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Protein

Pterin-4-alpha-carbinolamine dehydratase 2

Gene

Pcbd2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2 (By similarity).By similarity
Regulates the dimerization of homeodomain protein HNF-1-alpha and enhances its transcriptional activity.1 Publication

Catalytic activityi

(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H2O.

GO - Molecular functioni

GO - Biological processi

  • positive regulation of transcription, DNA-templated Source: MGI
  • protein heterooligomerization Source: MGI
  • protein homotetramerization Source: MGI
  • tetrahydrobiopterin biosynthetic process Source: UniProtKB-KW

Keywordsi

Molecular functionLyase
Biological processTetrahydrobiopterin biosynthesis

Enzyme and pathway databases

BRENDAi4.2.1.96. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Pterin-4-alpha-carbinolamine dehydratase 2 (EC:4.2.1.96)
Short name:
PHS 2
Alternative name(s):
4-alpha-hydroxy-tetrahydropterin dehydratase 2
DcoH-like protein DCoHm
Dimerization cofactor of hepatocyte nuclear factor 1 from muscle
HNF-1-alpha dimerization cofactor
Gene namesi
Name:Pcbd2
Synonyms:Dcoh2, Dcohm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1919812. Pcbd2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000630581 – 136Pterin-4-alpha-carbinolamine dehydratase 2Add BLAST136

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei120N6-acetyllysine; alternateCombined sources1
Modified residuei120N6-succinyllysine; alternateCombined sources1
Modified residuei124N6-acetyllysine; alternateCombined sources1
Modified residuei124N6-succinyllysine; alternateCombined sources1
Modified residuei131N6-acetyllysine; alternateCombined sources1
Modified residuei131N6-succinyllysine; alternateCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9CZL5.
MaxQBiQ9CZL5.
PaxDbiQ9CZL5.
PeptideAtlasiQ9CZL5.
PRIDEiQ9CZL5.

PTM databases

iPTMnetiQ9CZL5.
PhosphoSitePlusiQ9CZL5.

Expressioni

Gene expression databases

BgeeiENSMUSG00000021496.
ExpressionAtlasiQ9CZL5. baseline and differential.
GenevisibleiQ9CZL5. MM.

Interactioni

Subunit structurei

Homotetramer. Interacts with DYRK1B (By similarity).By similarity

Protein-protein interaction databases

BioGridi215439. 2 interactors.
CORUMiQ9CZL5.
IntActiQ9CZL5. 2 interactors.
MINTiMINT-4092896.
STRINGi10090.ENSMUSP00000021958.

Structurei

Secondary structure

1136
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 55Combined sources13
Beta strandi62 – 65Combined sources4
Beta strandi67 – 72Combined sources6
Helixi76 – 93Combined sources18
Beta strandi98 – 102Combined sources5
Beta strandi105 – 110Combined sources6
Turni113 – 116Combined sources4
Helixi120 – 133Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RU0X-ray1.60A/B36-136[»]
4WILX-ray1.36A/B34-136[»]
ProteinModelPortaliQ9CZL5.
SMRiQ9CZL5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CZL5.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi3 – 11Poly-Ala9

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4073. Eukaryota.
COG2154. LUCA.
GeneTreeiENSGT00390000007221.
HOGENOMiHOG000007680.
HOVERGENiHBG000259.
InParanoidiQ9CZL5.
KOiK01724.
OMAiTSHDCGE.
OrthoDBiEOG091G120V.
PhylomeDBiQ9CZL5.
TreeFamiTF300188.

Family and domain databases

Gene3Di3.30.1360.20. 1 hit.
HAMAPiMF_00434. Pterin_4_alpha. 1 hit.
InterProiView protein in InterPro
IPR001533. Trans/pterin_deHydtase.
PfamiView protein in Pfam
PF01329. Pterin_4a. 1 hit.
SUPFAMiSSF55248. SSF55248. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CZL5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAAAAVAVA AVGARSAGRW LAALRSPGAS RAAMSSDAQW LTAEERDQLI
60 70 80 90 100
PGLKAAGWSE LSERDAIYKE FSFKNFNQAF GFMSRVALQA EKMNHHPEWF
110 120 130
NVYNKVQITL TSHDCGGLTK RDVKLAQFIE KAAASL
Length:136
Mass (Da):14,830
Last modified:June 16, 2009 - v2
Checksum:i5E447CDD57CF7496
GO

Sequence cautioni

The sequence AAH28642 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAB28260 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC028642 mRNA. Translation: AAH28642.1. Different initiation.
AK012465 mRNA. Translation: BAB28260.1. Different initiation.
CCDSiCCDS26554.1.
RefSeqiNP_082557.1. NM_028281.1.
UniGeneiMm.28145.

Genome annotation databases

EnsembliENSMUST00000021958; ENSMUSP00000021958; ENSMUSG00000021496.
GeneIDi72562.
KEGGimmu:72562.
UCSCiuc007qrz.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiPHS2_MOUSE
AccessioniPrimary (citable) accession number: Q9CZL5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: June 16, 2009
Last modified: September 27, 2017
This is version 125 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families