PHS2_MOUSE
ID PHS2_MOUSE Reviewed; 136 AA.
AC Q9CZL5;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Pterin-4-alpha-carbinolamine dehydratase 2;
DE Short=PHS 2;
DE EC=4.2.1.96;
DE AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase 2;
DE AltName: Full=DcoH-like protein DCoHm;
DE AltName: Full=Dimerization cofactor of hepatocyte nuclear factor 1 from muscle;
DE AltName: Full=HNF-1-alpha dimerization cofactor;
GN Name=Pcbd2; Synonyms=Dcoh2, Dcohm;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-136.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-131, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-120; LYS-124 AND LYS-131, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-124 AND LYS-131, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 34-136, SUBUNIT, AND FUNCTION AS A
RP PHS.
RX PubMed=15182178; DOI=10.1021/bi049620t;
RA Rose R.B., Pullen K.E., Bayle J.H., Crabtree G.R., Alber T.;
RT "Biochemical and structural basis for partially redundant enzymatic and
RT transcriptional functions of DCoH and DCoH2.";
RL Biochemistry 43:7345-7355(2004).
CC -!- FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both
CC prevent the formation of 7-pterins and accelerate the formation of
CC quinonoid-BH2 (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Regulates the dimerization of homeodomain protein HNF-1-alpha
CC and enhances its transcriptional activity.
CC {ECO:0000269|PubMed:15182178}.
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 -!- SUBUNIT: Homotetramer. Interacts with DYRK1B (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH28642.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB28260.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC028642; AAH28642.1; ALT_INIT; mRNA.
DR EMBL; AK012465; BAB28260.1; ALT_INIT; mRNA.
DR CCDS; CCDS26554.1; -.
DR RefSeq; NP_082557.1; NM_028281.1.
DR PDB; 1RU0; X-ray; 1.60 A; A/B=36-136.
DR PDB; 4WIL; X-ray; 1.36 A; A/B=34-136.
DR PDBsum; 1RU0; -.
DR PDBsum; 4WIL; -.
DR AlphaFoldDB; Q9CZL5; -.
DR SMR; Q9CZL5; -.
DR BioGRID; 215439; 4.
DR CORUM; Q9CZL5; -.
DR STRING; 10090.ENSMUSP00000021958; -.
DR iPTMnet; Q9CZL5; -.
DR PhosphoSitePlus; Q9CZL5; -.
DR EPD; Q9CZL5; -.
DR jPOST; Q9CZL5; -.
DR MaxQB; Q9CZL5; -.
DR PaxDb; Q9CZL5; -.
DR PeptideAtlas; Q9CZL5; -.
DR PRIDE; Q9CZL5; -.
DR ProteomicsDB; 289413; -.
DR Antibodypedia; 26376; 63 antibodies from 18 providers.
DR DNASU; 72562; -.
DR Ensembl; ENSMUST00000021958; ENSMUSP00000021958; ENSMUSG00000021496.
DR GeneID; 72562; -.
DR KEGG; mmu:72562; -.
DR UCSC; uc007qrz.1; mouse.
DR CTD; 84105; -.
DR MGI; MGI:1919812; Pcbd2.
DR VEuPathDB; HostDB:ENSMUSG00000021496; -.
DR eggNOG; KOG4073; Eukaryota.
DR GeneTree; ENSGT00390000007221; -.
DR HOGENOM; CLU_081974_3_1_1; -.
DR InParanoid; Q9CZL5; -.
DR OrthoDB; 1588292at2759; -.
DR PhylomeDB; Q9CZL5; -.
DR TreeFam; TF300188; -.
DR BRENDA; 4.2.1.96; 3474.
DR BioGRID-ORCS; 72562; 0 hits in 59 CRISPR screens.
DR ChiTaRS; Pcbd2; mouse.
DR EvolutionaryTrace; Q9CZL5; -.
DR PRO; PR:Q9CZL5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9CZL5; protein.
DR Bgee; ENSMUSG00000021496; Expressed in renal corpuscle and 260 other tissues.
DR ExpressionAtlas; Q9CZL5; baseline and differential.
DR Genevisible; Q9CZL5; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; IPI:MGI.
DR GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0004505; F:phenylalanine 4-monooxygenase activity; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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 3D-structure; Acetylation; Lyase; Reference proteome;
KW Tetrahydrobiopterin biosynthesis.
FT CHAIN 1..136
FT /note="Pterin-4-alpha-carbinolamine dehydratase 2"
FT /id="PRO_0000063058"
FT MOD_RES 120
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 120
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 124
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 124
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 131
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 131
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:4WIL"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:4WIL"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:4WIL"
FT HELIX 76..93
FT /evidence="ECO:0007829|PDB:4WIL"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:4WIL"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4WIL"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:4WIL"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:4WIL"
SQ SEQUENCE 136 AA; 14830 MW; 5E447CDD57CF7496 CRC64;
MVAAAAVAVA AVGARSAGRW LAALRSPGAS RAAMSSDAQW LTAEERDQLI PGLKAAGWSE
LSERDAIYKE FSFKNFNQAF GFMSRVALQA EKMNHHPEWF NVYNKVQITL TSHDCGGLTK
RDVKLAQFIE KAAASL
