIFVER RYTAVVLNRL IKEAGKQDPE LAYISSNFIT
GHGIGKNQPR NKQMEAEFRK QEEVLRKFRA HETNLLIATS IVEEGVDIPK CNLVVRFDLP
TEYRSYVQSK GRARAPISNY IMLADTDKIK SFEEDLKTYK AIEKILRNKC SKSVDTGETD
IDPVMDDDDV FPPYVLRPDD GGPRVTINTA IGHINRYCAR LPSDPFTHLA PKCRTRELPD
GTFYSTLYLP INSPLRASIV GPPMSCVRLA ERVVALICCE KLHKIGELDD HLMPVGKETV
KYEEELDLHD EEETSVPGRP GSTKRRQCYP KAIPECLRDS YPRPDQPCYL YVIGMVLTTP
LPDELNFRRR KLYPPEDTTR CFGILTAKPI PQIPHFPVYT RSGEVTISIE LKKSGFMLSL
QMLELITRLH QYIFSHILRL EKPALEFKPT DADSAYCVLP LNVVNDSSTL DIDFKFMEDI
EKSEARIGIP STKYTKETPF VFKLEDYQDA VIIPRYRNFD QPHRFYVADV YTDLTPLSKF
PSPEYETFAE YYKTKYNLDL TNLNQPLLDV DHTSSRLNLL TPRHLNQKGK ALPLSSAEKR
KAKWESLQNK QILVPELCAI HPIPASLWRK AVCLPSILYR LHCLLTAEEL RAQTASDAGV
GVRSLPADFR YPNLDFGWKK SIDSKSFISI SNSSSAENDN YCKHSTIVPE NAAHQGANRT
SSLENHDQMS VNCRTLLSES PGKLHVEVSA DLTAINGLSY NQNLANGSYD LANRDFCQGN
QLNYYKQEIP VQPTTSYSIQ NLYSYENQPQ PSDECTLLSN KYLDGNANKS TSDGSPVMAV
MPGTTDTIQV LKGRMDSEQS PSIGYSSRTL GPNPGLILQA LTLSNASDGF NLERLEMLGD
SFLKHAITTY LFCTYPDAHE GRLSYMRSKK VSNCNLYRLG KKKGLPSRMV VSIFDPPVNW
LPPGYVVNQD KSNTDKWEKD EMTKDCMLAN GKLDEDYEEE DEEEESLMWR APKEEADYED
DFLEYDQEHI RFIDNMLMGS GAFVKKISLS PFSTTDSAYE WKMPKKSSLG SMPFSSDFED
FDYSSWDAMC YLDPSKAVEE DDFVVGFWNP SEENCGVDTG KQSISYDLHT EQCIADKSIA
DCVEALLGCY LTSCGERAAQ LFLCSLGLKV LPVIKRTDRE KALCPTRENF NSQQKNLSVS
CAAASVASSR SSVLKDSEYG CLKIPPRCMF DHPDADKTLN HLISGFENFE KKINYRFKNK
AYLLQAFTHA SYHYNTITDC YQRLEFLGDA ILDYLITKHL YEDPRQHSPG VLTDLRSALV
NNTIFASLAV KYDYHKYFKA VSPELFHVID DFVQFQLEKN EMQGMDSELR RSEEDEEKEE
DIEVPKAMGD IFESLAGAIY MDSGMSLETV WQVYYPMMRP LIEKFSANVP RSPVRELLEM
EPETAKFSPA ERTYDGKVRV TVEVVGKGKF KGVGRSYRIA KSAAARRALR SLKANQPQVP
NS


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