HDHD1_MOUSE
ID HDHD1_MOUSE Reviewed; 234 AA.
AC Q9D5U5; Q5RL33; Q9D9A0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Pseudouridine-5'-phosphatase {ECO:0000250|UniProtKB:Q08623};
DE EC=3.1.3.96;
DE AltName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein 1;
DE AltName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein 1A;
DE AltName: Full=Pseudouridine-5'-monophosphatase;
DE Short=5'-PsiMPase;
GN Name=Pudp {ECO:0000250|UniProtKB:Q08623};
GN Synonyms=Hdhd1, Hdhd1a {ECO:0000312|MGI:MGI:1914615};
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=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Dephosphorylates pseudouridine 5'-phosphate, a potential
CC intermediate in rRNA degradation. Pseudouridine is then excreted intact
CC in urine. {ECO:0000250|UniProtKB:Q08623}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + psi-UMP = phosphate + pseudouridine;
CC Xref=Rhea:RHEA:10944, ChEBI:CHEBI:15377, ChEBI:CHEBI:17802,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58380; EC=3.1.3.96;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q08623};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR EMBL; AK007231; BAB24906.1; -; mRNA.
DR EMBL; AK014922; BAB29622.1; -; mRNA.
DR EMBL; BC048447; AAH48447.1; -; mRNA.
DR CCDS; CCDS29244.1; -.
DR RefSeq; NP_080384.2; NM_026108.3.
DR AlphaFoldDB; Q9D5U5; -.
DR SMR; Q9D5U5; -.
DR BioGRID; 212136; 1.
DR STRING; 10090.ENSMUSP00000057378; -.
DR PhosphoSitePlus; Q9D5U5; -.
DR PaxDb; Q9D5U5; -.
DR PRIDE; Q9D5U5; -.
DR ProteomicsDB; 269686; -.
DR DNASU; 67365; -.
DR GeneID; 67365; -.
DR KEGG; mmu:67365; -.
DR UCSC; uc008ewy.2; mouse.
DR CTD; 8226; -.
DR MGI; MGI:1914615; Pudp.
DR eggNOG; KOG2914; Eukaryota.
DR InParanoid; Q9D5U5; -.
DR OrthoDB; 1510544at2759; -.
DR PhylomeDB; Q9D5U5; -.
DR TreeFam; TF105946; -.
DR Reactome; R-MMU-73614; Pyrimidine salvage.
DR BioGRID-ORCS; 67365; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9D5U5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D5U5; protein.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:1990738; F:pseudouridine 5'-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd07529; HAD_AtGPP-like; 1.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR045228; Gpp1/Gpp2-like.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Reference proteome.
FT CHAIN 1..234
FT /note="Pseudouridine-5'-phosphatase"
FT /id="PRO_0000320103"
FT ACT_SITE 19
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 21
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 2..4
FT /note="AAA -> GGG (in Ref. 1; BAB24906)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="P -> H (in Ref. 1; BAB24906 and 2; AAH48447)"
FT /evidence="ECO:0000305"
FT CONFLICT 20..23
FT /note="LDGL -> REGF (in Ref. 1; BAB24906)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="L -> Q (in Ref. 1; BAB24906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 26161 MW; 246AFF9DCF2ED9FF CRC64;
MAAAVPVPQF RPVTPLIFDL DGLILNTEDL YTDVFEEICN RYGKKYNWDV KSLVMGKKAL
ETAQTIVEFL NLPISKEELL KESQEKLQMV LHTAGFMPGA EELIHHLKKH RLPFALATSS
ETVTFQTKTS RHTGFFGLFH HIVLGDDPEV KNGKPGMDIF LTCAKRFSPP PDPKDCLVFE
DSPNGVEAAI HCGMQVVMVP HENLSADLTR KATLVLSSLH DFKPELFGLP AFTE
