DDC_DROME
ID DDC_DROME Reviewed; 510 AA.
AC P05031; O18379; P05032; Q24295; Q7YSJ0; Q7YSK5; Q7YSV6; Q7Z0E1; Q7Z0E2;
AC Q7Z0E3; Q7Z0E4; Q7Z0E5; Q7Z0E6; Q7Z0E7; Q7Z0E8; Q7Z0E9; Q95SL9; Q9VIZ5;
AC Q9VIZ6;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 4.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase;
DE Short=AADC;
DE EC=4.1.1.28;
DE AltName: Full=DOPA decarboxylase;
DE Short=DDC;
GN Name=Ddc; ORFNames=CG10697;
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] (ISOFORMS CNS AND HYPODERM), AND TISSUE
RP SPECIFICITY.
RC STRAIN=Canton-S;
RX PubMed=3102230; DOI=10.1002/j.1460-2075.1986.tb04648.x;
RA Morgan B.A., Johnson W.A., Hirsh J.;
RT "Regulated splicing produces different forms of dopa decarboxylase in the
RT central nervous system and hypoderm of Drosophila melanogaster.";
RL EMBO J. 5:3335-3342(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS CNS AND 3).
RC STRAIN=Canton-S;
RX PubMed=3023054; DOI=10.1002/j.1460-2075.1986.tb04549.x;
RA Eveleth D.D., Gietz R.D., Spencer C.A., Nargang F.E., Hodgetts R.B.,
RA Marsh J.L.;
RT "Sequence and structure of the dopa decarboxylase gene of Drosophila:
RT evidence for novel RNA splicing variants.";
RL EMBO J. 5:2663-2672(1986).
RN [3]
RP SEQUENCE REVISION.
RA Marsh J.L.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS CNS; HYPODERM AND 3), FUNCTION,
RP AND VARIANTS PRO-12; ASN-197; MET-264; MET-390; PHE-428 AND ALA-489.
RC STRAIN=Allele Ddc-2b, Allele Ddc-Ore, Allele Ddc-R11, Allele Ddc-R12,
RC Allele Ddc-R16, Allele Ddc-R18, Allele Ddc-R20, Allele Ddc-R24,
RC Allele Ddc-R25, Allele Ddc-R27, Allele Ddc-R30, Allele Ddc-R33,
RC Allele Ddc-R6, and Allele Ddc-R9; TISSUE=Brain, and Epidermis;
RX PubMed=12881721; DOI=10.1038/ng1218;
RA De Luca M., Roshina N.V., Geiger-Thornsberry G.L., Lyman R.F.,
RA Pasyukova E.G., Mackay T.F.C.;
RT "Dopa decarboxylase (Ddc) affects variation in Drosophila longevity.";
RL Nat. Genet. 34:429-433(2003).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-510.
RC STRAIN=St. Lucia;
RX PubMed=10231575; DOI=10.1016/s0378-1119(99)00096-7;
RA Tatarenkov A., Saez A.G., Ayala F.J.;
RT "A compact gene cluster in Drosophila: the unrelated Cs gene is compressed
RT between duplicated amd and Ddc.";
RL Gene 231:111-120(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 493-510.
RX PubMed=3478553; DOI=10.1007/bf00329656;
RA Eveleth D.D., Marsh J.L.;
RT "Overlapping transcription units in Drosophila: sequence and structure of
RT the Cs gene.";
RL Mol. Gen. Genet. 209:290-298(1987).
RN [10]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=3095924; DOI=10.1126/science.3095924;
RA Scholnick S.B., Bray S.J., Morgan B.A., McCormick C.A., Hirsh J.;
RT "CNS and hypoderm regulatory elements of the Drosophila melanogaster dopa
RT decarboxylase gene.";
RL Science 234:998-1002(1986).
RN [11]
RP DEVELOPMENTAL STAGE.
RX PubMed=3007242; DOI=10.1016/0012-1606(86)90402-1;
RA Spencer C.A., Gietz R.D., Hodgetts R.B.;
RT "Analysis of the transcription unit adjacent to the 3'-end of the dopa
RT decarboxylase gene in Drosophila melanogaster.";
RL Dev. Biol. 114:260-264(1986).
RN [12]
RP INDUCTION.
RX PubMed=3007239; DOI=10.1016/0012-1606(86)90390-8;
RA Clark W.C., Doctor J., Fristrom J.W., Hodgetts R.B.;
RT "Differential responses of the dopa decarboxylase gene to 20-OH-ecdysone in
RT Drosophila melanogaster.";
RL Dev. Biol. 114:141-150(1986).
CC -!- FUNCTION: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine
CC (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan
CC to tryptamine. Variation in the synthesis of bioamines may be a factor
CC contributing to natural variation in life span.
CC {ECO:0000269|PubMed:12881721}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-dopa = CO2 + dopamine; Xref=Rhea:RHEA:12272,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57504,
CC ChEBI:CHEBI:59905; EC=4.1.1.28;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxy-L-tryptophan + H(+) = CO2 + serotonin;
CC Xref=Rhea:RHEA:18533, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:58266, ChEBI:CHEBI:350546; EC=4.1.1.28;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=CNS; Synonyms=Long, Brain, 56.7 kDa, C;
CC IsoId=P05031-1; Sequence=Displayed;
CC Name=Hypoderm; Synonyms=Short, B, D;
CC IsoId=P05031-2; Sequence=VSP_001305;
CC Name=3; Synonyms=Hypoderm, 56.2 kDa;
CC IsoId=P05031-3; Sequence=VSP_001306;
CC -!- TISSUE SPECIFICITY: Hypoderm isoform is expressed only in hypodermal
CC epithelium and the CNS isoform only in central nervous system.
CC {ECO:0000269|PubMed:3095924, ECO:0000269|PubMed:3102230}.
CC -!- DEVELOPMENTAL STAGE: Hypoderm isoform has high expression levels in
CC hypoderm during late embryogenesis, late larval development,
CC pupariation and adult eclosion. CNS isoform has constant expression
CC level in CNS throughout the life cycle. {ECO:0000269|PubMed:3007242,
CC ECO:0000269|PubMed:3095924}.
CC -!- INDUCTION: By ecdysone. In larval epidermis, expression is rapidly
CC induced. In adult epidermis expression responds to a pulse of hormone
CC and there is a time lag between initial exposure and appearance of DDC.
CC {ECO:0000269|PubMed:3007239}.
CC -!- POLYMORPHISM: Three common molecular polymorphisms (2 in the promoter
CC region and Phe-12) account for 15.5% of the genetic contribution to
CC variance in life span, the polymorphisms are maintained by balancing
CC selection. {ECO:0000269|PubMed:12881721}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; X04661; CAB37087.1; -; Genomic_DNA.
DR EMBL; X04661; CAB37088.1; -; Genomic_DNA.
DR EMBL; X04426; CAA28022.1; -; Genomic_DNA.
DR EMBL; X04426; CAA28023.1; -; Genomic_DNA.
DR EMBL; AY197756; AAO16831.1; -; Genomic_DNA.
DR EMBL; AY197756; AAO16832.1; -; Genomic_DNA.
DR EMBL; AY197757; AAO16833.1; -; Genomic_DNA.
DR EMBL; AY197757; AAO16834.1; -; Genomic_DNA.
DR EMBL; AY197758; AAO16835.1; -; Genomic_DNA.
DR EMBL; AY197758; AAO16836.1; -; Genomic_DNA.
DR EMBL; AY197759; AAO16837.1; -; Genomic_DNA.
DR EMBL; AY197759; AAO16838.1; -; Genomic_DNA.
DR EMBL; AY197760; AAO16839.1; -; Genomic_DNA.
DR EMBL; AY197760; AAO16840.1; -; Genomic_DNA.
DR EMBL; AY197761; AAO16841.1; -; Genomic_DNA.
DR EMBL; AY197761; AAO16842.1; -; Genomic_DNA.
DR EMBL; AY197762; AAO16843.1; -; Genomic_DNA.
DR EMBL; AY197762; AAO16844.1; -; Genomic_DNA.
DR EMBL; AY197763; AAO16845.1; -; Genomic_DNA.
DR EMBL; AY197763; AAO16846.1; -; Genomic_DNA.
DR EMBL; AY197764; AAO16847.1; -; Genomic_DNA.
DR EMBL; AY197764; AAO16848.1; -; Genomic_DNA.
DR EMBL; AY197765; AAO16849.1; -; Genomic_DNA.
DR EMBL; AY197765; AAO16850.1; -; Genomic_DNA.
DR EMBL; AY197766; AAO16851.1; -; Genomic_DNA.
DR EMBL; AY197766; AAO16852.1; -; Genomic_DNA.
DR EMBL; AY197767; AAO16853.1; -; Genomic_DNA.
DR EMBL; AY197767; AAO16854.1; -; Genomic_DNA.
DR EMBL; AY197768; AAO16855.1; -; Genomic_DNA.
DR EMBL; AY197768; AAO16856.1; -; Genomic_DNA.
DR EMBL; AY197769; AAO16857.1; -; Genomic_DNA.
DR EMBL; AY197769; AAO16858.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53762.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53763.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53764.3; -; Genomic_DNA.
DR EMBL; AY060708; AAL28256.1; -; mRNA.
DR EMBL; AF091328; AAC67582.1; -; Genomic_DNA.
DR EMBL; X05991; CAA29409.2; -; Genomic_DNA.
DR PIR; A25697; DCFFD1.
DR PIR; A25709; DCFFA.
DR PIR; B25697; DCFFD2.
DR RefSeq; NP_523600.5; NM_078876.5. [P05031-2]
DR RefSeq; NP_724163.1; NM_165279.2. [P05031-1]
DR RefSeq; NP_724164.1; NM_165280.2. [P05031-2]
DR PDB; 3K40; X-ray; 1.75 A; A/B=36-510.
DR PDBsum; 3K40; -.
DR AlphaFoldDB; P05031; -.
DR SMR; P05031; -.
DR BioGRID; 61175; 4.
DR DIP; DIP-18733N; -.
DR IntAct; P05031; 2.
DR STRING; 7227.FBpp0080710; -.
DR PaxDb; P05031; -.
DR DNASU; 35190; -.
DR EnsemblMetazoa; FBtr0081166; FBpp0080709; FBgn0000422. [P05031-2]
DR EnsemblMetazoa; FBtr0081167; FBpp0080710; FBgn0000422. [P05031-1]
DR EnsemblMetazoa; FBtr0290291; FBpp0288730; FBgn0000422. [P05031-2]
DR GeneID; 35190; -.
DR KEGG; dme:Dmel_CG10697; -.
DR CTD; 1644; -.
DR FlyBase; FBgn0000422; Ddc.
DR VEuPathDB; VectorBase:FBgn0000422; -.
DR eggNOG; KOG0628; Eukaryota.
DR GeneTree; ENSGT00940000156004; -.
DR InParanoid; P05031; -.
DR PhylomeDB; P05031; -.
DR BRENDA; 4.1.1.28; 1994.
DR Reactome; R-DME-209905; Catecholamine biosynthesis.
DR Reactome; R-DME-209931; Serotonin and melatonin biosynthesis.
DR SignaLink; P05031; -.
DR BioGRID-ORCS; 35190; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Ddc; fly.
DR EvolutionaryTrace; P05031; -.
DR GenomeRNAi; 35190; -.
DR PRO; PR:P05031; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000422; Expressed in capitellum (Drosophila) and 23 other tissues.
DR ExpressionAtlas; P05031; baseline and differential.
DR Genevisible; P05031; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036467; F:5-hydroxy-L-tryptophan decarboxylase activity; IDA:FlyBase.
DR GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IDA:FlyBase.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0036468; F:L-dopa decarboxylase activity; IDA:FlyBase.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0048085; P:adult chitin-containing cuticle pigmentation; IMP:FlyBase.
DR GO; GO:0007615; P:anesthesia-resistant memory; IDA:FlyBase.
DR GO; GO:0006584; P:catecholamine metabolic process; IBA:GO_Central.
DR GO; GO:0006585; P:dopamine biosynthetic process from tyrosine; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IGI:FlyBase.
DR GO; GO:0048082; P:regulation of adult chitin-containing cuticle pigmentation; IMP:FlyBase.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:FlyBase.
DR GO; GO:0009611; P:response to wounding; IEP:FlyBase.
DR GO; GO:0042427; P:serotonin biosynthetic process; IBA:GO_Central.
DR GO; GO:0006587; P:serotonin biosynthetic process from tryptophan; IMP:FlyBase.
DR GO; GO:0040040; P:thermosensory behavior; IMP:FlyBase.
DR GO; GO:0043052; P:thermotaxis; IMP:FlyBase.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Catecholamine biosynthesis;
KW Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..510
FT /note="Aromatic-L-amino-acid decarboxylase"
FT /id="PRO_0000146945"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 337
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform Hypoderm)"
FT /evidence="ECO:0000305"
FT /id="VSP_001305"
FT VAR_SEQ 1..33
FT /note="MSHIPISNTIPTKQTDGNGKANISPDKLDPKVS -> MSIGFRYRANNYARL
FT ITKYFCIHIK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_001306"
FT VARIANT 12
FT /note="T -> P (in allele Ddc-R6, allele Ddc-R9, allele Ddc-
FT R16, allele Ddc-R20, allele Ddc-R25 and allele Ddc-R30)"
FT /evidence="ECO:0000269|PubMed:12881721"
FT VARIANT 197
FT /note="K -> N (in allele Ddc-R9)"
FT /evidence="ECO:0000269|PubMed:12881721"
FT VARIANT 264
FT /note="V -> M (in allele Ddc-R11 and allele Ddc-R18)"
FT /evidence="ECO:0000269|PubMed:12881721"
FT VARIANT 390
FT /note="R -> M (in allele Ddc-Ore)"
FT /evidence="ECO:0000269|PubMed:12881721"
FT VARIANT 428
FT /note="S -> F (in allele Ddc-R33)"
FT /evidence="ECO:0000269|PubMed:12881721"
FT VARIANT 489
FT /note="S -> A (in allele Ddc-2b)"
FT /evidence="ECO:0000269|PubMed:12881721"
FT CONFLICT 32..33
FT /note="Missing (in Ref. 1; CAB37087)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="R -> A (in Ref. 1; CAB37087/CAB37088)"
FT /evidence="ECO:0000305"
FT HELIX 38..57
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:3K40"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3K40"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 183..205
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:3K40"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:3K40"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:3K40"
FT STRAND 269..278
FT /evidence="ECO:0007829|PDB:3K40"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 288..297
FT /evidence="ECO:0007829|PDB:3K40"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 316..322
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:3K40"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:3K40"
FT STRAND 346..352
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 391..426
FT /evidence="ECO:0007829|PDB:3K40"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:3K40"
FT STRAND 440..447
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 449..462
FT /evidence="ECO:0007829|PDB:3K40"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:3K40"
FT STRAND 475..481
FT /evidence="ECO:0007829|PDB:3K40"
FT HELIX 489..507
FT /evidence="ECO:0007829|PDB:3K40"
FT CONFLICT P05031-3:13
FT /note="A -> V (in Ref. 4; AAO16848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 57288 MW; 0A850488D407D4BF CRC64;
MSHIPISNTI PTKQTDGNGK ANISPDKLDP KVSIDMEAPE FKDFAKTMVD FIAEYLENIR
ERRVLPEVKP GYLKPLIPDA APEKPEKWQD VMQDIERVIM PGVTHWHSPK FHAYFPTANS
YPAIVADMLS GAIACIGFTW IASPACTELE VVMMDWLGKM LELPAEFLAC SGGKGGGVIQ
GTASESTLVA LLGAKAKKLK EVKELHPEWD EHTILGKLVG YCSDQAHSSV ERAGLLGGVK
LRSVQSENHR MRGAALEKAI EQDVAEGLIP FYAVVTLGTT NSCAFDYLDE CGPVGNKHNL
WIHVDAAYAG SAFICPEYRH LMKGIESADS FNFNPHKWML VNFDCSAMWL KDPSWVVNAF
NVDPLYLKHD MQGSAPDYRH WQIPLGRRFR ALKLWFVLRL YGVENLQAHI RRHCNFAKQF
GDLCVADSRF ELAAEINMGL VCFRLKGSNE RNEALLKRIN GRGHIHLVPA KIKDVYFLRM
AICSRFTQSE DMEYSWKEVS AAADEMEQEQ
