CHDM_DROME
ID CHDM_DROME Reviewed; 1982 AA.
AC O97159; Q8MZ43; Q9VW50;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2000, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein Mi-2 homolog;
DE EC=3.6.4.12 {ECO:0000269|PubMed:18250149};
DE AltName: Full=ATP-dependent helicase Mi-2;
DE Short=dMi-2;
GN Name=Mi-2; ORFNames=CG8103;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF GLY-737.
RX PubMed=9836641; DOI=10.1126/science.282.5395.1897;
RA Kehle J., Beuchle D., Treuheit S., Christen B., Kennison J.A., Bienz M.,
RA Muller J.;
RT "dMi-2, a hunchback-interacting protein that functions in Polycomb
RT repression.";
RL Science 282:1897-1900(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1191-1982.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-83; SER-201; SER-204;
RP SER-210; SER-221; SER-284; SER-285; SER-292; SER-295; SER-299; SER-310;
RP SER-313; TYR-701; THR-702; SER-1691 AND SER-1694, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH HDAC1,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18250149; DOI=10.1128/mcb.01839-07;
RA Murawska M., Kunert N., van Vugt J., Laengst G., Kremmer E., Logie C.,
RA Brehm A.;
RT "dCHD3, a novel ATP-dependent chromatin remodeler associated with sites of
RT active transcription.";
RL Mol. Cell. Biol. 28:2745-2757(2008).
CC -!- FUNCTION: Helicase which acts in nucleosome-remodeling by catalyzing
CC ATP-dependent nucleosome mobilization (PubMed:18250149). Involved in
CC regulating transcription (PubMed:9836641, PubMed:18250149). Plays a
CC vital role in development (PubMed:9836641). Binds to a portion of
CC Hunchback (HB) protein that is critical for repression of bithorax
CC complex (BXC) genes (PubMed:9836641). May also function in polycomb
CC group (PcG) repression of Hox genes (PubMed:9836641). May also act as
CC part of the nucleosome remodeling and deacetylase complex (the NuRD
CC complex) which participates in the remodeling of chromatin by
CC deacetylating histones (PubMed:18250149). {ECO:0000269|PubMed:18250149,
CC ECO:0000269|PubMed:9836641}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000269|PubMed:18250149};
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by binding to either
CC DNA or nucleosomes. {ECO:0000269|PubMed:18250149}.
CC -!- SUBUNIT: Interacts with the NuRD complex member HDAC1/Rpd3.
CC {ECO:0000269|PubMed:18250149}.
CC -!- INTERACTION:
CC O97159; Q9VZ27: CDK2AP1; NbExp=4; IntAct=EBI-112333, EBI-196367;
CC O97159; Q0E8J0: MEP-1; NbExp=13; IntAct=EBI-112333, EBI-91014;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18250149}. Chromosome
CC {ECO:0000269|PubMed:18250149}. Note=During embryogenesis, detected in
CC nuclei before and after their migration to the membrane of the
CC preblastoderm embryo (PubMed:18250149). Expression is diffuse in
CC mitotic nuclei and is still detectable in nuclei at postgastrulation
CC (PubMed:18250149). In polytene chromosomes of third instar larvae,
CC weakly expressed at the chromocenter and fourth chromosome
CC (PubMed:18250149). {ECO:0000269|PubMed:18250149}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, with levels peaking around 6
CC to 9 hours after egg deposition, and then sharply decreases becoming
CC undetectable at the first larval stage (at protein level)
CC (PubMed:18250149). Reappears at the pupal stage when it is weakly
CC expressed (at protein level) (PubMed:18250149). Strongly expressed in
CC adult females but expression is low to absent in adult males (at
CC protein level) (PubMed:18250149). {ECO:0000269|PubMed:18250149}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM29373.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF119716; AAD17276.1; -; mRNA.
DR EMBL; AE014296; AAF49099.2; -; Genomic_DNA.
DR EMBL; AY113368; AAM29373.1; ALT_INIT; mRNA.
DR RefSeq; NP_001163476.1; NM_001170005.2.
DR RefSeq; NP_649154.2; NM_140897.4.
DR AlphaFoldDB; O97159; -.
DR SMR; O97159; -.
DR BioGRID; 65438; 56.
DR DIP; DIP-22862N; -.
DR IntAct; O97159; 220.
DR MINT; O97159; -.
DR STRING; 7227.FBpp0099808; -.
DR iPTMnet; O97159; -.
DR PaxDb; O97159; -.
DR PRIDE; O97159; -.
DR EnsemblMetazoa; FBtr0074919; FBpp0074688; FBgn0262519.
DR EnsemblMetazoa; FBtr0302046; FBpp0291256; FBgn0262519.
DR GeneID; 40170; -.
DR KEGG; dme:Dmel_CG8103; -.
DR CTD; 40170; -.
DR FlyBase; FBgn0262519; Mi-2.
DR VEuPathDB; VectorBase:FBgn0262519; -.
DR eggNOG; KOG0383; Eukaryota.
DR GeneTree; ENSGT00940000169383; -.
DR HOGENOM; CLU_000315_22_3_1; -.
DR InParanoid; O97159; -.
DR PhylomeDB; O97159; -.
DR Reactome; R-DME-3214815; HDACs deacetylate histones.
DR Reactome; R-DME-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
DR SignaLink; O97159; -.
DR BioGRID-ORCS; 40170; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Mi-2; fly.
DR GenomeRNAi; 40170; -.
DR PRO; PR:O97159; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0262519; Expressed in egg cell and 24 other tissues.
DR ExpressionAtlas; O97159; baseline and differential.
DR Genevisible; O97159; DM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0016581; C:NuRD complex; ISS:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:FlyBase.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0140750; F:nucleosome array spacer activity; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0030261; P:chromosome condensation; IMP:FlyBase.
DR GO; GO:0051276; P:chromosome organization; IMP:CACAO.
DR GO; GO:0071923; P:negative regulation of cohesin loading; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IGI:UniProtKB.
DR GO; GO:0034728; P:nucleosome organization; IDA:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF06461; DUF1086; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Chromosome; DNA-binding; Helicase; Hydrolase; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1982
FT /note="Chromodomain-helicase-DNA-binding protein Mi-2
FT homolog"
FT /id="PRO_0000080236"
FT DOMAIN 488..566
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 612..673
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 742..924
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1056..1218
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 377..424
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 437..484
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1536..1715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 875..878
FT /note="DEAH box"
FT COMPBIAS 1..21
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..74
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..268
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1568..1670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 755..762
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 701
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 702
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1691
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1694
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 737
FT /note="G->D: In allele MI-2-5; larval lethal."
FT /evidence="ECO:0000269|PubMed:9836641"
FT CONFLICT 101
FT /note="G -> A (in Ref. 1; AAD17276)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1982 AA; 224201 MW; ED8E256D1AD0AC2F CRC64;
MASEEENDDN FQEEEEAQED NAPAAELSND SDAPLKPNND EDDDYDPEDS RRKKKGKKRK
TRKGEEKGRK KKKRKKNESE EDSDFVQHDE EVEYPSTSKR GRKRKEEKQA AKEKESASSG
MPSVEDVCSA FSVCNVEIEY SEEELQSLTT YKAFMHHVRP ILQKENPKIA APKLVMLVAA
KWREFCESNP HIQQEGGAAG SGGSAGQARS VTGDEPEEPR SSRSSRNEKP DDIYEEAVEE
EEEEEEEEKK PRRKRSGRGK KGRRPSGKVP TLKIKLLGKR KRDSSDEEQD ASGASERDSD
LEFERMLQKS DDSADEKEAP VSSKADNSAP AAQDDGSGAP VVRKKAKTKI GNKFKKKNKL
KKTKNFPEGE DGEHEHQDYC EVCQQGGEII LCDTCPRAYH LVCLEPELDE PPEGKWSCPH
CEADGGAAEE EDDDEHQEFC RVCKDGGELL CCDSCPSAYH TFCLNPPLDT IPDGDWRCPR
CSCPPLTGKA EKIITWRWAQ RSNDDGPSTS KGSKNSNSRV REYFIKWHNM SYWHCEWVPE
VQLDVHHPLM IRSFQRKYDM EEPPKFEESL DEADTRYKRI QRHKDKVGMK ANDDAEVLEE
RFYKNGVKPE WLIVQRVINH RTARDGSTMY LVKWRELPYD KSTWEEEGDD IQGLRQAIDY
YQDLRAVCTS ETTQSRSKKS KKGRKSKLKV EDDEDRPVKH YTPPPEKPTT DLKKKYEDQP
AFLEGTGMQL HPYQIEGINW LRYSWGQGID TILADEMGLG KTIQTVTFLY SLYKEGHCRG
PFLVAVPLST LVNWEREFEL WAPDFYCITY IGDKDSRAVI RENELSFEEG AIRGSKVSRL
RTTQYKFNVL LTSYELISMD AACLGSIDWA VLVVDEAHRL KSNQSKFFRI LNSYTIAYKL
LLTGTPLQNN LEELFHLLNF LSRDKFNDLQ AFQGEFADVS KEEQVKRLHE MLGPHMLRRL
KTDVLKNMPS KSEFIVRVEL SAMQKKFYKF ILTKNYEALN SKSGGGSCSL INIMMDLKKC
CNHPYLFPSA AEEATTAAGG LYEINSLTKA AGKLVLLSKM LKQLKAQNHR VLIFSQMTKM
LDILEDFLEG EQYKYERIDG GITGTLRQEA IDRFNAPGAQ QFVFLLSTRA GGLGINLATA
DTVIIYDSDW NPHNDIQAFS RAHRIGQANK VMIYRFVTRN SVEERVTQVA KRKMMLTHLV
VRPGMGGKGA NFTKQELDDI LRFGTEDLFK EDDKEEAIHY DDKAVAELLD RTNRGIEEKE
SWANEYLSSF KVASYATKEE EEEEETEIIK QDAENSDPAY WVKLLRHHYE QHQEDVGRSL
GKGKRVRKQV NYTDGGVVAA DTTRDDSNWQ DNGSEYNSEY SAGSDEDGGD DDFDDQNGAE
RKAKRRLERR DDRPLPPLLA RVGGNIEVLG FNARQRKSFL NAIMRYGMPP QDAFNSQWLV
RDLRGKSERN FKAYVSLFMR HLCEPGADNA ETFADGVPRE GLSRQHVLTR IGVMSLIRKK
VQEFEHINGY YSMPELILKP CEPVRSALKQ DVAALEAPPT GGNVDKSATT SNSVTPATSA
APSPAPASEK GEDKDKDSEK EKDKTSAEKS EVKQEQEAEE DKKPGDVKQE NPVEEAAGDT
KPSDAEVKTE VAKTEPKEET KDPEVKEEPK TEEKEKEKVD DKKPIPPTTV IDDDDDDVMI
VKEDGELEKP SASSPKDQKA VAAATSAATG ATGKGAEDSL EVLKRKFMFN IADGGFTELH
TLWLNEEKAA VPGREYEIWH RRHDYWLLAG IVTHGYGRWQ DIQNDIRFAI INEPFKMDVG
KGNFLEIKNK FLARRFKLLE QALVIEEQLR RAAYLNLAQD PSHPAMSLNA RFAEVECLAE
SHQHLSKESL AGNKPANAVL HKVLNQLEEL LSDMKSDVSR LPATLARIPP VAQRLQMSER
SILSRLAATA GNASNAAQLM AQFPAGFQGT TLPAFTSGPA GNFANFRPQF SVPGQLSNNS
GV
