PHS_CHICK
ID PHS_CHICK Reviewed; 104 AA.
AC O73930;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
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 Short=cDcoH;
DE AltName: Full=Phenylalanine hydroxylase-stimulating protein;
DE AltName: Full=Pterin carbinolamine dehydratase;
DE Short=PCD;
GN Name=PCBD1; Synonyms=DCOH, PCBD;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9865610;
RA Bossow S., Riepl S., Igo-Kemenes T.;
RT "Characterization of the chicken and rat DCoH gene domains using an
RT improved ligation-mediated PCR method.";
RL Biol. Chem. 379:1359-1365(1998).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=11237869; DOI=10.1042/0264-6021:3540645;
RA Kim H., You S., Foster L.K., Farris J., Choi Y.-J., Foster D.N.;
RT "Differential expression of chicken dimerization cofactor of hepatocyte
RT nuclear factor-1 (DcoH) and its novel counterpart, DcoHalpha.";
RL Biochem. J. 354:645-653(2001).
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. {ECO:0000250|UniProtKB:P61459}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61459}. Nucleus
CC {ECO:0000250|UniProtKB:P61459}.
CC -!- TISSUE SPECIFICITY: The major tissues expressing cDcoH are
CC hypothalamus, kidney and liver. {ECO:0000269|PubMed:11237869}.
CC -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AJ005158; CAA06395.1; -; Genomic_DNA.
DR EMBL; AJ005157; CAA06394.1; -; mRNA.
DR RefSeq; NP_990236.1; NM_204905.1.
DR AlphaFoldDB; O73930; -.
DR SMR; O73930; -.
DR STRING; 9031.ENSGALP00000043457; -.
DR GeneID; 395729; -.
DR KEGG; gga:395729; -.
DR CTD; 5092; -.
DR VEuPathDB; HostDB:geneid_395729; -.
DR eggNOG; KOG4073; Eukaryota.
DR HOGENOM; CLU_081974_3_2_1; -.
DR InParanoid; O73930; -.
DR OrthoDB; 1588292at2759; -.
DR PhylomeDB; O73930; -.
DR PRO; PR:O73930; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
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"
FT CHAIN 2..104
FT /note="Pterin-4-alpha-carbinolamine dehydratase"
FT /id="PRO_0000063055"
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"
SQ SEQUENCE 104 AA; 11998 MW; 0786C7DF71A4EA99 CRC64;
MAGKAHRLNA EEREQLLPNL RAVGWNEVEG RDAIFKEFHF KDFNRAFGFM TRVALQAEKL
DHHPEWFNVY NKVHITLSTH ECTGLSERDI NLASFIEQVA ASLS
