Skip Header

Contribute Send feedback
Read comments (?) or add your own

P61458 (PHS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pterin-4-alpha-carbinolamine dehydratase

Short name=PHS
EC=4.2.1.96
Alternative name(s):
4-alpha-hydroxy-tetrahydropterin dehydratase
Dimerization cofactor of hepatocyte nuclear factor 1-alpha
Short name=DCoH
Short name=Dimerization cofactor of HNF1
Phenylalanine hydroxylase-stimulating protein
Pterin carbinolamine dehydratase
Short name=PCD
Gene names
Name:Pcbd1
Synonyms:Dcoh, Pcbd
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length104 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity By similarity.

Catalytic activity

(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.

Subunit structure

Homotetramer and homodimer. Heterotetramer with HNF1A; formed by a dimer of dimers By similarity.

Subcellular location

Cytoplasm. Nucleus. Note: Cytoplasmic and/or nuclear.

Sequence similarities

Belongs to the pterin-4-alpha-carbinolamine dehydratase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 104103Pterin-4-alpha-carbinolamine dehydratase
PRO_0000063053

Regions

Region61 – 633Substrate binding By similarity
Region78 – 814Substrate binding By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue411N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P61458 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 13C798C25D9117E9

FASTA10411,986
        10         20         30         40         50         60 
MAGKAHRLSA EERDQLLPNL RAVGWNEVEG RDAIFKQFHF KDFNRAFGFM TRVALQAEKL 

        70         80         90        100 
DHHPEWFNVY NKVHITLSTH ECAGLSERDI NLASFIEQVA VSMT 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a cofactor that regulates dimerization of a mammalian homeodomain protein."
Mendel D.B., Khavari P.A., Conley P.B., Graves M.K., Hansen L.P., Admon A., Crabtree G.R.
Science 254:1762-1767(1991) [PubMed: 1763325] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: C57BL/6 X CBA.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Pancreas.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M83741 mRNA. No translation available.
AK007401 mRNA. Translation: BAB25014.1.
BC024354 mRNA. Translation: AAH24354.1.
IPIIPI00223800.
RefSeqNP_079549.1. NM_025273.3.
UniGeneMm.39473.

3D structure databases

ProteinModelPortalP61458.
SMRP61458. Positions 2-104.
ModBaseSearch...

Protein-protein interaction databases

STRINGP61458.

PTM databases

PhosphoSiteP61458.

Proteomic databases

PRIDEP61458.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020298; ENSMUSP00000020298; ENSMUSG00000020098.
GeneID13180.
KEGGmmu:13180.
UCSCuc007ffj.2. mouse.

Organism-specific databases

CTD5092.
MGIMGI:94873. Pcbd1.

Phylogenomic databases

eggNOGroNOG16514.
GeneTreeENSGT00390000007221.
HOGENOMHBG705804.
HOVERGENHBG000259.
InParanoidP61458.
OMASEERKTR.
OrthoDBEOG4QNMXP.
PhylomeDBP61458.

Gene expression databases

ArrayExpressP61458.
BgeeP61458.
GenevestigatorP61458.
GermOnlineENSMUSG00000020098. Mus musculus.

Family and domain databases

InterProIPR001533. Trans/pterin_deHydtase.
[Graphical view]
Gene3DG3DSA:3.30.1360.20. Trans_pterinDh. 1 hit.
KOK01724.
PANTHERPTHR12599. Trans_pterinDh. 1 hit.
PfamPF01329. Pterin_4a. 1 hit.
[Graphical view]
SUPFAMSSF55248. Trans_pterinDh. 1 hit.
ProtoNetSearch...

Other

NextBio283296.
SOURCESearch...

Entry information

Entry namePHS_MOUSE
AccessionPrimary (citable) accession number: P61458
Secondary accession number(s): P70519, P80095, Q9D930
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families