ISWI_DROME
ID ISWI_DROME Reviewed; 1027 AA.
AC Q24368; A4UZF0; B5X0J3; Q0E9A4; Q8SX14; Q9V6E8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Chromatin-remodeling complex ATPase chain Iswi;
DE EC=3.6.4.-;
DE AltName: Full=CHRAC 140 kDa subunit;
DE AltName: Full=Nucleosome-remodeling factor 140 kDa subunit;
DE Short=NURF-140;
DE AltName: Full=Protein imitation swi;
GN Name=Iswi; ORFNames=CG8625;
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].
RC STRAIN=Iso-1; TISSUE=Embryo;
RX PubMed=7908117; DOI=10.1128/mcb.14.4.2225-2234.1994;
RA Elfring L.K., Deuring R., McCallum C.M., Peterson C.L., Tamkun J.W.;
RT "Identification and characterization of Drosophila relatives of the yeast
RT transcriptional activator SNF2/SWI2.";
RL Mol. Cell. Biol. 14:2225-2234(1994).
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].
RC STRAIN=Berkeley; TISSUE=Head;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 95-124; 175-186; 578-610 AND 775-787, IDENTIFICATION IN
RP THE NURF COMPLEX, FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=8521502; DOI=10.1016/0092-8674(95)90217-1;
RA Tsukiyama T., Daniel C., Tamkun J., Wu C.;
RT "ISWI, a member of the SWI2/SNF2 ATPase family, encodes the 140 kDa subunit
RT of the nucleosome remodeling factor.";
RL Cell 83:1021-1026(1995).
RN [7]
RP FUNCTION.
RX PubMed=8521501; DOI=10.1016/0092-8674(95)90216-3;
RA Tsukiyama T., Wu C.;
RT "Purification and properties of an ATP-dependent nucleosome remodeling
RT factor.";
RL Cell 83:1011-1020(1995).
RN [8]
RP IDENTIFICATION IN THE CHRAC COMPLEX, FUNCTION, AND INTERACTION WITH
RP CHRAC-14 AND CHRAC-16.
RX PubMed=10856248; DOI=10.1093/emboj/19.12.3049;
RA Corona D.F., Eberharter A., Budde A., Deuring R., Ferrari S.,
RA Varga-Weisz P., Wilm M., Tamkun J., Becker P.B.;
RT "Two histone fold proteins, CHRAC-14 and CHRAC-16, are developmentally
RT regulated subunits of chromatin accessibility complex (CHRAC).";
RL EMBO J. 19:3049-3059(2000).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE CHRAC COMPLEX, AND INTERACTION WITH
RP CHRAC-16.
RX PubMed=11447119; DOI=10.1093/emboj/20.14.3781;
RA Eberharter A., Ferrari S., Laengst G., Straub T., Imhof A., Varga-Weisz P.,
RA Wilm M., Becker P.B.;
RT "Acf1, the largest subunit of CHRAC, regulates ISWI-induced nucleosome
RT remodelling.";
RL EMBO J. 20:3781-3788(2001).
RN [10]
RP FUNCTION.
RX PubMed=12502740; DOI=10.1101/gad.1032202;
RA Badenhorst P., Voas M., Rebay I., Wu C.;
RT "Biological functions of the ISWI chromatin remodeling complex NURF.";
RL Genes Dev. 16:3186-3198(2002).
RN [11]
RP FUNCTION.
RX PubMed=16264191; DOI=10.1101/gad.1342605;
RA Badenhorst P., Xiao H., Cherbas L., Kwon S.Y., Voas M., Rebay I.,
RA Cherbas P., Wu C.;
RT "The Drosophila nucleosome remodeling factor NURF is required for
RT Ecdysteroid signaling and metamorphosis.";
RL Genes Dev. 19:2540-2545(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, 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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 688-991.
RX PubMed=14536084; DOI=10.1016/s1097-2765(03)00273-9;
RA Grune T., Brzeski J., Eberharter A., Clapier C.R., Corona D.F.V.,
RA Becker P.B., Mueller C.W.;
RT "Crystal structure and functional analysis of a nucleosome recognition
RT module of the remodeling factor ISWI.";
RL Mol. Cell 12:449-460(2003).
CC -!- FUNCTION: Energy-transducing component of the chromatin-remodeling
CC complexes NURF (nucleosome-remodeling factor), ACF (ATP-utilizing
CC chromatin assembly and remodeling factor), and CHRAC (chromatin
CC accessibility complex) (PubMed:10856248, PubMed:11447119). NURF
CC catalyzes ATP-dependent nucleosome sliding and facilitates
CC transcription of chromatin. It is required for homeotic gene
CC expression, proper larval blood cell development, normal male X
CC chromosome morphology, ecdysteroid signaling and metamorphosis
CC (PubMed:12502740, PubMed:16264191, PubMed:8521501, PubMed:8521502).
CC {ECO:0000269|PubMed:10856248, ECO:0000269|PubMed:11447119,
CC ECO:0000269|PubMed:12502740, ECO:0000269|PubMed:16264191,
CC ECO:0000269|PubMed:8521501, ECO:0000269|PubMed:8521502}.
CC -!- SUBUNIT: Component of the NURF complex composed of Caf1-55, E(bx),
CC Nurf-38 and Iswi (PubMed:8521502). Component of the chromatin
CC accessibility complex (CHRAC), composed of Chrac-14, Chrac-16, Acf and
CC Iswi (PubMed:10856248, PubMed:11447119). Interacts directly with Chrac-
CC 14 and this interaction is further stabilized by associated Chrac-16
CC (PubMed:10856248). {ECO:0000269|PubMed:10856248,
CC ECO:0000269|PubMed:11447119, ECO:0000269|PubMed:8521502}.
CC -!- INTERACTION:
CC Q24368; P18824: arm; NbExp=2; IntAct=EBI-367628, EBI-216128;
CC Q24368; P35875: Parp; NbExp=4; IntAct=EBI-367628, EBI-266172;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC ECO:0000269|PubMed:8521502}.
CC -!- DEVELOPMENTAL STAGE: Present throughout embryonic, larval and pupal
CC development and in female adults. Present at low levels in adult males
CC (at protein level). {ECO:0000269|PubMed:8521502}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000305}.
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DR EMBL; L27127; AAA19868.1; -; mRNA.
DR EMBL; AE013599; AAF58479.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68638.1; -; Genomic_DNA.
DR EMBL; AY094908; AAM11261.1; -; mRNA.
DR EMBL; BT044562; ACI15757.1; -; mRNA.
DR PIR; A56533; A56533.
DR RefSeq; NP_523719.1; NM_078995.2.
DR RefSeq; NP_725203.1; NM_165930.2.
DR RefSeq; NP_725204.1; NM_165931.2.
DR PDB; 1OFC; X-ray; 1.90 A; X=691-991.
DR PDBsum; 1OFC; -.
DR AlphaFoldDB; Q24368; -.
DR SMR; Q24368; -.
DR BioGRID; 62163; 59.
DR DIP; DIP-24067N; -.
DR IntAct; Q24368; 8.
DR MINT; Q24368; -.
DR STRING; 7227.FBpp0086954; -.
DR iPTMnet; Q24368; -.
DR PaxDb; Q24368; -.
DR PRIDE; Q24368; -.
DR DNASU; 36390; -.
DR EnsemblMetazoa; FBtr0087841; FBpp0086954; FBgn0011604.
DR EnsemblMetazoa; FBtr0087842; FBpp0086955; FBgn0011604.
DR EnsemblMetazoa; FBtr0087843; FBpp0086956; FBgn0011604.
DR GeneID; 36390; -.
DR KEGG; dme:Dmel_CG8625; -.
DR CTD; 36390; -.
DR FlyBase; FBgn0011604; Iswi.
DR VEuPathDB; VectorBase:FBgn0011604; -.
DR eggNOG; KOG0385; Eukaryota.
DR GeneTree; ENSGT00940000157297; -.
DR HOGENOM; CLU_000315_0_3_1; -.
DR InParanoid; Q24368; -.
DR OMA; IHDWQFF; -.
DR OrthoDB; 61251at2759; -.
DR PhylomeDB; Q24368; -.
DR SignaLink; Q24368; -.
DR BioGRID-ORCS; 36390; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Iswi; fly.
DR EvolutionaryTrace; Q24368; -.
DR GenomeRNAi; 36390; -.
DR PRO; PR:Q24368; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0011604; Expressed in wing disc and 39 other tissues.
DR ExpressionAtlas; Q24368; baseline and differential.
DR Genevisible; Q24368; DM.
DR GO; GO:0016590; C:ACF complex; IDA:FlyBase.
DR GO; GO:0008623; C:CHRAC; IDA:FlyBase.
DR GO; GO:0031010; C:ISWI-type complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0016589; C:NURF complex; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0031213; C:RSF complex; IPI:FlyBase.
DR GO; GO:0005667; C:transcription regulator complex; IPI:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:FlyBase.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:FlyBase.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0140751; F:histone octamer slider activity; IDA:FlyBase.
DR GO; GO:0140750; F:nucleosome array spacer activity; IDA:FlyBase.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; TAS:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IDA:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR GO; GO:0035076; P:ecdysone receptor-mediated signaling pathway; IGI:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0035063; P:nuclear speck organization; IMP:FlyBase.
DR GO; GO:0006334; P:nucleosome assembly; IDA:FlyBase.
DR GO; GO:0034728; P:nucleosome organization; IDA:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0035092; P:sperm DNA condensation; IMP:FlyBase.
DR GO; GO:0035041; P:sperm DNA decondensation; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.1040.30; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR020838; DBINO.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF13892; DBINO; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; SSF101224; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromatin regulator; Direct protein sequencing;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1027
FT /note="Chromatin-remodeling complex ATPase chain Iswi"
FT /id="PRO_0000074333"
FT DOMAIN 140..305
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 435..586
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 795..847
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 898..962
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 256..259
FT /note="DEAH box"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 645
FT /note="E -> D (in Ref. 4; AAM11261)"
FT /evidence="ECO:0000305"
FT HELIX 698..705
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 727..729
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 733..749
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 766..776
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 783..792
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 802..815
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 820..823
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 832..845
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 846..848
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 852..881
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 886..889
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 904..917
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 924..934
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 936..938
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 942..945
FT /evidence="ECO:0007829|PDB:1OFC"
FT HELIX 949..974
FT /evidence="ECO:0007829|PDB:1OFC"
SQ SEQUENCE 1027 AA; 118873 MW; 008FC81AE15E071F CRC64;
MSKTDTAAVE ATEENSNETT SDAATSSSGE KEAEFDNKIE ADRSRRFDFL LKQTEIFTHF
MTNSAKSPTK PKGRPKKIKD KDKEKDVADH RHRKTEQEED EELLAEDSAT KEIFRFDASP
AYIKSGEMRD YQIRGLNWMI SLYENGINGI LADEMGLGKT LQTISLLGYL KHFKNQAGPH
IVIVPKSTLQ NWVNEFKKWC PSLRAVCLIG DQDTRNTFIR DVLMPGEWDV CVTSYEMCIR
EKSVFKKFNW RYLVIDEAHR IKNEKSKLSE ILREFKTANR LLITGTPLQN NLHELWALLN
FLLPDVFNSS EDFDEWFNTN TCLGDDALIT RLHAVLKPFL LRRLKAEVEK RLKPKKEMKI
FVGLSKMQRD WYTKVLLKDI DVVNGAGKVE KMRLQNILMQ LRKCTNHPYL FDGAEPGPPY
TTDTHLVYNS GKMAILDKLL PKLQEQGSRV LIFSQMTRML DILEDYCHWR NYNYCRLDGQ
TPHEDRNRQI QEFNMDNSAK FLFMLSTRAG GLGINLATAD VVIIYDSDWN PQMDLQAMDR
AHRIGQKKQV RVFRLITEST VEEKIVERAE VKLRLDKMVI QGGRLVDNRS NQLNKDEMLN
IIRFGANQVF SSKETDITDE DIDVILERGE AKTAEQKAAL DSLGESSLRT FTMDTNGEAG
TSSVYQFEGE DWREKQKLNA LGNWIEPPKR ERKANYAVDA YFREALRVSE PKAPKAPRPP
KQPIVQDFQF FPPRLFELLD QEIYYFRKTV GYKVPKNTEL GSDATKVQRE EQRKIDEAEP
LTEEEIQEKE NLLSQGFTAW TKRDFNQFIK ANEKYGRDDI DNIAKDVEGK TPEEVIEYNA
VFWERCTELQ DIERIMGQIE RGEGKIQRRL SIKKALDQKM SRYRAPFHQL RLQYGNNKGK
NYTEIEDRFL VCMLHKLGFD KENVYEELRA AIRASPQFRF DWFIKSRTAL ELQRRCNTLI
TLIERENIEL EEKERAEKKK KAPKGSVSAG SGSASSNTPA PAPQPKASQK RKSEVVATSS
NSKKKKK
