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Database: UniProt
Entry: Q8R418
LinkDB: Q8R418
Original site: Q8R418 
ID   DICER_MOUSE             Reviewed;        1916 AA.
AC   Q8R418; Q8R419;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 3.
DT   16-OCT-2019, entry version 165.
DE   RecName: Full=Endoribonuclease Dicer;
DE            EC=3.1.26.3;
DE   AltName: Full=Double-strand-specific ribonuclease mDCR-1;
GN   Name=Dicer1; Synonyms=Dicer, Mdcr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP   [GENOMIC DNA] OF 17-1916.
RC   STRAIN=C57BL/6J;
RX   PubMed=11889553; DOI=10.1007/s00335-001-2119-6;
RA   Nicholson R.H., Nicholson A.W.;
RT   "Molecular characterization of a mouse cDNA encoding Dicer, a
RT   ribonuclease III ortholog involved in RNA interference.";
RL   Mamm. Genome 13:67-73(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=12526743; DOI=10.1016/s0960-9822(02)01394-5;
RA   Doi N., Zenno S., Ueda R., Ohki-Hamazaki H., Ui-Tei K., Saigo K.;
RT   "Short-interfering-RNA-mediated gene silencing in mammalian cells
RT   requires Dicer and eIF2C translation initiation factors.";
RL   Curr. Biol. 13:41-46(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=Czech II;
RX   PubMed=15081373; DOI=10.1016/j.ydbio.2004.01.028;
RA   Svoboda P., Stein P., Anger M., Bernstein E., Hannon G.J.,
RA   Schultz R.M.;
RT   "RNAi and expression of retrotransposons MuERV-L and IAP in
RT   preimplantation mouse embryos.";
RL   Dev. Biol. 269:276-285(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1464, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   IDENTIFICATION OF ISOFORM 2, FUNCTION (ISOFORMS 1 AND 2), DISRUPTION
RP   PHENOTYPE (ISOFORM 2), AND TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
RX   PubMed=24209619; DOI=10.1016/j.cell.2013.10.001;
RA   Flemr M., Malik R., Franke V., Nejepinska J., Sedlacek R.,
RA   Vlahovicek K., Svoboda P.;
RT   "A retrotransposon-driven dicer isoform directs endogenous small
RT   interfering RNA production in mouse oocytes.";
RL   Cell 155:807-816(2013).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1647-1910, AND MUTAGENESIS
RP   OF LYS-1800.
RX   PubMed=18268334; DOI=10.1073/pnas.0711506105;
RA   Du Z., Lee J.K., Tjhen R., Stroud R.M., James T.L.;
RT   "Structural and biochemical insights into the dicing mechanism of
RT   mouse Dicer: a conserved lysine is critical for dsRNA cleavage.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2391-2396(2008).
CC   -!- FUNCTION: Double-stranded RNA (dsRNA) endoribonuclease playing a
CC       central role in short dsRNA-mediated post-transcriptional gene
CC       silencing. Cleaves naturally occurring long dsRNAs and short
CC       hairpin pre-microRNAs (miRNA) into fragments of twenty-one to
CC       twenty-three nucleotides with 3' overhang of two nucleotides,
CC       producing respectively short interfering RNAs (siRNA) and mature
CC       microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-
CC       induced silencing complex (RISC) to complementary RNAs to degrade
CC       them or prevent their translation. Gene silencing mediated by
CC       siRNAs, also called RNA interference, controls the elimination of
CC       transcripts from mobile and repetitive DNA elements of the genome
CC       but also the degradation of exogenous RNA of viral origin for
CC       instance. The miRNA pathway on the other side is a mean to
CC       specifically regulate the expression of target genes (By
CC       similarity). {ECO:0000250|UniProtKB:Q9UPY3}.
CC   -!- FUNCTION: Isoform 2: More active than isoform 1 to process long
CC       double-stranded RNA into siRNAs. Responsible for the accumulation
CC       of endogenous siRNAs observed in mouse oocytes compared to somatic
CC       cells and it regulates meiotic spindle organization in female
CC       germline.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.;
CC         EC=3.1.26.3;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000305};
CC   -!- SUBUNIT: Component of the RISC loading complex (RLC), or micro-RNA
CC       (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2
CC       and TARBP2; DICER1 and TARBP2 are required to process precursor
CC       miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2.
CC       Note that the trimeric RLC/miRLC is also referred to as RISC.
CC       Interacts with DHX9, AGO1, PIWIL1 and PRKRA. Interacts with AGO2,
CC       TARBP2, EIF6, MOV10 and RPL7A (60S ribosome subunit); they form a
CC       large RNA-induced silencing complex (RISC). Interacts with BCDIN3D
CC       (By similarity). {ECO:0000250|UniProtKB:Q9UPY3}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPY3}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=1; Synonyms=DicerS;
CC         IsoId=Q8R418-1; Sequence=Displayed;
CC       Name=2; Synonyms=DicerO;
CC         IsoId=Q8R418-2; Sequence=VSP_053586;
CC         Note=An MT-C retrotransposon in intron 6 of the mouse DICER gene
CC         functions as a promoter producing a transcript lacking exons 1
CC         to 6. A new alternative first exon is directly derived from the
CC         retrotransposon.;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in a wide variety of
CC       tissues. Isoform 2 is specifically expressed in oocytes during
CC       their growth (at protein level).
CC   -!- DISRUPTION PHENOTYPE: Isoform 2: Mice lacking isoform 2 are viable
CC       and males are fertile. However, females are sterile, their oocytes
CC       displaying meiotic spindle defects.
CC   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM21495.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAC15765.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC15765.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
DR   EMBL; AF484523; AAL84637.1; -; Genomic_DNA.
DR   EMBL; AF484524; AAL84638.1; -; Genomic_DNA.
DR   EMBL; AB081470; BAC15765.1; ALT_INIT; mRNA.
DR   EMBL; AF430845; AAM21495.1; ALT_FRAME; mRNA.
DR   PDB; 3C4B; X-ray; 1.68 A; A=1648-1910.
DR   PDB; 3C4T; X-ray; 2.80 A; A=1648-1910.
DR   PDBsum; 3C4B; -.
DR   PDBsum; 3C4T; -.
DR   SMR; Q8R418; -.
DR   ComplexPortal; CPX-1073; RISC-loading complex, PRKRA variant.
DR   ComplexPortal; CPX-135; RISC-loading complex, TARBP2 variant.
DR   DIP; DIP-29721N; -.
DR   IntAct; Q8R418; 4.
DR   STRING; 10090.ENSMUSP00000043676; -.
DR   iPTMnet; Q8R418; -.
DR   PhosphoSitePlus; Q8R418; -.
DR   EPD; Q8R418; -.
DR   jPOST; Q8R418; -.
DR   PaxDb; Q8R418; -.
DR   PeptideAtlas; Q8R418; -.
DR   PRIDE; Q8R418; -.
DR   MGI; MGI:2177178; Dicer1.
DR   eggNOG; KOG0701; Eukaryota.
DR   eggNOG; COG0571; LUCA.
DR   eggNOG; COG1111; LUCA.
DR   HOGENOM; HOG000001567; -.
DR   InParanoid; Q8R418; -.
DR   PhylomeDB; Q8R418; -.
DR   BRENDA; 3.1.26.3; 3474.
DR   Reactome; R-MMU-203927; MicroRNA (miRNA) biogenesis.
DR   Reactome; R-MMU-426486; Small interfering RNA (siRNA) biogenesis.
DR   ChiTaRS; Dicer1; mouse.
DR   EvolutionaryTrace; Q8R418; -.
DR   PRO; PR:Q8R418; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0034507; C:chromosome, centromeric outer repeat region; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0030426; C:growth cone; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016442; C:RISC complex; IDA:MGI.
DR   GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004530; F:deoxyribonuclease I activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR   GO; GO:0004521; F:endoribonuclease activity; ISO:MGI.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035198; F:miRNA binding; IDA:MGI.
DR   GO; GO:0070883; F:pre-miRNA binding; ISO:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0004525; F:ribonuclease III activity; IDA:MGI.
DR   GO; GO:0035197; F:siRNA binding; ISO:MGI.
DR   GO; GO:0048856; P:anatomical structure development; IMP:MGI.
DR   GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR   GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
DR   GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
DR   GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
DR   GO; GO:0061309; P:cardiac neural crest cell development involved in outflow tract morphogenesis; IMP:MGI.
DR   GO; GO:0051216; P:cartilage development; IMP:MGI.
DR   GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:1990141; P:chromatin silencing at centromere outer repeat region; IMP:MGI.
DR   GO; GO:0036404; P:conversion of ds siRNA to ss siRNA; ISO:MGI.
DR   GO; GO:0033168; P:conversion of ds siRNA to ss siRNA involved in RNA interference; ISO:MGI.
DR   GO; GO:0051607; P:defense response to virus; IMP:MGI.
DR   GO; GO:0048565; P:digestive tract development; IMP:MGI.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR   GO; GO:0048730; P:epidermis morphogenesis; IMP:MGI.
DR   GO; GO:0061548; P:ganglion development; IMP:MGI.
DR   GO; GO:0071335; P:hair follicle cell proliferation; IMP:MGI.
DR   GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR   GO; GO:0060119; P:inner ear receptor cell development; IMP:MGI.
DR   GO; GO:0060576; P:intestinal epithelial cell development; IGI:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0000212; P:meiotic spindle organization; IMP:UniProtKB.
DR   GO; GO:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; ISO:MGI.
DR   GO; GO:0048255; P:mRNA stabilization; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0014835; P:myoblast differentiation involved in skeletal muscle regeneration; IMP:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:0060253; P:negative regulation of glial cell proliferation; IMP:MGI.
DR   GO; GO:0010626; P:negative regulation of Schwann cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
DR   GO; GO:0021675; P:nerve development; IMP:BHF-UCL.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0038061; P:NIK/NF-kappaB signaling; ISO:MGI.
DR   GO; GO:0021889; P:olfactory bulb interneuron differentiation; IMP:MGI.
DR   GO; GO:0032290; P:peripheral nervous system myelin formation; IMP:BHF-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR   GO; GO:2000630; P:positive regulation of miRNA metabolic process; IMP:MGI.
DR   GO; GO:0031643; P:positive regulation of myelination; IMP:BHF-UCL.
DR   GO; GO:0014040; P:positive regulation of Schwann cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0031054; P:pre-miRNA processing; IDA:MGI.
DR   GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IMP:BHF-UCL.
DR   GO; GO:0030422; P:production of siRNA involved in RNA interference; IDA:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR   GO; GO:0045595; P:regulation of cell differentiation; IMP:MGI.
DR   GO; GO:0070173; P:regulation of enamel mineralization; IMP:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR   GO; GO:2000628; P:regulation of miRNA metabolic process; IMP:MGI.
DR   GO; GO:0010660; P:regulation of muscle cell apoptotic process; IMP:MGI.
DR   GO; GO:0031641; P:regulation of myelination; IMP:MGI.
DR   GO; GO:0050767; P:regulation of neurogenesis; IMP:MGI.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IMP:MGI.
DR   GO; GO:0008593; P:regulation of Notch signaling pathway; IC:BHF-UCL.
DR   GO; GO:0042487; P:regulation of odontogenesis of dentin-containing tooth; IMP:MGI.
DR   GO; GO:0048713; P:regulation of oligodendrocyte differentiation; IMP:MGI.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IMP:BHF-UCL.
DR   GO; GO:0045589; P:regulation of regulatory T cell differentiation; IMP:MGI.
DR   GO; GO:0051252; P:regulation of RNA metabolic process; IMP:MGI.
DR   GO; GO:2000736; P:regulation of stem cell differentiation; IMP:MGI.
DR   GO; GO:0045069; P:regulation of viral genome replication; IMP:MGI.
DR   GO; GO:0048608; P:reproductive structure development; IMP:MGI.
DR   GO; GO:0016246; P:RNA interference; IMP:MGI.
DR   GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; ISO:MGI.
DR   GO; GO:0006396; P:RNA processing; IDA:MGI.
DR   GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro.
DR   GO; GO:0035087; P:siRNA loading onto RISC involved in RNA interference; ISO:MGI.
DR   GO; GO:0007284; P:spermatogonial cell division; IMP:MGI.
DR   GO; GO:0021522; P:spinal cord motor neuron differentiation; IMP:MGI.
DR   GO; GO:0051225; P:spindle assembly; IMP:MGI.
DR   GO; GO:0048536; P:spleen development; IMP:MGI.
DR   GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR   GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; ISS:UniProtKB.
DR   GO; GO:0001834; P:trophectodermal cell proliferation; IMP:MGI.
DR   GO; GO:0035148; P:tube formation; ISO:MGI.
DR   GO; GO:0010070; P:zygote asymmetric cell division; IMP:MGI.
DR   CDD; cd00048; DSRM; 1.
DR   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 1.10.1520.10; -; 1.
DR   Gene3D; 3.30.160.380; -; 1.
DR   HAMAP; MF_00104; RNase_III; 1.
DR   InterPro; IPR038248; Dicer_dimer_sf.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003100; PAZ_dom.
DR   InterPro; IPR036085; PAZ_dom_sf.
DR   InterPro; IPR011907; RNase_III.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR036389; RNase_III_sf.
DR   Pfam; PF03368; Dicer_dimer; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF02170; PAZ; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   Pfam; PF00636; Ribonuclease_3; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00949; PAZ; 1.
DR   SMART; SM00535; RIBOc; 2.
DR   SUPFAM; SSF101690; SSF101690; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF69065; SSF69065; 2.
DR   PROSITE; PS51327; DICER_DSRBF; 1.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50821; PAZ; 1.
DR   PROSITE; PS00517; RNASE_3_1; 1.
DR   PROSITE; PS50142; RNASE_3_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative promoter usage; ATP-binding;
KW   Complete proteome; Cytoplasm; Endonuclease; Helicase; Hydrolase;
KW   Magnesium; Manganese; Metal-binding; Nuclease; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW   RNA-mediated gene silencing.
FT   CHAIN         1   1916       Endoribonuclease Dicer.
FT                                /FTId=PRO_0000180471.
FT   DOMAIN       51    227       Helicase ATP-binding.
FT   DOMAIN      433    602       Helicase C-terminal.
FT   DOMAIN      630    722       Dicer dsRNA-binding fold.
FT   DOMAIN      891   1042       PAZ.
FT   DOMAIN     1276   1403       RNase III 1.
FT   DOMAIN     1660   1818       RNase III 2.
FT   DOMAIN     1843   1908       DRBM.
FT   NP_BIND      64     71       ATP. {ECO:0000250}.
FT   REGION      256    595       Required for interaction with PRKRA and
FT                                TARBP2. {ECO:0000250}.
FT   MOTIF       175    178       DECH box.
FT   METAL      1316   1316       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL      1395   1395       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL      1398   1398       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL      1699   1699       Magnesium or manganese 2.
FT                                {ECO:0000250|UniProtKB:Q9UPY3}.
FT   METAL      1804   1804       Magnesium or manganese 2.
FT                                {ECO:0000250|UniProtKB:Q9UPY3}.
FT   METAL      1807   1807       Magnesium or manganese 2.
FT                                {ECO:0000250|UniProtKB:Q9UPY3}.
FT   SITE       1800   1800       Important for activity.
FT                                {ECO:0000269|PubMed:18268334}.
FT   MOD_RES     413    413       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UPY3}.
FT   MOD_RES     415    415       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UPY3}.
FT   MOD_RES    1016   1016       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UPY3}.
FT   MOD_RES    1160   1160       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UPY3}.
FT   MOD_RES    1456   1456       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UPY3}.
FT   MOD_RES    1464   1464       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1466   1466       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UPY3}.
FT   MOD_RES    1862   1862       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UPY3}.
FT   VAR_SEQ       1    245       MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNI
FT                                YTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKELA
FT                                HQIRGDLNPHAKRTVFLVNSANQVAQQVSAVRTHSDLKVGE
FT                                YSDLEVNASWTKERWSQEFTKHQVLIMTCYVALTVLKNGYL
FT                                SLSDINLLVFDECHLAILDHPYREIMKLCESCPSCPRILGL
FT                                TASILNGKCDPEELEEKIQKLERILRSDAETATDLVVLDR
FT                                -> MSRDTEV (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_053586.
FT   MUTAGEN    1800   1800       K->A,R,S,T: Loss of activity.
FT                                {ECO:0000269|PubMed:18268334}.
FT   CONFLICT      1      1       M -> L (in Ref. 2; BAC15765).
FT                                {ECO:0000305}.
FT   CONFLICT    107    107       A -> C (in Ref. 3; AAM21495).
FT                                {ECO:0000305}.
FT   CONFLICT    167    167       S -> P (in Ref. 2; BAC15765).
FT                                {ECO:0000305}.
FT   CONFLICT    289    289       H -> Y (in Ref. 3; AAM21495).
FT                                {ECO:0000305}.
FT   CONFLICT    610    610       A -> T (in Ref. 2; BAC15765).
FT                                {ECO:0000305}.
FT   CONFLICT    759    759       E -> D (in Ref. 3; AAM21495).
FT                                {ECO:0000305}.
FT   CONFLICT    837    837       T -> I (in Ref. 3; AAM21495).
FT                                {ECO:0000305}.
FT   CONFLICT    888    888       G -> S (in Ref. 1; AAL84638).
FT                                {ECO:0000305}.
FT   CONFLICT    965    965       Y -> C (in Ref. 2; BAC15765).
FT                                {ECO:0000305}.
FT   CONFLICT    993    993       T -> A (in Ref. 2; BAC15765).
FT                                {ECO:0000305}.
FT   CONFLICT   1090   1090       R -> G (in Ref. 2; BAC15765).
FT                                {ECO:0000305}.
FT   CONFLICT   1110   1110       T -> S (in Ref. 2; BAC15765).
FT                                {ECO:0000305}.
FT   CONFLICT   1336   1336       P -> H (in Ref. 1; AAL84638).
FT                                {ECO:0000305}.
FT   CONFLICT   1619   1619       A -> S (in Ref. 1; AAL84637 and 2;
FT                                BAC15765). {ECO:0000305}.
FT   CONFLICT   1860   1860       K -> E (in Ref. 2; BAC15765).
FT                                {ECO:0000305}.
FT   HELIX      1649   1656       {ECO:0000244|PDB:3C4B}.
FT   TURN       1657   1659       {ECO:0000244|PDB:3C4B}.
FT   HELIX      1660   1667       {ECO:0000244|PDB:3C4B}.
FT   HELIX      1674   1681       {ECO:0000244|PDB:3C4B}.
FT   HELIX      1696   1716       {ECO:0000244|PDB:3C4B}.
FT   HELIX      1723   1733       {ECO:0000244|PDB:3C4B}.
FT   HELIX      1736   1745       {ECO:0000244|PDB:3C4B}.
FT   HELIX      1748   1750       {ECO:0000244|PDB:3C4B}.
FT   HELIX      1757   1774       {ECO:0000244|PDB:3C4B}.
FT   HELIX      1800   1816       {ECO:0000244|PDB:3C4B}.
FT   HELIX      1821   1842       {ECO:0000244|PDB:3C4B}.
FT   HELIX      1847   1854       {ECO:0000244|PDB:3C4B}.
FT   TURN       1856   1858       {ECO:0000244|PDB:3C4B}.
FT   STRAND     1859   1861       {ECO:0000244|PDB:3C4B}.
FT   STRAND     1872   1878       {ECO:0000244|PDB:3C4B}.
FT   TURN       1879   1881       {ECO:0000244|PDB:3C4B}.
FT   STRAND     1882   1890       {ECO:0000244|PDB:3C4B}.
FT   HELIX      1891   1908       {ECO:0000244|PDB:3C4B}.
SQ   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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