DDC_MOUSE
ID DDC_MOUSE Reviewed; 480 AA.
AC O88533;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase;
DE Short=AADC;
DE EC=4.1.1.28 {ECO:0000250|UniProtKB:P80041};
DE AltName: Full=DOPA decarboxylase;
DE Short=DDC;
GN Name=Ddc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Swiss Webster;
RA Duchemin A.M., Quach T.T., Gudehithlu K.F., Hadjiconstantinou M.,
RA Neff N.H.;
RT "Cloning of mouse brain aromatic-L-amino-acid decarboxylase cDNA.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine
CC (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin.
CC {ECO:0000250|UniProtKB:P80041}.
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 Evidence={ECO:0000250|UniProtKB:P80041};
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 Evidence={ECO:0000250|UniProtKB:P80041};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P20711};
CC -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine
CC from L-tyrosine: step 2/2. {ECO:0000250|UniProtKB:P80041}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P20711}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; AF071068; AAC25566.1; -; mRNA.
DR CCDS; CCDS24439.1; -.
DR RefSeq; NP_001177377.1; NM_001190448.1.
DR RefSeq; NP_057881.1; NM_016672.4.
DR RefSeq; XP_006514550.1; XM_006514487.3.
DR RefSeq; XP_006514551.1; XM_006514488.3.
DR RefSeq; XP_006514552.1; XM_006514489.2.
DR AlphaFoldDB; O88533; -.
DR SMR; O88533; -.
DR IntAct; O88533; 1.
DR STRING; 10090.ENSMUSP00000136467; -.
DR BindingDB; O88533; -.
DR ChEMBL; CHEMBL4230; -.
DR iPTMnet; O88533; -.
DR PhosphoSitePlus; O88533; -.
DR SwissPalm; O88533; -.
DR jPOST; O88533; -.
DR PaxDb; O88533; -.
DR PeptideAtlas; O88533; -.
DR PRIDE; O88533; -.
DR ProteomicsDB; 277967; -.
DR Antibodypedia; 2793; 529 antibodies from 47 providers.
DR DNASU; 13195; -.
DR Ensembl; ENSMUST00000066237; ENSMUSP00000068525; ENSMUSG00000020182.
DR Ensembl; ENSMUST00000109659; ENSMUSP00000105286; ENSMUSG00000020182.
DR Ensembl; ENSMUST00000178704; ENSMUSP00000136467; ENSMUSG00000020182.
DR GeneID; 13195; -.
DR KEGG; mmu:13195; -.
DR UCSC; uc007iaw.2; mouse.
DR CTD; 1644; -.
DR MGI; MGI:94876; Ddc.
DR VEuPathDB; HostDB:ENSMUSG00000020182; -.
DR eggNOG; KOG0628; Eukaryota.
DR GeneTree; ENSGT00940000156004; -.
DR HOGENOM; CLU_011856_3_0_1; -.
DR InParanoid; O88533; -.
DR OMA; NPGFNWS; -.
DR OrthoDB; 856958at2759; -.
DR PhylomeDB; O88533; -.
DR TreeFam; TF313863; -.
DR BRENDA; 4.1.1.28; 3474.
DR Reactome; R-MMU-209905; Catecholamine biosynthesis.
DR Reactome; R-MMU-209931; Serotonin and melatonin biosynthesis.
DR UniPathway; UPA00747; UER00734.
DR BioGRID-ORCS; 13195; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ddc; mouse.
DR PRO; PR:O88533; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O88533; protein.
DR Bgee; ENSMUSG00000020182; Expressed in superior cervical ganglion and 216 other tissues.
DR ExpressionAtlas; O88533; baseline and differential.
DR Genevisible; O88533; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0036467; F:5-hydroxy-L-tryptophan decarboxylase activity; IEA:RHEA.
DR GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IDA:MGI.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0036468; F:L-dopa decarboxylase activity; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISO:MGI.
DR GO; GO:0015842; P:aminergic neurotransmitter loading into synaptic vesicle; ISO:MGI.
DR GO; GO:0006584; P:catecholamine metabolic process; IBA:GO_Central.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0071312; P:cellular response to alkaloid; IEA:Ensembl.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0042416; P:dopamine biosynthetic process; ISO:MGI.
DR GO; GO:0033076; P:isoquinoline alkaloid metabolic process; IEA:Ensembl.
DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR GO; GO:0052314; P:phytoalexin metabolic process; IEA:Ensembl.
DR GO; GO:0046684; P:response to pyrethroid; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IDA:MGI.
DR GO; GO:0042427; P:serotonin biosynthetic process; ISO:MGI.
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 Acetylation; Catecholamine biosynthesis; Decarboxylase; Lyase;
KW Pyridoxal phosphate; Reference proteome; Repeat.
FT CHAIN 1..480
FT /note="Aromatic-L-amino-acid decarboxylase"
FT /id="PRO_0000146940"
FT REPEAT 58..115
FT /note="1"
FT REPEAT 118..178
FT /note="2"
FT REGION 58..178
FT /note="2 X approximate tandem repeats"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P80041"
FT BINDING 148
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P20711"
FT BINDING 149
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P20711"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P80041"
FT BINDING 246
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P20711"
FT BINDING 300
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P20711"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P80041"
FT MOD_RES 303
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P80041"
SQ SEQUENCE 480 AA; 53874 MW; D6C1CA504AC2D10E CRC64;
MDSREFRRRG KEMVDYIADY LDGIEGRPVY PDVEPGYLRP LIPATAPQEP ETYEDIIKDI
EKIIMPGVTH WHSPYFFAYF PTASSYPAML ADMLCGAIGC IGFSWAASPA CTELETVMMD
WLGKMLELPE AFLAGRAGEG GGVIQGSASE ATLVALLAAR TKVIRQLQAA SPEFTQAAIM
EKLVAYTSDQ AHSSVERAGL IGGIKLKAVP SDGNFSMRAS ALREALERDK AAGLIPFFVV
ATLGTTSCCS FDNLLEVGPI CNQEGVWLHI DAAYAGSAFI CPEFRYLLNG VEFADSFNFN
PHKWLLVNFD CSAMWVKRRT DLTGAFNMDP VYLKHSHQDS GFITDYRHWQ IPLGRRFRSL
KMWFVFRMYG VKGLQAYIRK HVELSHEFES LVRQDPRFEI CTEVILGLVC FRLKGSNELN
ETLLQRINSA KKIHLVPCRL RDKFVLRFAV CARTVESAHV QLAWEHISDL ASSVLRAEKE
