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P14173

- DDC_RAT

UniProt

P14173 - DDC_RAT

Protein

Aromatic-L-amino-acid decarboxylase

Gene

Ddc

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine.

    Catalytic activityi

    L-dopa = dopamine + CO2.
    5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2.

    Cofactori

    Pyridoxal phosphate.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei82 – 821SubstrateBy similarity
    Binding sitei148 – 1481PLP; via amide nitrogenBy similarity
    Binding sitei149 – 1491PLPBy similarity
    Binding sitei192 – 1921SubstrateBy similarity
    Binding sitei246 – 2461PLP; via carbonyl oxygenBy similarity
    Binding sitei300 – 3001PLPBy similarity

    GO - Molecular functioni

    1. amino acid binding Source: RGD
    2. aromatic-L-amino-acid decarboxylase activity Source: RGD
    3. protein binding Source: RGD
    4. protein domain specific binding Source: RGD
    5. pyridoxal phosphate binding Source: RGD

    GO - Biological processi

    1. catecholamine biosynthetic process Source: RGD
    2. cellular amino acid metabolic process Source: InterPro
    3. cellular response to alkaloid Source: RGD
    4. cellular response to drug Source: RGD
    5. cellular response to growth factor stimulus Source: RGD
    6. circadian rhythm Source: RGD
    7. dopamine biosynthetic process Source: RGD
    8. dopamine metabolic process Source: RGD
    9. isoquinoline alkaloid metabolic process Source: RGD
    10. multicellular organismal aging Source: RGD
    11. phytoalexin metabolic process Source: RGD
    12. response to pyrethroid Source: RGD
    13. serotonin biosynthetic process Source: RGD
    14. synaptic vesicle amine transport Source: RGD

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Catecholamine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15070.
    UniPathwayiUPA00747; UER00734.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aromatic-L-amino-acid decarboxylase (EC:4.1.1.28)
    Short name:
    AADC
    Alternative name(s):
    DOPA decarboxylase
    Short name:
    DDC
    Gene namesi
    Name:Ddc
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 14

    Organism-specific databases

    RGDi2494. Ddc.

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: RGD
    2. cytoplasm Source: RGD
    3. intracellular Source: RGD
    4. neuronal cell body Source: RGD
    5. synaptic vesicle Source: RGD

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi192 – 1921H → A: Abolishes decarboxylase activity. 2 Publications
    Mutagenesisi192 – 1921H → Q: Reduces decarboxylase activity by 96%. 2 Publications
    Mutagenesisi252 – 2521D → A or E: Abolishes decarboxylase activity. 1 Publication
    Mutagenesisi271 – 2711D → A: Abolishes decarboxylase activity. 2 Publications
    Mutagenesisi271 – 2711D → E: Reduces decarboxylase activity by 65%. 2 Publications
    Mutagenesisi296 – 2961S → A: Abolishes decarboxylase activity. 1 Publication
    Mutagenesisi300 – 3001N → A: Reduces decarboxylase activity by 75%. 1 Publication
    Mutagenesisi302 – 3021H → Q: Reduces decarboxylase activity by 99.8%. 1 Publication
    Mutagenesisi303 – 3031K → A or R: Abolishes decarboxylase activity. 1 Publication
    Mutagenesisi332 – 3321Y → A or F: Abolishes decarboxylase activity. 1 Publication
    Mutagenesisi355 – 3551R → A: Abolishes decarboxylase activity. 1 Publication
    Mutagenesisi355 – 3551R → K: No effect. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 480480Aromatic-L-amino-acid decarboxylasePRO_0000146942Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei303 – 3031N6-(pyridoxal phosphate)lysine

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP14173.
    PRIDEiP14173.

    PTM databases

    PhosphoSiteiP14173.

    Expressioni

    Gene expression databases

    GenevestigatoriP14173.

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    3D structure databases

    ProteinModelPortaliP14173.
    SMRiP14173. Positions 1-475.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati58 – 115581Add
    BLAST
    Repeati118 – 178612Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 1781212 X approximate tandem repeatsAdd
    BLAST

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0076.
    GeneTreeiENSGT00730000110825.
    HOVERGENiHBG000944.
    KOiK01593.
    OMAiPICNKED.
    OrthoDBiEOG75B851.
    PhylomeDBiP14173.
    TreeFamiTF313863.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR010977. Aromatic_deC.
    IPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR021115. Pyridoxal-P_BS.
    [Graphical view]
    PfamiPF00282. Pyridoxal_deC. 1 hit.
    [Graphical view]
    PRINTSiPR00800. YHDCRBOXLASE.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14173-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDSREFRRRG KEMVDYIADY LDGIEGRPVY PDVEPGYLRA LIPTTAPQEP    50
    ETYEDIIRDI EKIIMPGVTH WHSPYFFAYF PTASSYPAML ADMLCGAIGC 100
    IGFSWAASPA CTELETVMMD WLGKMLELPE AFLAGRAGEG GGVIQGSASE 150
    ATLVALLAAR TKMIRQLQAA SPELTQAALM EKLVAYTSDQ AHSSVERAGL 200
    IGGVKIKAIP SDGNYSMRAA ALREALERDK AAGLIPFFVV VTLGTTSCCS 250
    FDNLLEVGPI CNQEGVWLHI DAAYAGSAFI CPEFRYLLNG VEFADSFNFN 300
    PHKWLLVNFD CSAMWVKKRT DLTEAFNMDP VYLRHSHQDS GLITDYRHWQ 350
    IPLGRRFRSL KMWFVFRMYG VKGLQAYIRK HVKLSHEFES LVRQDPRFEI 400
    CTEVILGLVC FRLKGSNQLN ETLLQRINSA KKIHLVPCRL RDKFVLRFAV 450
    CSRTVESAHV QLAWEHIRDL ASSVLRAEKE 480
    Length:480
    Mass (Da):54,053
    Last modified:January 1, 1990 - v1
    Checksum:i1E1D077488704574
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33001
    , L32989, L32990, L32991, L32992, L32993, L32994, L32995, L32996, L32997, L33003, L32999, L33000 Genomic DNA. Translation: AAA40646.1.
    M27716 mRNA. Translation: AAA41087.1.
    BC087032 mRNA. Translation: AAH87032.1.
    L03417 Genomic DNA. Translation: AAA99905.1.
    PIRiA33994. DCRTA.
    RefSeqiNP_001257781.1. NM_001270852.1.
    NP_001257782.1. NM_001270853.1.
    NP_036677.1. NM_012545.4.
    XP_006251537.1. XM_006251475.1.
    UniGeneiRn.11064.

    Genome annotation databases

    EnsembliENSRNOT00000005851; ENSRNOP00000005851; ENSRNOG00000004327.
    ENSRNOT00000073892; ENSRNOP00000064520; ENSRNOG00000004327.
    GeneIDi24311.
    KEGGirno:24311.
    UCSCiRGD:2494. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33001
    , L32989 , L32990 , L32991 , L32992 , L32993 , L32994 , L32995 , L32996 , L32997 , L33003 , L32999 , L33000 Genomic DNA. Translation: AAA40646.1 .
    M27716 mRNA. Translation: AAA41087.1 .
    BC087032 mRNA. Translation: AAH87032.1 .
    L03417 Genomic DNA. Translation: AAA99905.1 .
    PIRi A33994. DCRTA.
    RefSeqi NP_001257781.1. NM_001270852.1.
    NP_001257782.1. NM_001270853.1.
    NP_036677.1. NM_012545.4.
    XP_006251537.1. XM_006251475.1.
    UniGenei Rn.11064.

    3D structure databases

    ProteinModelPortali P14173.
    SMRi P14173. Positions 1-475.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei P14173.

    Proteomic databases

    PaxDbi P14173.
    PRIDEi P14173.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000005851 ; ENSRNOP00000005851 ; ENSRNOG00000004327 .
    ENSRNOT00000073892 ; ENSRNOP00000064520 ; ENSRNOG00000004327 .
    GeneIDi 24311.
    KEGGi rno:24311.
    UCSCi RGD:2494. rat.

    Organism-specific databases

    CTDi 1644.
    RGDi 2494. Ddc.

    Phylogenomic databases

    eggNOGi COG0076.
    GeneTreei ENSGT00730000110825.
    HOVERGENi HBG000944.
    KOi K01593.
    OMAi PICNKED.
    OrthoDBi EOG75B851.
    PhylomeDBi P14173.
    TreeFami TF313863.

    Enzyme and pathway databases

    UniPathwayi UPA00747 ; UER00734 .
    BioCyci MetaCyc:MONOMER-15070.

    Miscellaneous databases

    NextBioi 602949.
    PROi P14173.

    Gene expression databases

    Genevestigatori P14173.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR010977. Aromatic_deC.
    IPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR021115. Pyridoxal-P_BS.
    [Graphical view ]
    Pfami PF00282. Pyridoxal_deC. 1 hit.
    [Graphical view ]
    PRINTSi PR00800. YHDCRBOXLASE.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    PROSITEi PS00392. DDC_GAD_HDC_YDC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and sequencing of a cDNA of rat dopa decarboxylase: partial amino acid homologies with other enzymes synthesizing catecholamines."
      Tanaka T., Horio Y., Taketoshi M., Imamura I., Ando-Yamamoto M., Kangawa K., Matsuo H., Kurodo M., Wada H.
      Proc. Natl. Acad. Sci. U.S.A. 86:8142-8146(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    3. "Distinct promoters direct neuronal and nonneuronal expression of rat aromatic L-amino acid decarboxylase."
      Albert V.R., Lee M.R., Bolden A.H., Wurzburger R.J., Aguanno A.
      Proc. Natl. Acad. Sci. U.S.A. 89:12053-12057(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
      Strain: Sprague-Dawley.
    4. "Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis."
      Ishii S., Mizugichi H., Nishino J., Hayashi H., Kagamiyama H.
      J. Biochem. 120:369-376(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-192; ASP-252; ASP-271; SER-296; LYS-303; TYR-332 AND ARG-355, COFACTOR.
    5. "Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase. Effects on catalytic properties."
      Bertoldi M., Castellani S., Bori Voltattorni C.
      Eur. J. Biochem. 268:2975-2981(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-192; ASP-271; ASN-300 AND HIS-302.

    Entry informationi

    Entry nameiDDC_RAT
    AccessioniPrimary (citable) accession number: P14173
    Secondary accession number(s): Q6LEG4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3