FTZF1_DROME
ID FTZF1_DROME Reviewed; 1027 AA.
AC P33244; B9EQU1; Q24538; Q8IQT5; Q960U2; Q9VVS8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Nuclear hormone receptor FTZ-F1;
DE AltName: Full=FTZ-F1 alpha;
DE AltName: Full=Nuclear receptor subfamily 5 group A member 3;
GN Name=ftz-f1; Synonyms=NR5A3; ORFNames=CG4059;
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] (ISOFORM B), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1709303; DOI=10.1126/science.1709303;
RA Lavorgna G., Ueda H., Clos J., Wu C.;
RT "FTZ-F1, a steroid hormone receptor-like protein implicated in the
RT activation of fushi tarazu.";
RL Science 252:848-851(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=8096644; DOI=10.1073/pnas.90.7.3004;
RA Lavorgna G., Karim F.D., Thummel C.S., Wu C.;
RT "Potential role for a TZ-F1 steroid receptor superfamily member in the
RT control of Drosophila metamorphosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3004-3008(1993).
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 601-1027.
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 [7]
RP DNA-BINDING, SUBUNIT, AND MUTAGENESIS OF CYS-563; ARG-579; ARG-582;
RP MET-583; ARG-584; 585-GLY--GLY-586; ARG-587 AND LYS-589.
RX PubMed=1448096; DOI=10.1128/mcb.12.12.5667-5672.1992;
RA Ueda H., Sun G.-C., Murata T., Hirose S.;
RT "A novel DNA-binding motif abuts the zinc finger domain of insect nuclear
RT hormone receptor FTZ-F1 and mouse embryonal long terminal repeat-binding
RT protein.";
RL Mol. Cell. Biol. 12:5667-5672(1992).
RN [8]
RP DNA-BINDING, AND SUBUNIT.
RX PubMed=8164672; DOI=10.1128/mcb.14.5.3166-3175.1994;
RA Ohno C.K., Ueda H., Petkovich M.;
RT "The Drosophila nuclear receptors FTZ-F1 alpha and FTZ-F1 beta compete as
RT monomers for binding to a site in the fushi tarazu gene.";
RL Mol. Cell. Biol. 14:3166-3175(1994).
RN [9]
RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9020363; DOI=10.1038/385548a0;
RA Guichet A., Copeland J.W.R., Erdelyi M., Hlousek D., Zavorszky P., Ho J.,
RA Brown S., Percival-Smith A., Krause H.M., Ephrussi A.;
RT "The nuclear receptor homologue Ftz-F1 and the homeodomain protein Ftz are
RT mutually dependent cofactors.";
RL Nature 385:548-552(1997).
RN [10]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=9020364; DOI=10.1038/385552a0;
RA Yu Y., Li W., Su K., Yussa M., Han W., Perrimon N., Pick L.;
RT "The nuclear hormone receptor Ftz-F1 is a cofactor for the Drosophila
RT homeodomain protein Ftz.";
RL Nature 385:552-555(1997).
CC -!- FUNCTION: Acts as a cofactor to fushi tarazu (ftz). Facilitates the
CC binding of ftz to DNA. Binds the sequence element 5'-YCYYGGYCR-3' in
CC the zebra element of ftz. Probably also functions as a receptor for a
CC yet unknown ligand. {ECO:0000269|PubMed:9020363,
CC ECO:0000269|PubMed:9020364}.
CC -!- SUBUNIT: Monomer; forms a complex with ftz.
CC {ECO:0000269|PubMed:1448096, ECO:0000269|PubMed:8164672,
CC ECO:0000269|PubMed:9020363, ECO:0000269|PubMed:9020364}.
CC -!- INTERACTION:
CC P33244; P02835: ftz; NbExp=3; IntAct=EBI-160447, EBI-125786;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=P33244-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P33244-2; Sequence=VSP_012917, VSP_012918;
CC -!- TISSUE SPECIFICITY: Expression in the parasegmental primordia of the
CC embryonic blastoderm. {ECO:0000269|PubMed:9020363}.
CC -!- DEVELOPMENTAL STAGE: First appears in blastoderm embryos. It is absent
CC in subsequent embryo stages, and then reappears in late embryogenesis
CC to be found in larvae, pupae and adults. {ECO:0000269|PubMed:9020363}.
CC -!- DISRUPTION PHENOTYPE: Ftz-like pair-rule cuticular defects.
CC {ECO:0000269|PubMed:9020364}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR5
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28542.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA28915.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAK93269.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M63711; AAA28542.1; ALT_FRAME; mRNA.
DR EMBL; M98397; AAA28915.1; ALT_FRAME; mRNA.
DR EMBL; AE014296; AAF49231.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN11667.1; -; Genomic_DNA.
DR EMBL; BT058016; ACM16732.1; -; mRNA.
DR EMBL; AY051845; AAK93269.1; ALT_INIT; mRNA.
DR PIR; A47303; A47303.
DR PIR; T13733; T13733.
DR RefSeq; NP_001246824.1; NM_001259895.2. [P33244-2]
DR RefSeq; NP_524143.2; NM_079419.3. [P33244-1]
DR RefSeq; NP_730359.1; NM_168775.2. [P33244-2]
DR PDB; 2XHS; X-ray; 2.80 A; A=790-1027.
DR PDBsum; 2XHS; -.
DR AlphaFoldDB; P33244; -.
DR SMR; P33244; -.
DR BioGRID; 65326; 46.
DR IntAct; P33244; 7.
DR STRING; 7227.FBpp0074853; -.
DR PaxDb; P33244; -.
DR DNASU; 40045; -.
DR EnsemblMetazoa; FBtr0075086; FBpp0074853; FBgn0001078. [P33244-1]
DR EnsemblMetazoa; FBtr0075087; FBpp0074854; FBgn0001078. [P33244-2]
DR EnsemblMetazoa; FBtr0304627; FBpp0293169; FBgn0001078. [P33244-2]
DR GeneID; 40045; -.
DR KEGG; dme:Dmel_CG4059; -.
DR CTD; 40045; -.
DR FlyBase; FBgn0001078; ftz-f1.
DR VEuPathDB; VectorBase:FBgn0001078; -.
DR eggNOG; KOG4218; Eukaryota.
DR GeneTree; ENSGT00940000153391; -.
DR HOGENOM; CLU_011437_2_0_1; -.
DR InParanoid; P33244; -.
DR OMA; LDYCITA; -.
DR PhylomeDB; P33244; -.
DR Reactome; R-DME-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-DME-4090294; SUMOylation of intracellular receptors.
DR SignaLink; P33244; -.
DR BioGRID-ORCS; 40045; 1 hit in 3 CRISPR screens.
DR ChiTaRS; ftz-f1; fly.
DR GenomeRNAi; 40045; -.
DR PRO; PR:P33244; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0001078; Expressed in cleaving embryo and 32 other tissues.
DR ExpressionAtlas; P33244; baseline and differential.
DR Genevisible; P33244; DM.
DR GO; GO:0005737; C:cytoplasm; NAS:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0004879; F:nuclear receptor activity; NAS:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:FlyBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008219; P:cell death; TAS:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0002165; P:instar larval or pupal development; IMP:FlyBase.
DR GO; GO:0035626; P:juvenile hormone mediated signaling pathway; IMP:FlyBase.
DR GO; GO:0055088; P:lipid homeostasis; IMP:FlyBase.
DR GO; GO:0007552; P:metamorphosis; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0035073; P:pupariation; IMP:FlyBase.
DR GO; GO:0035074; P:pupation; IMP:FlyBase.
DR GO; GO:0040034; P:regulation of development, heterochronic; TAS:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0035075; P:response to ecdysone; TAS:FlyBase.
DR GO; GO:0009725; P:response to hormone; TAS:FlyBase.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID50244; -.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR016355; NR5_fam.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR24086; PTHR24086; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Direct protein sequencing;
KW DNA-binding; Metal-binding; Nucleus; Receptor; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1027
FT /note="Nuclear hormone receptor FTZ-F1"
FT /id="PRO_0000053739"
FT DOMAIN 792..1024
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 505..580
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 508..528
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 544..568
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 20..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..174
FT /note="MDTFNVPMLAESSNTNYATEATSNHHHLQHQHQQQHSHQQQQQQQLLMPHHH
FT KDQMLAAGSSPMLPFYSHLQLQQKDATATIGPAAAAAAVEAATTSANADNFSSLQTIDA
FT SQLDGGISLSGLCDRFFVASPNPHSNSNMTLMGTATAATTTTTNNNNNNNTNNNNNNNV
FT EAKT -> MLLEMDQQQATVQFISSLNISPFSMQLEQQQQPSSPALAAGGNSSNNAASG
FT SNNNSASGNNTSSSSNNNNNNNNDNDAHVLTKFEHEYNAYTLQLAGGGGSGSGNQQHHS
FT NHSNHGNHHQQQQQQQQQQQQHQQQQQEHYQQQQQQNIANNANQFNSSSYSYIYNFDSQ
FT YIFPT (in isoform A)"
FT /evidence="ECO:0000303|PubMed:8096644"
FT /id="VSP_012917"
FT VAR_SEQ 175..398
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:8096644"
FT /id="VSP_012918"
FT MUTAGEN 563
FT /note="C->S: 100-fold less binding."
FT /evidence="ECO:0000269|PubMed:1448096"
FT MUTAGEN 579
FT /note="R->Q: 100-fold less binding."
FT /evidence="ECO:0000269|PubMed:1448096"
FT MUTAGEN 582
FT /note="R->Q: 100-fold less binding."
FT /evidence="ECO:0000269|PubMed:1448096"
FT MUTAGEN 583
FT /note="M->I: 10-fold less binding."
FT /evidence="ECO:0000269|PubMed:1448096"
FT MUTAGEN 584
FT /note="R->Q: 10-fold less binding."
FT /evidence="ECO:0000269|PubMed:1448096"
FT MUTAGEN 585..586
FT /note="GG->AA: No binding."
FT /evidence="ECO:0000269|PubMed:1448096"
FT MUTAGEN 587
FT /note="R->Q: 10-fold less reduced binding."
FT /evidence="ECO:0000269|PubMed:1448096"
FT MUTAGEN 589
FT /note="K->Q: No effect on binding."
FT /evidence="ECO:0000269|PubMed:1448096"
FT CONFLICT 45
FT /note="Q -> QQQ (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="R -> S (in Ref. 1; AAA28542)"
FT /evidence="ECO:0000305"
FT CONFLICT 752..753
FT /note="GN -> DS (in Ref. 1; AAA28542 and 2; AAA28915)"
FT /evidence="ECO:0000305"
FT CONFLICT 832
FT /note="L -> LL (in Ref. 1; AAA28542 and 2; AAA28915)"
FT /evidence="ECO:0000305"
FT CONFLICT 912
FT /note="L -> P (in Ref. 1; AAA28542 and 2; AAA28915)"
FT /evidence="ECO:0000305"
FT HELIX 790..792
FT /evidence="ECO:0007829|PDB:2XHS"
FT HELIX 795..802
FT /evidence="ECO:0007829|PDB:2XHS"
FT HELIX 806..821
FT /evidence="ECO:0007829|PDB:2XHS"
FT HELIX 829..849
FT /evidence="ECO:0007829|PDB:2XHS"
FT HELIX 854..856
FT /evidence="ECO:0007829|PDB:2XHS"
FT HELIX 859..884
FT /evidence="ECO:0007829|PDB:2XHS"
FT STRAND 889..892
FT /evidence="ECO:0007829|PDB:2XHS"
FT STRAND 894..896
FT /evidence="ECO:0007829|PDB:2XHS"
FT STRAND 898..900
FT /evidence="ECO:0007829|PDB:2XHS"
FT HELIX 901..905
FT /evidence="ECO:0007829|PDB:2XHS"
FT TURN 906..908
FT /evidence="ECO:0007829|PDB:2XHS"
FT HELIX 910..912
FT /evidence="ECO:0007829|PDB:2XHS"
FT HELIX 913..925
FT /evidence="ECO:0007829|PDB:2XHS"
FT HELIX 930..941
FT /evidence="ECO:0007829|PDB:2XHS"
FT HELIX 952..973
FT /evidence="ECO:0007829|PDB:2XHS"
FT HELIX 980..1007
FT /evidence="ECO:0007829|PDB:2XHS"
FT STRAND 1013..1015
FT /evidence="ECO:0007829|PDB:2XHS"
FT HELIX 1016..1022
FT /evidence="ECO:0007829|PDB:2XHS"
FT CONFLICT P33244-2:67..68
FT /note="NN -> N (in Ref. 2; AAA28915)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1027 AA; 108418 MW; 6A2240934830290D CRC64;
MDTFNVPMLA ESSNTNYATE ATSNHHHLQH QHQQQHSHQQ QQQQQLLMPH HHKDQMLAAG
SSPMLPFYSH LQLQQKDATA TIGPAAAAAA VEAATTSANA DNFSSLQTID ASQLDGGISL
SGLCDRFFVA SPNPHSNSNM TLMGTATAAT TTTTNNNNNN NTNNNNNNNV EAKTVRPSNG
NSVIIESVTM PSFANILFPT HRSANECIDP ALLQKNPQNP NGNNSSIIVP PVEYHQLKPL
EVNSSTSVST SNFLSSTTAQ LLDFEVQVGK DDGHISTTTT TGPGSGSASG SGSGSGSGSG
SIARTIGTAT PTTTTSMSNT ANPTRSSLHS IEELAASSCA PRAASPNSNH TSSASTTPQQ
QQQQQHHMQS GNHSGSNLSS DDESMSEDEF GLEIDDNGGY QDTTSSHSQQ SGGGGGGGGG
NLLNGSSGGS SAGGGYMLLP QAASSSGNNG NPNAGHMSSG SVGNGSGGAG NGGAGGNSGP
GNPMGGTSAT PGHGGEVIDF KHLFEELCPV CGDKVSGYHY GLLTCESCKG FFKRTVQNKK
VYTCVAERSC HIDKTQRKRC PYCRFQKCLE VGMKLEAVRA DRMRGGRNKF GPMYKRDRAR
KLQVMRQRQL ALQALRNSMG PDIKPTPISP GYQQAYPNMN IKQEIQIPQV SSLTQSPDSS
PSPIAIALGQ VNASTGGVIA TPMNAGTGGS GGGGLNGPSS VGNGNSSNGS SNGNNNSSTG
NGTSGGGGGN NAGGGGGGTN SNDGLHRNGG NGNSSCHEAG IGSLQNTADS KLCFDSGTHP
SSTADALIEP LRVSPMIREF VQSIDDREWQ TQLFALLQKQ TYNQVEVDLF ELMCKVLDQN
LFSQVDWARN TVFFKDLKVD DQMKLLQHSW SDMLVLDHLH HRIHNGLPDE TQLNNGQVFN
LMSLGLLGVP QLGDYFNELQ NKLQDLKFDM GDYVCMKFLI LLNPSVRGIV NRKTVSEGHD
NVQAALLDYT LTCYPSVNDK FRGLVNILPE IHAMAVRGED HLYTKHCAGS APTQTLLMEM
LHAKRKG
