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Endoribonuclease Dicer (EC 3.1.26.3) (Double-strand-specific ribonuclease mDCR-1)

 DICER_MOUSE             Reviewed;        1916 AA.
Q8R418; Q8R419;
25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
01-SEP-2009, sequence version 3.
25-OCT-2017, entry version 150.
RecName: Full=Endoribonuclease Dicer;
EC=3.1.26.3;
AltName: Full=Double-strand-specific ribonuclease mDCR-1;
Name=Dicer1; Synonyms=Dicer, Mdcr;
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] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
[GENOMIC DNA] OF 17-1916.
STRAIN=C57BL/6J;
PubMed=11889553; DOI=10.1007/s00335-001-2119-6;
Nicholson R.H., Nicholson A.W.;
"Molecular characterization of a mouse cDNA encoding Dicer, a
ribonuclease III ortholog involved in RNA interference.";
Mamm. Genome 13:67-73(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=12526743; DOI=10.1016/S0960-9822(02)01394-5;
Doi N., Zenno S., Ueda R., Ohki-Hamazaki H., Ui-Tei K., Saigo K.;
"Short-interfering-RNA-mediated gene silencing in mammalian cells
requires Dicer and eIF2C translation initiation factors.";
Curr. Biol. 13:41-46(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Czech II;
PubMed=15081373; DOI=10.1016/j.ydbio.2004.01.028;
Svoboda P., Stein P., Anger M., Bernstein E., Hannon G.J.,
Schultz R.M.;
"RNAi and expression of retrotransposons MuERV-L and IAP in
preimplantation mouse embryos.";
Dev. Biol. 269:276-285(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1464, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
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).
[5]
IDENTIFICATION OF ISOFORM 2, FUNCTION (ISOFORMS 1 AND 2), DISRUPTION
PHENOTYPE (ISOFORM 2), AND TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
PubMed=24209619; DOI=10.1016/j.cell.2013.10.001;
Flemr M., Malik R., Franke V., Nejepinska J., Sedlacek R.,
Vlahovicek K., Svoboda P.;
"A retrotransposon-driven dicer isoform directs endogenous small
interfering RNA production in mouse oocytes.";
Cell 155:807-816(2013).
[6]
X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1647-1910, AND MUTAGENESIS
OF LYS-1800.
PubMed=18268334; DOI=10.1073/pnas.0711506105;
Du Z., Lee J.K., Tjhen R., Stroud R.M., James T.L.;
"Structural and biochemical insights into the dicing mechanism of
mouse Dicer: a conserved lysine is critical for dsRNA cleavage.";
Proc. Natl. Acad. Sci. U.S.A. 105:2391-2396(2008).
-!- 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 (By
similarity). {ECO:0000250|UniProtKB:Q9UPY3}.
-!- FUNCTION: Isoform 2: More active than isoform 1 to process long
double-stranded RNA into siRNAs. Responsible for the accumulation
of endogenous siRNAs observed in mouse oocytes compared to somatic
cells and it regulates meiotic spindle organization in female
germline.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000305};
-!- 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. Interacts with AGO2,
TARBP2, EIF6, MOV10 and RPL7A (60S ribosome subunit); they form a
large RNA-induced silencing complex (RISC). Interacts with BCDIN3D
(By similarity). {ECO:0000250|UniProtKB:Q9UPY3}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPY3}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=1; Synonyms=DicerS;
IsoId=Q8R418-1; Sequence=Displayed;
Name=2; Synonyms=DicerO;
IsoId=Q8R418-2; Sequence=VSP_053586;
Note=An MT-C retrotransposon in intron 6 of the mouse DICER gene
functions as a promoter producing a transcript lacking exons 1
to 6. A new alternative first exon is directly derived from the
retrotransposon.;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed in a wide variety of
tissues. Isoform 2 is specifically expressed in oocytes during
their growth (at protein level).
-!- DISRUPTION PHENOTYPE: Isoform 2: Mice lacking isoform 2 are viable
and males are fertile. However, females are sterile, their oocytes
displaying meiotic spindle defects.
-!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM21495.1; Type=Frameshift; Positions=8; Evidence={ECO:0000305};
Sequence=BAC15765.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC15765.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF484523; AAL84637.1; -; Genomic_DNA.
EMBL; AF484524; AAL84638.1; -; Genomic_DNA.
EMBL; AB081470; BAC15765.1; ALT_INIT; mRNA.
EMBL; AF430845; AAM21495.1; ALT_FRAME; mRNA.
UniGene; Mm.21135; -.
PDB; 3C4B; X-ray; 1.68 A; A=1648-1910.
PDB; 3C4T; X-ray; 2.80 A; A=1648-1910.
PDBsum; 3C4B; -.
PDBsum; 3C4T; -.
ProteinModelPortal; Q8R418; -.
SMR; Q8R418; -.
DIP; DIP-29721N; -.
IntAct; Q8R418; 4.
STRING; 10090.ENSMUSP00000043676; -.
iPTMnet; Q8R418; -.
PhosphoSitePlus; Q8R418; -.
EPD; Q8R418; -.
PaxDb; Q8R418; -.
PeptideAtlas; Q8R418; -.
PRIDE; Q8R418; -.
MGI; MGI:2177178; Dicer1.
eggNOG; KOG0701; Eukaryota.
eggNOG; COG0571; LUCA.
eggNOG; COG1111; LUCA.
HOGENOM; HOG000001567; -.
HOVERGEN; HBG107811; -.
InParanoid; Q8R418; -.
PhylomeDB; Q8R418; -.
BRENDA; 3.1.26.3; 3474.
EvolutionaryTrace; Q8R418; -.
PRO; PR:Q8R418; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_DICER1; -.
GO; GO:0034507; C:chromosome, centromeric outer repeat region; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0035068; C:micro-ribonucleoprotein complex; IDA:MGI.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0016442; C:RISC complex; IBA:GO_Central.
GO; GO:0070578; C:RISC-loading complex; ISS: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; ISO:MGI.
GO; GO:0004521; F:endoribonuclease activity; ISO:MGI.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035198; F:miRNA binding; IDA:MGI.
GO; GO:0070883; F:pre-miRNA binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0004525; F:ribonuclease III activity; IDA:MGI.
GO; GO:0035197; F:siRNA binding; ISO:MGI.
GO; GO:0048856; P:anatomical structure development; IMP:MGI.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
GO; GO:0061309; P:cardiac neural crest cell development involved in outflow tract morphogenesis; IMP:MGI.
GO; GO:0051216; P:cartilage development; IMP:MGI.
GO; GO:0008283; P:cell proliferation; IMP:MGI.
GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
GO; GO:1990141; P:chromatin silencing at centromere outer repeat region; IMP:MGI.
GO; GO:0036404; P:conversion of ds siRNA to ss siRNA; ISO:MGI.
GO; GO:0033168; P:conversion of ds siRNA to ss siRNA involved in RNA interference; ISO:MGI.
GO; GO:0051607; P:defense response to virus; IMP:MGI.
GO; GO:0048565; P:digestive tract development; IMP:MGI.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
GO; GO:0048730; P:epidermis morphogenesis; IMP:MGI.
GO; GO:0061548; P:ganglion development; IMP:MGI.
GO; GO:0071335; P:hair follicle cell proliferation; IMP:MGI.
GO; GO:0001942; P:hair follicle development; IMP:MGI.
GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
GO; GO:0060119; P:inner ear receptor cell development; IMP:MGI.
GO; GO:0060576; P:intestinal epithelial cell development; IGI:MGI.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:0000212; P:meiotic spindle organization; IMP:UniProtKB.
GO; GO:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; ISO:MGI.
GO; GO:0048255; P:mRNA stabilization; IMP:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0014835; P:myoblast differentiation involved in skeletal muscle regeneration; IMP:MGI.
GO; GO:0060253; P:negative regulation of glial cell proliferation; IMP:MGI.
GO; GO:0010626; P:negative regulation of Schwann cell proliferation; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0021675; P:nerve development; IMP:BHF-UCL.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:BHF-UCL.
GO; GO:0021889; P:olfactory bulb interneuron differentiation; IMP:MGI.
GO; GO:0032290; P:peripheral nervous system myelin formation; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
GO; GO:2000630; P:positive regulation of miRNA metabolic process; IMP:MGI.
GO; GO:0031643; P:positive regulation of myelination; IMP:BHF-UCL.
GO; GO:0014040; P:positive regulation of Schwann cell differentiation; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0031054; P:pre-miRNA processing; IDA:MGI.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IMP:BHF-UCL.
GO; GO:0030422; P:production of siRNA involved in RNA interference; IDA:MGI.
GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
GO; GO:0045595; P:regulation of cell differentiation; IMP:MGI.
GO; GO:0070173; P:regulation of enamel mineralization; IMP:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
GO; GO:2000628; P:regulation of miRNA metabolic process; IMP:MGI.
GO; GO:0010660; P:regulation of muscle cell apoptotic process; IMP:MGI.
GO; GO:0031641; P:regulation of myelination; IMP:MGI.
GO; GO:0050767; P:regulation of neurogenesis; IMP:MGI.
GO; GO:0045664; P:regulation of neuron differentiation; IMP:MGI.
GO; GO:0008593; P:regulation of Notch signaling pathway; IC:BHF-UCL.
GO; GO:0042487; P:regulation of odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0048713; P:regulation of oligodendrocyte differentiation; IMP:MGI.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:BHF-UCL.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; IMP:MGI.
GO; GO:0051252; P:regulation of RNA metabolic process; IMP:MGI.
GO; GO:2000736; P:regulation of stem cell differentiation; IMP:MGI.
GO; GO:0045069; P:regulation of viral genome replication; IMP:MGI.
GO; GO:0048608; P:reproductive structure development; IMP:MGI.
GO; GO:0016246; P:RNA interference; IMP:MGI.
GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; ISO:MGI.
GO; GO:0006396; P:RNA processing; IDA:MGI.
GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro.
GO; GO:0035087; P:siRNA loading onto RISC involved in RNA interference; ISO:MGI.
GO; GO:0007284; P:spermatogonial cell division; IMP:MGI.
GO; GO:0021522; P:spinal cord motor neuron differentiation; IMP:MGI.
GO; GO:0051225; P:spindle assembly; IMP:MGI.
GO; GO:0048536; P:spleen development; IMP:MGI.
GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; ISS:UniProtKB.
GO; GO:0010070; P:zygote asymmetric cell division; IMP:MGI.
CDD; cd00079; HELICc; 1.
CDD; cd00593; RIBOc; 2.
Gene3D; 1.10.1520.10; -; 3.
HAMAP; MF_00104; RNase_III; 1.
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; IPR036085; PAZ_dom_sf.
InterPro; IPR011907; RNase_III.
InterPro; IPR000999; RNase_III_dom.
InterPro; IPR036389; RNase_III_sf.
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 promoter usage; ATP-binding;
Complete proteome; Cytoplasm; Endonuclease; Helicase; Hydrolase;
Magnesium; Manganese; Metal-binding; Nuclease; Nucleotide-binding;
Phosphoprotein; Reference proteome; Repeat; RNA-binding;
RNA-mediated gene silencing.
CHAIN 1 1916 Endoribonuclease Dicer.
/FTId=PRO_0000180471.
DOMAIN 51 227 Helicase ATP-binding.
DOMAIN 433 602 Helicase C-terminal.
DOMAIN 630 722 Dicer dsRNA-binding fold.
DOMAIN 891 1042 PAZ.
DOMAIN 1276 1403 RNase III 1.
DOMAIN 1660 1818 RNase III 2.
DOMAIN 1843 1908 DRBM.
NP_BIND 64 71 ATP. {ECO:0000250}.
REGION 256 595 Required for interaction with PRKRA and
TARBP2. {ECO:0000250}.
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 1699 1699 Magnesium or manganese 2.
{ECO:0000250|UniProtKB:Q9UPY3}.
METAL 1804 1804 Magnesium or manganese 2.
{ECO:0000250|UniProtKB:Q9UPY3}.
METAL 1807 1807 Magnesium or manganese 2.
{ECO:0000250|UniProtKB:Q9UPY3}.
SITE 1800 1800 Important for activity.
{ECO:0000269|PubMed:18268334}.
MOD_RES 413 413 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UPY3}.
MOD_RES 415 415 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UPY3}.
MOD_RES 1016 1016 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UPY3}.
MOD_RES 1160 1160 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UPY3}.
MOD_RES 1456 1456 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UPY3}.
MOD_RES 1464 1464 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1466 1466 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UPY3}.
MOD_RES 1862 1862 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UPY3}.
VAR_SEQ 1 245 MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNI
YTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKELA
HQIRGDLNPHAKRTVFLVNSANQVAQQVSAVRTHSDLKVGE
YSDLEVNASWTKERWSQEFTKHQVLIMTCYVALTVLKNGYL
SLSDINLLVFDECHLAILDHPYREIMKLCESCPSCPRILGL
TASILNGKCDPEELEEKIQKLERILRSDAETATDLVVLDR
-> MSRDTEV (in isoform 2). {ECO:0000305}.
/FTId=VSP_053586.
MUTAGEN 1800 1800 K->A,R,S,T: Loss of activity.
{ECO:0000269|PubMed:18268334}.
CONFLICT 1 1 M -> L (in Ref. 2; BAC15765).
{ECO:0000305}.
CONFLICT 107 107 A -> C (in Ref. 3; AAM21495).
{ECO:0000305}.
CONFLICT 167 167 S -> P (in Ref. 2; BAC15765).
{ECO:0000305}.
CONFLICT 289 289 H -> Y (in Ref. 3; AAM21495).
{ECO:0000305}.
CONFLICT 610 610 A -> T (in Ref. 2; BAC15765).
{ECO:0000305}.
CONFLICT 759 759 E -> D (in Ref. 3; AAM21495).
{ECO:0000305}.
CONFLICT 837 837 T -> I (in Ref. 3; AAM21495).
{ECO:0000305}.
CONFLICT 888 888 G -> S (in Ref. 1; AAL84638).
{ECO:0000305}.
CONFLICT 965 965 Y -> C (in Ref. 2; BAC15765).
{ECO:0000305}.
CONFLICT 993 993 T -> A (in Ref. 2; BAC15765).
{ECO:0000305}.
CONFLICT 1090 1090 R -> G (in Ref. 2; BAC15765).
{ECO:0000305}.
CONFLICT 1110 1110 T -> S (in Ref. 2; BAC15765).
{ECO:0000305}.
CONFLICT 1336 1336 P -> H (in Ref. 1; AAL84638).
{ECO:0000305}.
CONFLICT 1619 1619 A -> S (in Ref. 1; AAL84637 and 2;
BAC15765). {ECO:0000305}.
CONFLICT 1860 1860 K -> E (in Ref. 2; BAC15765).
{ECO:0000305}.
HELIX 1649 1656 {ECO:0000244|PDB:3C4B}.
TURN 1657 1659 {ECO:0000244|PDB:3C4B}.
HELIX 1660 1667 {ECO:0000244|PDB:3C4B}.
HELIX 1674 1681 {ECO:0000244|PDB:3C4B}.
HELIX 1696 1716 {ECO:0000244|PDB:3C4B}.
HELIX 1723 1733 {ECO:0000244|PDB:3C4B}.
HELIX 1736 1745 {ECO:0000244|PDB:3C4B}.
HELIX 1748 1750 {ECO:0000244|PDB:3C4B}.
HELIX 1757 1774 {ECO:0000244|PDB:3C4B}.
HELIX 1800 1816 {ECO:0000244|PDB:3C4B}.
HELIX 1821 1842 {ECO:0000244|PDB:3C4B}.
HELIX 1847 1854 {ECO:0000244|PDB:3C4B}.
TURN 1856 1858 {ECO:0000244|PDB:3C4B}.
STRAND 1859 1861 {ECO:0000244|PDB:3C4B}.
STRAND 1872 1878 {ECO:0000244|PDB:3C4B}.
TURN 1879 1881 {ECO:0000244|PDB:3C4B}.
STRAND 1882 1890 {ECO:0000244|PDB:3C4B}.
HELIX 1891 1908 {ECO:0000244|PDB:3C4B}.
SEQUENCE 1916 AA; 216821 MW; D97EA17922D7E79C CRC64;
MKSPALQPLS MAGLQLMTPA SSPMGPFFGL PWQQEAIHDN IYTPRKYQVE LLEAALDHNT
IVCLNTGSGK TFIAVLLTKE LAHQIRGDLN PHAKRTVFLV NSANQVAQQV SAVRTHSDLK
VGEYSDLEVN ASWTKERWSQ EFTKHQVLIM TCYVALTVLK NGYLSLSDIN LLVFDECHLA
ILDHPYREIM KLCESCPSCP RILGLTASIL NGKCDPEELE EKIQKLERIL RSDAETATDL
VVLDRYTSQP CEIVVDCGPF TDRSGLYERL LMELEAALDF INDCNVAVHS KERDSTLISK
QILSDCRAVL VVLGPWCADK VAGMMVRELQ KYIKHEQEEL HRKFLLFTDT LLRKIHALCE
EYFSPASLDL KYVTPKVMKL LEILRKYKPY ERQQFESVEW YNNRNQDNYV SWSDSEDDDD
DEEIEEKEKP ETNFPSPFTN ILCGIIFVER RYTAVVLNRL IKEAGKQDPE LAYISSNFIT
GHGIGKNQPR SKQMEAEFRK QEEVLRKFRA HETNLLIATS VVEEGVDIPK CNLVVRFDLP
TEYRSYVQSK GRARAPISNY VMLADTDKIK SFEEDLKTYK AIEKILRNKC SKSADGAEAD
VHAGVDDEDA FPPYVLRPDD GGPRVTINTA IGHINRYCAR LPSDPFTHLA PKCRTRELPD
GTFYSTLYLP INSPLRASIV GPPMDSVRLA ERVVALICCE KLHKIGELDE HLMPVGKETV
KYEEELDLHD EEETSVPGRP GSTKRRQCYP KAIPECLRES YPKPDQPCYL YVIGMVLTTP
LPDELNFRRR KLYPPEDTTR CFGILTAKPI PQIPHFPVYT RSGEVTISIE LKKSGFTLSQ
QMLELITRLH QYIFSHILRL EKPALEFKPT GAESAYCVLP LNVVNDSGTL DIDFKFMEDI
EKSEARIGIP STKYSKETPF VFKLEDYQDA VIIPRYRNFD QPHRFYVADV YTDLTPLSKF
PSPEYETFAE YYKTKYNLDL TNLNQPLLDV DHTSSRLNLL TPRHLNQKGK ALPLSSAEKR
KAKWESLQNK QILVPELCAI HPIPASLWRK AVCLPSILYR LHCLLTAEEL RAQTASDAGV
GVRSLPVDFR YPNLDFGWKK SIDSKSFIST CNSSLAESDN YCKHSTTVVP EHAAHQGATR
PSLENHDQMS VNCKRLPAES PAKLQSEVST DLTAINGLSY NKNLANGSYD LVNRDFCQGN
QLNYFKQEIP VQPTTSYPIQ NLYNYENQPK PSNECPLLSN TYLDGNANTS TSDGSPAVST
MPAMMNAVKA LKDRMDSEQS PSVGYSSRTL GPNPGLILQA LTLSNASDGF NLERLEMLGD
SFLKHAITTY LFCTYPDAHE GRLSYMRSKK VSNCNLYRLG KKKGLPSRMV VSIFDPPVNW
LPPGYVVNQD KSNSEKWEKD EMTKDCLLAN GKLGEACEEE EDLTWRAPKE EAEDEDDFLE
YDQEHIQFID SMLMGSGAFV RKISLSPFSA SDSAYEWKMP KKASLGSMPF ASGLEDFDYS
SWDAMCYLDP SKAVEEDDFV VGFWNPSEEN CGVDTGKQSI SYDLHTEQCI ADKSIADCVE
ALLGCYLTSC GERAAQLFLC SLGLKVLPVI KRTSREKALD PAQENGSSQQ KSLSGSCAAP
VGPRSSAGKD LEYGCLKIPP RCMFDHPDAE KTLNHLISGF ETFEKKINYR FKNKAYLLQA
FTHASYHYNT ITDCYQRLEF LGDAILDYLI TKHLYEDPRQ HSPGVLTDLR SALVNNTIFA
SLAVKYDYHK YFKAVSPELF HVIDDFVKFQ LEKNEMQGMD SELRRSEEDE EKEEDIEVPK
AMGDIFESLA GAIYMDSGMS LEVVWQVYYP MMQPLIEKFS ANVPRSPVRE LLEMEPETAK
FSPAERTYDG KVRVTVEVVG KGKFKGVGRS YRIAKSAAAR RALRSLKANQ PQVPNS


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