PHS_BOVIN
ID PHS_BOVIN Reviewed; 104 AA.
AC Q3ZBD3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Pterin-4-alpha-carbinolamine dehydratase;
DE Short=PHS;
DE EC=4.2.1.96 {ECO:0000250|UniProtKB:P61459};
DE AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase;
DE AltName: Full=Dimerization cofactor of hepatocyte nuclear factor 1-alpha;
DE Short=DCoH;
DE Short=Dimerization cofactor of HNF1;
DE AltName: Full=Phenylalanine hydroxylase-stimulating protein;
DE AltName: Full=Pterin carbinolamine dehydratase;
DE Short=PCD;
GN Name=PCBD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both
CC prevent the formation of 7-pterins and accelerate the formation of
CC quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates
CC the dimerization of homeodomain protein HNF1A and enhances its
CC transcriptional activity (By similarity). Also acts as a coactivator
CC for HNF1B-dependent transcription (By similarity).
CC {ECO:0000250|UniProtKB:P61457, ECO:0000250|UniProtKB:P61459}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin =
CC (6R)-L-erythro-6,7-dihydrobiopterin + H2O; Xref=Rhea:RHEA:11920,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15642, ChEBI:CHEBI:43120; EC=4.2.1.96;
CC Evidence={ECO:0000250|UniProtKB:P61459};
CC -!- SUBUNIT: Homotetramer and homodimer. Heterotetramer with HNF1A; formed
CC by a dimer of dimers (By similarity). Interacts with HNF1B (via HNF-p1
CC domain); the interaction increases HNF1B transactivation activity (By
CC similarity). {ECO:0000250|UniProtKB:P35680,
CC ECO:0000250|UniProtKB:P61459}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61459}. Nucleus
CC {ECO:0000250|UniProtKB:P61459}. Note=Recruited to the nucleus through
CC the interaction with HNF1B. {ECO:0000250|UniProtKB:P35680}.
CC -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI03435.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC103434; AAI03435.1; ALT_INIT; mRNA.
DR RefSeq; NP_001193403.1; NM_001206474.1.
DR AlphaFoldDB; Q3ZBD3; -.
DR SMR; Q3ZBD3; -.
DR STRING; 9913.ENSBTAP00000015750; -.
DR PaxDb; Q3ZBD3; -.
DR PeptideAtlas; Q3ZBD3; -.
DR PRIDE; Q3ZBD3; -.
DR Ensembl; ENSBTAT00000015750; ENSBTAP00000015750; ENSBTAG00000011866.
DR GeneID; 530736; -.
DR KEGG; bta:530736; -.
DR CTD; 5092; -.
DR VEuPathDB; HostDB:ENSBTAG00000011866; -.
DR VGNC; VGNC:32612; PCBD1.
DR eggNOG; KOG4073; Eukaryota.
DR GeneTree; ENSGT00390000007221; -.
DR HOGENOM; CLU_081974_3_2_1; -.
DR InParanoid; Q3ZBD3; -.
DR OMA; WAEKWNH; -.
DR OrthoDB; 1588292at2759; -.
DR TreeFam; TF300188; -.
DR Reactome; R-BTA-8964208; Phenylalanine metabolism.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000011866; Expressed in liver and 104 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IEA:Ensembl.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1360.20; -; 1.
DR HAMAP; MF_00434; Pterin_4_alpha; 1.
DR InterPro; IPR036428; PCD_sf.
DR InterPro; IPR001533; Pterin_deHydtase.
DR PANTHER; PTHR12599; PTHR12599; 1.
DR Pfam; PF01329; Pterin_4a; 1.
DR SUPFAM; SSF55248; SSF55248; 1.
PE 3: Inferred from homology;
KW Acetylation; Activator; Cytoplasm; Lyase; Nucleus; Reference proteome;
KW Tetrahydrobiopterin biosynthesis; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61457"
FT CHAIN 2..104
FT /note="Pterin-4-alpha-carbinolamine dehydratase"
FT /id="PRO_0000315210"
FT BINDING 61..63
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 78..81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P61457"
SQ SEQUENCE 104 AA; 11986 MW; 997DF8C2417FFD56 CRC64;
MAGKAHRLSA EERDQLLPNL RAVGWNELEG RDAIFKQFHF KDFNRAFGFM TRVALQAEKL
DHHPEWFNVY NKVHITLSTH ECAGLSERDV NLASFIEQVA VSMT
