Q9CZL5 (PHS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pterin-4-alpha-carbinolamine dehydratase 2
Short name=PHS 2
EC=4.2.1.96

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 names

Name:	Pcbd2
Synonyms:	Dcoh2, Dcohm

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	136 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity. Ref.3 Regulates the dimerization of homeodomain protein HNF-1-alpha and enhances its transcriptional activity. Ref.3
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. Interacts with DYRK1B By similarity. Ref.3
Sequence similarities	Belongs to the pterin-4-alpha-carbinolamine dehydratase family.
Sequence caution	The sequence AAH28642.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB28260.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Tetrahydrobiopterin biosynthesis
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein heterooligomerization Inferred from physical interaction Ref.3. Source: MGI protein homotetramerization Inferred from physical interaction Ref.3. Source: MGI tetrahydrobiopterin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: MGI nucleus Inferred from physical interaction Ref.3. Source: MGI
Molecular function	4-alpha-hydroxytetrahydrobiopterin dehydratase activity Inferred from electronic annotation. Source: EC phenylalanine 4-monooxygenase activity Inferred from direct assay Ref.3. Source: MGI protein binding Inferred from physical interaction Ref.3. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 136

136

Pterin-4-alpha-carbinolamine dehydratase 2

PRO_0000063058

Regions

Compositional bias

3 – 11

9

Poly-Ala

Amino acid modifications

Modified residue

131

1

N6-acetyllysine By similarity

Secondary structure

1

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136

Helix Strand Turn

Details...

Helix

44 – 56

13

Beta strand

63 – 66

4

Beta strand

68 – 73

6

Helix

77 – 94

18

Beta strand

99 – 103

5

Beta strand

106 – 111

6

Turn

114 – 116

3

Helix

121 – 134

14

Sequences

	Sequence		Length	Mass (Da)
	Q9CZL5 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: 5E447CDD57CF7496	FASTA	136	14,830
	10 20 30 40 50 60 MVAAAAVAVA AVGARSAGRW LAALRSPGAS RAAMSSDAQW LTAEERDQLI PGLKAAGWSE 70 80 90 100 110 120 LSERDAIYKE FSFKNFNQAF GFMSRVALQA EKMNHHPEWF NVYNKVQITL TSHDCGGLTK 130 RDVKLAQFIE KAAASL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: C57BL/6J. Tissue: Mammary gland.
[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. , 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] OF 14-136. Strain: C57BL/6J. Tissue: Embryo.
[3]	"Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2." Rose R.B., Pullen K.E., Bayle J.H., Crabtree G.R., Alber T. Biochemistry 43:7345-7355(2004) [PubMed: 15182178] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 34-136, SUBUNIT, FUNCTION AS A PHS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BC028642 mRNA. Translation: AAH28642.1. Different initiation.
AK012465 mRNA. Translation: BAB28260.1. Different initiation.

IPI

IPI00469840.

RefSeq

NP_082557.1. NM_028281.1.

UniGene

Mm.28145.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RU0	X-ray	1.60	A/B	34-136	[»]

ProteinModelPortal

Q9CZL5.

SMR

Q9CZL5. Positions 37-136.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9CZL5.

PTM databases

PhosphoSite

Q9CZL5.

Proteomic databases

PRIDE

Q9CZL5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000021958; ENSMUSP00000021958; ENSMUSG00000021496.
ENSMUST00000124968; ENSMUSP00000115392; ENSMUSG00000021496.

GeneID

72562.

KEGG

mmu:72562.

NMPDR

fig|10090.3.peg.27910.

UCSC

uc007qrz.1. mouse.

Organism-specific databases

CTD

84105.

MGI

MGI:1919812. Pcbd2.

Phylogenomic databases

eggNOG

roNOG17104.

GeneTree

ENSGT00390000007221.

HOGENOM

HBG705804.

HOVERGEN

HBG000259.

InParanoid

Q9CZL5.

OMA

TSHDCGE.

PhylomeDB

Q9CZL5.

Gene expression databases

ArrayExpress

Q9CZL5.

Bgee

Q9CZL5.

Genevestigator

Q9CZL5.

GermOnline

ENSMUSG00000021496. Mus musculus.

Family and domain databases

InterPro

IPR001533. Trans/pterin_deHydtase.
[Graphical view]

Gene3D

G3DSA:3.30.1360.20. Trans_pterinDh. 1 hit.

KO

K01724.

PANTHER

PTHR12599. Trans_pterinDh. 1 hit.

Pfam

PF01329. Pterin_4a. 1 hit.
[Graphical view]

SUPFAM

SSF55248. Trans_pterinDh. 1 hit.

ProtoNet

Search...

Other

NextBio

336495.

SOURCE

Search...

Entry information

Entry name

PHS2_MOUSE

Accession

Primary (citable) accession number: Q9CZL5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	June 16, 2009
Last modified:	November 16, 2011
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program