PHS_MOUSE
ID PHS_MOUSE Reviewed; 104 AA.
AC P61458; P70519; P80095; Q9D930;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
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; Synonyms=Dcoh, Pcbd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=1763325; DOI=10.1126/science.1763325;
RA Mendel D.B., Khavari P.A., Conley P.B., Graves M.K., Hansen L.P., Admon A.,
RA Crabtree G.R.;
RT "Characterization of a cofactor that regulates dimerization of a mammalian
RT homeodomain protein.";
RL Science 254:1762-1767(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION BY LOW MAGNESIUM.
RX PubMed=24204001; DOI=10.1681/asn.2013040337;
RA Ferre S., de Baaij J.H., Ferreira P., Germann R., de Klerk J.B.,
RA Lavrijsen M., van Zeeland F., Venselaar H., Kluijtmans L.A.,
RA Hoenderop J.G., Bindels R.J.;
RT "Mutations in PCBD1 cause hypomagnesemia and renal magnesium wasting.";
RL J. Am. Soc. Nephrol. 25:574-586(2014).
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 -!- TISSUE SPECIFICITY: Mainly expressed in the liver, in pancreatic cells,
CC and in the kidney, especially in the distal convoluted tubule, in the
CC cortical thick ascending limb of Henle's loop and in the connecting
CC tubule. {ECO:0000269|PubMed:24204001}.
CC -!- INDUCTION: Up-regulated by a low magnesium-containing diet.
CC {ECO:0000269|PubMed:24204001}.
CC -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC family. {ECO:0000305}.
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DR EMBL; M83741; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK007401; BAB25014.1; -; mRNA.
DR EMBL; BC024354; AAH24354.1; -; mRNA.
DR CCDS; CCDS35913.1; -.
DR RefSeq; NP_079549.1; NM_025273.4.
DR AlphaFoldDB; P61458; -.
DR SMR; P61458; -.
DR BioGRID; 199068; 21.
DR IntAct; P61458; 17.
DR MINT; P61458; -.
DR STRING; 10090.ENSMUSP00000020298; -.
DR iPTMnet; P61458; -.
DR PhosphoSitePlus; P61458; -.
DR jPOST; P61458; -.
DR MaxQB; P61458; -.
DR PaxDb; P61458; -.
DR PeptideAtlas; P61458; -.
DR PRIDE; P61458; -.
DR ProteomicsDB; 288146; -.
DR Antibodypedia; 29081; 236 antibodies from 28 providers.
DR DNASU; 13180; -.
DR Ensembl; ENSMUST00000020298; ENSMUSP00000020298; ENSMUSG00000020098.
DR GeneID; 13180; -.
DR KEGG; mmu:13180; -.
DR UCSC; uc007ffj.3; mouse.
DR CTD; 5092; -.
DR MGI; MGI:94873; Pcbd1.
DR VEuPathDB; HostDB:ENSMUSG00000020098; -.
DR eggNOG; KOG4073; Eukaryota.
DR GeneTree; ENSGT00390000007221; -.
DR HOGENOM; CLU_081974_3_2_1; -.
DR InParanoid; P61458; -.
DR OMA; WAEKWNH; -.
DR OrthoDB; 1588292at2759; -.
DR PhylomeDB; P61458; -.
DR TreeFam; TF300188; -.
DR Reactome; R-MMU-8964208; Phenylalanine metabolism.
DR BioGRID-ORCS; 13180; 1 hit in 75 CRISPR screens.
DR PRO; PR:P61458; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P61458; protein.
DR Bgee; ENSMUSG00000020098; Expressed in right kidney and 190 other tissues.
DR ExpressionAtlas; P61458; baseline and differential.
DR Genevisible; P61458; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IPI:MGI.
DR GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0006558; P:L-phenylalanine metabolic process; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0043393; P:regulation of protein binding; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Activator; Cytoplasm; Direct protein sequencing; Lyase;
KW Nucleus; Reference proteome; Tetrahydrobiopterin biosynthesis;
KW 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_0000063053"
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; 13C798C25D9117E9 CRC64;
MAGKAHRLSA EERDQLLPNL RAVGWNEVEG RDAIFKQFHF KDFNRAFGFM TRVALQAEKL
DHHPEWFNVY NKVHITLSTH ECAGLSERDI NLASFIEQVA VSMT
