PHOP2_MOUSE
ID PHOP2_MOUSE Reviewed; 241 AA.
AC Q9D9M5; A2AR04; Q3V1M5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Pyridoxal phosphate phosphatase PHOSPHO2;
DE EC=3.1.3.74 {ECO:0000250|UniProtKB:Q8TCD6};
GN Name=Phospho2;
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=Head, and 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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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).
CC -!- FUNCTION: Phosphatase that has high activity toward pyridoxal 5'-
CC phosphate (PLP). Also active at much lower level toward pyrophosphate,
CC phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine,
CC fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate.
CC {ECO:0000250|UniProtKB:Q8TCD6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal;
CC Xref=Rhea:RHEA:20533, ChEBI:CHEBI:15377, ChEBI:CHEBI:17310,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:597326; EC=3.1.3.74;
CC Evidence={ECO:0000250|UniProtKB:Q8TCD6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8TCT1};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PHOSPHO
CC family. {ECO:0000305}.
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DR EMBL; AK006724; BAB24714.1; -; mRNA.
DR EMBL; AK132362; BAE21125.1; -; mRNA.
DR EMBL; AK159551; BAE35176.1; -; mRNA.
DR EMBL; AL845261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025612; AAH25612.1; -; mRNA.
DR EMBL; BC031523; AAH31523.1; -; mRNA.
DR CCDS; CCDS16099.1; -.
DR RefSeq; NP_082797.1; NM_028521.2.
DR RefSeq; XP_006500320.1; XM_006500257.1.
DR AlphaFoldDB; Q9D9M5; -.
DR SMR; Q9D9M5; -.
DR STRING; 10090.ENSMUSP00000028494; -.
DR PhosphoSitePlus; Q9D9M5; -.
DR EPD; Q9D9M5; -.
DR MaxQB; Q9D9M5; -.
DR PaxDb; Q9D9M5; -.
DR PeptideAtlas; Q9D9M5; -.
DR PRIDE; Q9D9M5; -.
DR ProteomicsDB; 288201; -.
DR Antibodypedia; 33816; 100 antibodies from 24 providers.
DR Ensembl; ENSMUST00000028494; ENSMUSP00000028494; ENSMUSG00000027088.
DR Ensembl; ENSMUST00000112266; ENSMUSP00000107885; ENSMUSG00000027088.
DR Ensembl; ENSMUST00000180290; ENSMUSP00000136471; ENSMUSG00000027088.
DR GeneID; 73373; -.
DR KEGG; mmu:73373; -.
DR UCSC; uc008jyp.1; mouse.
DR CTD; 493911; -.
DR MGI; MGI:1920623; Phospho2.
DR VEuPathDB; HostDB:ENSMUSG00000027088; -.
DR eggNOG; KOG3120; Eukaryota.
DR GeneTree; ENSGT00390000007741; -.
DR HOGENOM; CLU_068983_0_1_1; -.
DR InParanoid; Q9D9M5; -.
DR OMA; HNLADCF; -.
DR OrthoDB; 1454608at2759; -.
DR PhylomeDB; Q9D9M5; -.
DR TreeFam; TF300112; -.
DR BioGRID-ORCS; 73373; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Phospho2; mouse.
DR PRO; PR:Q9D9M5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D9M5; protein.
DR Bgee; ENSMUSG00000027088; Expressed in spermatocyte and 258 other tissues.
DR ExpressionAtlas; Q9D9M5; baseline and differential.
DR Genevisible; Q9D9M5; MM.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0033883; F:pyridoxal phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006384; HAD_hydro_PyrdxlP_Pase-like.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR016965; Pase_PHOSPHO-typ.
DR PANTHER; PTHR20889; PTHR20889; 1.
DR Pfam; PF06888; Put_Phosphatase; 1.
DR PIRSF; PIRSF031051; PyrdxlP_Pase_PHOSPHO2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01489; DKMTPPase-SF; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..241
FT /note="Pyridoxal phosphate phosphatase PHOSPHO2"
FT /id="PRO_0000068834"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT1"
FT ACT_SITE 10
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT1"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT1"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT CONFLICT 186
FT /note="P -> Q (in Ref. 1; BAE21125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 241 AA; 27563 MW; 9E0036C310AD26BE CRC64;
MKVLLVFDFD NTIIDDNSDT WIVQCAPDKK LPIELQDSYQ KGLWTEFMGR VFKYLRDEGV
KADELKRAVT SLPFTSGMIE LLSFLRMNKD RFDCIIISDS NSIFIDWVLE AAAFHDVFDH
VFTNPASFDS SGRLTVKNYH AHSCTRCPKN LCKNTVLGEF IDKQLQKGVR YTRIVYIGDG
GNDVCPVTFL KKNDVAMPRE GYTLHRTLAK MSQNLEPMES SIVVWSSGVE IISHLQFLIK
M
