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P14173

- DDC_RAT

UniProt

P14173 - DDC_RAT

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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

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 – 821Substrate By similarity
Binding sitei148 – 1481PLP; via amide nitrogen By similarity
Binding sitei149 – 1491PLP By similarity
Binding sitei192 – 1921Substrate By similarity
Binding sitei246 – 2461PLP; via carbonyl oxygen By similarity
Binding sitei300 – 3001PLP By 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
Complete GO annotation...

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
Complete GO annotation...

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-acetylmethionine By 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.

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

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 120 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

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