UBX_DROME
ID UBX_DROME Reviewed; 389 AA.
AC P83949; P02834; Q9TX83; Q9VER4; Q9VER5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Homeotic protein ultrabithorax;
GN Name=Ubx; ORFNames=CG10388;
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 [GENOMIC DNA].
RC STRAIN=Canton-S;
RA Weinzierl R., Axton J.M., Ghysen A., Akam M.;
RT "Ultrabithorax mutations in constant and variable regions of the protein
RT coding sequence.";
RL Genes Dev. 1:386-397(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IA; IB; IIA; IIB; IVA AND IVB).
RX PubMed=2565858; DOI=10.1101/gad.3.2.243;
RA Kornfeld K., Saint R.B., Beachy P.A., Harte P.J., Peattie D.A.,
RA Hogness D.S.;
RT "Structure and expression of a family of Ultrabithorax mRNAs generated by
RT alternative splicing and polyadenylation in Drosophila.";
RL Genes Dev. 3:243-258(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS IA; IB; IIA; IIB AND IVA).
RC STRAIN=Canton-S;
RX PubMed=7667301; DOI=10.1073/pnas.92.18.8398;
RA Martin C.H., Mayeda C.A., Davis C.A., Ericsson C.L., Knafels J.D.,
RA Mathog D.R., Celniker S.E., Lewis E.B., Palazzolo M.J.;
RT "Complete sequence of the bithorax complex of Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8398-8402(1995).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IA).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 290-389.
RX PubMed=6327065; DOI=10.1016/0092-8674(84)90370-2;
RA McGinnis W., Garber R.L., Wirz J., Kuroiwa A., Gehring W.J.;
RT "A homologous protein-coding sequence in Drosophila homeotic genes and its
RT conservation in other metazoans.";
RL Cell 37:403-408(1984).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 290-384.
RX PubMed=6330741; DOI=10.1073/pnas.81.13.4115;
RA Scott M.P., Weiner A.J.;
RT "Structural relationships among genes that control development: sequence
RT homology between the Antennapedia, Ultrabithorax, and fushi tarazu loci of
RT Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4115-4119(1984).
RN [9]
RP NUCLEOTIDE SEQUENCE OF 294-355.
RX PubMed=8098307; DOI=10.1101/gad.7.5.796;
RA Chan S.K., Mann R.S.;
RT "The segment identity functions of Ultrabithorax are contained within its
RT homeo domain and carboxy-terminal sequences.";
RL Genes Dev. 7:796-811(1993).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RX PubMed=16453777; DOI=10.1002/j.1460-2075.1987.tb02430.x;
RA Saari G., Bienz M.;
RT "The structure of the ultrabithorax promoter of Drosophila melanogaster.";
RL EMBO J. 6:1775-1779(1987).
RN [11]
RP DNA-BINDING.
RX PubMed=1673656; DOI=10.1002/j.1460-2075.1991.tb08058.x;
RA Ekker S.C., Young K.E., von Kessler D.P., Beachy P.A.;
RT "Optimal DNA sequence recognition by the Ultrabithorax homeodomain of
RT Drosophila.";
RL EMBO J. 10:1179-1186(1991).
RN [12]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=7911773; DOI=10.1093/genetics/136.3.965;
RA Bomze H.M., Lopez A.J.;
RT "Evolutionary conservation of the structure and expression of alternatively
RT spliced Ultrabithorax isoforms from Drosophila.";
RL Genetics 136:965-977(1994).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170; SER-174 AND SER-177, AND
RP IDENTIFICATION BY 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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 233-356 IN COMPLEX WITH EXD.
RX PubMed=10067897; DOI=10.1038/17833;
RA Passner J.M., Ryoo H.-D., Shen L., Mann R.S., Aggarwal A.K.;
RT "Structure of a DNA-bound Ultrabithorax-Extradenticle homeodomain
RT complex.";
RL Nature 397:714-719(1999).
CC -!- FUNCTION: Sequence-specific transcription factor which is part of a
CC developmental regulatory system that provides cells with specific
CC positional identities on the anterior-posterior axis. Binds the
CC consensus region 5'-TTAAT[GT][GA]-3'. This homeotic protein controls
CC development of the cells in the posterior thoracic and first abdominal
CC segments. It activates the synthesis of the decapentaplegic (DPP)
CC growth factor.
CC -!- INTERACTION:
CC P83949; Q06453: al; NbExp=3; IntAct=EBI-202590, EBI-188244;
CC P83949; Q7K4N3: Cbp80; NbExp=3; IntAct=EBI-202590, EBI-137965;
CC P83949; P40427: exd; NbExp=5; IntAct=EBI-202590, EBI-101537;
CC P83949; P14003: h; NbExp=3; IntAct=EBI-202590, EBI-123011;
CC P83949-1; Q9TW27: DIP1; NbExp=7; IntAct=EBI-202571, EBI-443968;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=IB; Synonyms=A;
CC IsoId=P83949-1, P02834-1;
CC Sequence=Displayed;
CC Name=IA; Synonyms=E;
CC IsoId=P83949-2, P02834-2;
CC Sequence=VSP_002405;
CC Name=IIA; Synonyms=D;
CC IsoId=P83949-3, P02834-3;
CC Sequence=VSP_002406;
CC Name=IIB; Synonyms=C;
CC IsoId=P83949-4, P02834-4;
CC Sequence=VSP_002408;
CC Name=IVA; Synonyms=B;
CC IsoId=P83949-5, P02834-5;
CC Sequence=VSP_002407;
CC Name=IVB; Synonyms=F;
CC IsoId=P83949-6, P02834-6;
CC Sequence=VSP_002409;
CC -!- TISSUE SPECIFICITY: In the embryo, expression is seen in the epidermis,
CC somatic and visceral mesoderm, and the peripheral and central nervous
CC system. {ECO:0000269|PubMed:7911773}.
CC -!- DOMAIN: The QA motif is able to mediate transcriptional repression.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Antp homeobox family. {ECO:0000305}.
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DR EMBL; X05723; CAA29194.1; -; Genomic_DNA.
DR EMBL; X05724; CAA29194.1; JOINED; Genomic_DNA.
DR EMBL; X05725; CAA29194.1; JOINED; Genomic_DNA.
DR EMBL; X05727; CAA29194.1; JOINED; Genomic_DNA.
DR EMBL; X76210; CAA53803.1; -; mRNA.
DR EMBL; U31961; AAA84412.1; -; Genomic_DNA.
DR EMBL; U31961; AAA84411.1; -; Genomic_DNA.
DR EMBL; U31961; AAA84410.1; -; Genomic_DNA.
DR EMBL; U31961; AAA84409.1; -; Genomic_DNA.
DR EMBL; U31961; AAA84408.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55355.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF55356.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13717.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13718.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13719.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65158.1; -; Genomic_DNA.
DR EMBL; BT010241; AAQ23559.1; -; mRNA.
DR EMBL; K01963; AAA29008.1; ALT_SEQ; Genomic_DNA.
DR EMBL; K01959; AAA28615.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X05427; CAA29009.1; -; Genomic_DNA.
DR PIR; B27867; B27867.
DR PIR; D26995; D26995.
DR RefSeq; NP_536748.1; NM_080500.4. [P83949-5]
DR RefSeq; NP_536752.1; NM_080504.4. [P83949-1]
DR RefSeq; NP_732171.1; NM_169728.3. [P83949-3]
DR RefSeq; NP_732172.1; NM_169729.3. [P83949-2]
DR RefSeq; NP_732173.1; NM_169730.3. [P83949-4]
DR RefSeq; NP_996219.1; NM_206497.3. [P83949-6]
DR PDB; 1B8I; X-ray; 2.40 A; A=233-356.
DR PDB; 4CYC; X-ray; 2.36 A; A=233-367.
DR PDB; 4UUS; X-ray; 2.55 A; A/E=292-367.
DR PDB; 4UUT; X-ray; 2.80 A; A=233-367.
DR PDBsum; 1B8I; -.
DR PDBsum; 4CYC; -.
DR PDBsum; 4UUS; -.
DR PDBsum; 4UUT; -.
DR AlphaFoldDB; P83949; -.
DR SMR; P83949; -.
DR BioGRID; 67078; 259.
DR DIP; DIP-33048N; -.
DR IntAct; P83949; 28.
DR MINT; P83949; -.
DR STRING; 7227.FBpp0082793; -.
DR iPTMnet; P83949; -.
DR PaxDb; P83949; -.
DR DNASU; 42034; -.
DR EnsemblMetazoa; FBtr0083347; FBpp0082793; FBgn0003944. [P83949-1]
DR EnsemblMetazoa; FBtr0083348; FBpp0082794; FBgn0003944. [P83949-5]
DR EnsemblMetazoa; FBtr0083349; FBpp0082795; FBgn0003944. [P83949-4]
DR EnsemblMetazoa; FBtr0083350; FBpp0082796; FBgn0003944. [P83949-3]
DR EnsemblMetazoa; FBtr0083351; FBpp0082797; FBgn0003944. [P83949-2]
DR EnsemblMetazoa; FBtr0083352; FBpp0089155; FBgn0003944. [P83949-6]
DR GeneID; 42034; -.
DR KEGG; dme:Dmel_CG10388; -.
DR CTD; 42034; -.
DR FlyBase; FBgn0003944; Ubx.
DR VEuPathDB; VectorBase:FBgn0003944; -.
DR eggNOG; KOG0489; Eukaryota.
DR InParanoid; P83949; -.
DR OMA; HQNGYAA; -.
DR PhylomeDB; P83949; -.
DR SignaLink; P83949; -.
DR BioGRID-ORCS; 42034; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Ubx; fly.
DR EvolutionaryTrace; P83949; -.
DR GenomeRNAi; 42034; -.
DR PRO; PR:P83949; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003944; Expressed in parasegment 6 (Drosophila) and 19 other tissues.
DR ExpressionAtlas; P83949; baseline and differential.
DR Genevisible; P83949; DM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005704; C:polytene chromosome band; IDA:FlyBase.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CAFA.
DR GO; GO:0005667; C:transcription regulator complex; IMP:CAFA.
DR GO; GO:0017053; C:transcription repressor complex; IMP:CAFA.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IMP:CAFA.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:CAFA.
DR GO; GO:0061327; P:anterior Malpighian tubule development; IMP:FlyBase.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IBA:GO_Central.
DR GO; GO:0001709; P:cell fate determination; IMP:FlyBase.
DR GO; GO:0035052; P:dorsal vessel aortic cell fate commitment; TAS:FlyBase.
DR GO; GO:0001706; P:endoderm formation; TAS:FlyBase.
DR GO; GO:0007482; P:haltere development; IMP:FlyBase.
DR GO; GO:0007507; P:heart development; IMP:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0007501; P:mesodermal cell fate specification; IMP:FlyBase.
DR GO; GO:0007494; P:midgut development; TAS:FlyBase.
DR GO; GO:0042694; P:muscle cell fate specification; 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; IMP:CAFA.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0048636; P:positive regulation of muscle organ development; IMP:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CAFA.
DR GO; GO:0042659; P:regulation of cell fate specification; IMP:FlyBase.
DR GO; GO:0045570; P:regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
DR GO; GO:0010092; P:specification of animal organ identity; IMP:FlyBase.
DR GO; GO:0007384; P:specification of segmental identity, thorax; IMP:FlyBase.
DR CDD; cd00086; homeodomain; 1.
DR DisProt; DP00623; -.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001827; Homeobox_Antennapedia_CS.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR020479; Homeobox_metazoa.
DR Pfam; PF00046; Homeodomain; 1.
DR PRINTS; PR00024; HOMEOBOX.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00032; ANTENNAPEDIA; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Developmental protein;
KW DNA-binding; Homeobox; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..389
FT /note="Homeotic protein ultrabithorax"
FT /id="PRO_0000200268"
FT DNA_BIND 295..354
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 138..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 239..244
FT /note="Antp-type hexapeptide"
FT MOTIF 368..383
FT /note="QA"
FT COMPBIAS 175..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 248..290
FT /note="Missing (in isoform IVA)"
FT /evidence="ECO:0000303|PubMed:2565858"
FT /id="VSP_002407"
FT VAR_SEQ 248..273
FT /note="Missing (in isoform IIA)"
FT /evidence="ECO:0000303|PubMed:2565858"
FT /id="VSP_002406"
FT VAR_SEQ 248..256
FT /note="Missing (in isoform IA)"
FT /evidence="ECO:0000303|PubMed:2565858, ECO:0000303|Ref.6"
FT /id="VSP_002405"
FT VAR_SEQ 257..290
FT /note="Missing (in isoform IVB)"
FT /evidence="ECO:0000303|PubMed:2565858"
FT /id="VSP_002409"
FT VAR_SEQ 258..274
FT /note="Missing (in isoform IIB)"
FT /evidence="ECO:0000303|PubMed:2565858"
FT /id="VSP_002408"
FT CONFLICT 75
FT /note="N -> Y (in Ref. 3; AAA84412/AAA84411/AAA84410/
FT AAA84409/AAA84408)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="H -> Y (in Ref. 7; AAA28615)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="K -> E (in Ref. 7; AAA28615)"
FT /evidence="ECO:0000305"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:4CYC"
FT HELIX 304..316
FT /evidence="ECO:0007829|PDB:4CYC"
FT HELIX 322..332
FT /evidence="ECO:0007829|PDB:4CYC"
FT HELIX 336..355
FT /evidence="ECO:0007829|PDB:4CYC"
SQ SEQUENCE 389 AA; 40040 MW; D452E8FFE55D8F53 CRC64;
MNSYFEQASG FYGHPHQATG MAMGSGGHHD QTASAAAAAY RGFPLSLGMS PYANHHLQRT
TQDSPYDASI TAACNKIYGD GAGAYKQDCL NIKADAVNGY KDIWNTGGSN GGGGGGGGGG
GGGAGGTGGA GNANGGNAAN ANGQNNPAGG MPVRPSACTP DSRVGGYLDT SGGSPVSHRG
GSAGGNVSVS GGNGNAGGVQ SGVGVAGAGT AWNANCTISG AAAQTAAASS LHQASNHTFY
PWMAIAGECP EDPTKSKIRS DLTQYGGIST DMGKRYSESL AGSLLPDWLG TNGLRRRGRQ
TYTRYQTLEL EKEFHTNHYL TRRRRIEMAH ALCLTERQIK IWFQNRRMKL KKEIQAIKEL
NEQEKQAQAQ KAAAAAAAAA AVQGGHLDQ
