SERB_MOUSE
ID SERB_MOUSE Reviewed; 225 AA.
AC Q99LS3; Q3TI16; Q5XHW3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Phosphoserine phosphatase {ECO:0000250|UniProtKB:P78330};
DE Short=PSP {ECO:0000250|UniProtKB:P78330};
DE Short=PSPase {ECO:0000250|UniProtKB:P78330};
DE EC=3.1.3.3 {ECO:0000250|UniProtKB:P78330};
DE AltName: Full=O-phosphoserine phosphohydrolase {ECO:0000250|UniProtKB:P78330};
GN Name=Psph {ECO:0000312|MGI:MGI:97788};
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=BALB/cJ, and NOD; TISSUE=Thymus;
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 STRAIN=Czech II; TISSUE=Mammary tumor;
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=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and
RC 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: Catalyzes the last irreversible step in the biosynthesis of
CC L-serine from carbohydrates, the dephosphorylation of O-phospho-L-
CC serine to L-serine. L-serine can then be used in protein synthesis, to
CC produce other amino acids, in nucleotide metabolism or in glutathione
CC synthesis, or can be racemized to D-serine, a neuromodulator. May also
CC act on O-phospho-D-serine. {ECO:0000250|UniProtKB:P78330}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-serine = L-serine + phosphate;
CC Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3;
CC Evidence={ECO:0000250|UniProtKB:P78330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21209;
CC Evidence={ECO:0000250|UniProtKB:P78330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-D-serine = D-serine + phosphate;
CC Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3;
CC Evidence={ECO:0000250|UniProtKB:P78330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24874;
CC Evidence={ECO:0000250|UniProtKB:P78330};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P78330};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P78330};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3. {ECO:0000250|UniProtKB:P78330}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P78330}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P78330}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC {ECO:0000305}.
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DR EMBL; AK088865; BAC40622.1; -; mRNA.
DR EMBL; AK168048; BAE40030.1; -; mRNA.
DR EMBL; BC002251; AAH02251.1; -; mRNA.
DR CCDS; CCDS19699.1; -.
DR RefSeq; NP_598661.1; NM_133900.4.
DR RefSeq; XP_006504337.1; XM_006504274.3.
DR RefSeq; XP_017176063.1; XM_017320574.1.
DR AlphaFoldDB; Q99LS3; -.
DR SMR; Q99LS3; -.
DR BioGRID; 221509; 4.
DR IntAct; Q99LS3; 1.
DR MINT; Q99LS3; -.
DR STRING; 10090.ENSMUSP00000031399; -.
DR iPTMnet; Q99LS3; -.
DR PhosphoSitePlus; Q99LS3; -.
DR UCD-2DPAGE; Q99LS3; -.
DR EPD; Q99LS3; -.
DR MaxQB; Q99LS3; -.
DR PaxDb; Q99LS3; -.
DR PeptideAtlas; Q99LS3; -.
DR PRIDE; Q99LS3; -.
DR ProteomicsDB; 256780; -.
DR Antibodypedia; 13863; 347 antibodies from 33 providers.
DR DNASU; 100678; -.
DR Ensembl; ENSMUST00000031399; ENSMUSP00000031399; ENSMUSG00000029446.
DR GeneID; 100678; -.
DR KEGG; mmu:100678; -.
DR UCSC; uc008zth.2; mouse.
DR CTD; 5723; -.
DR MGI; MGI:97788; Psph.
DR VEuPathDB; HostDB:ENSMUSG00000029446; -.
DR eggNOG; KOG1615; Eukaryota.
DR GeneTree; ENSGT00390000003115; -.
DR HOGENOM; CLU_036368_2_1_1; -.
DR InParanoid; Q99LS3; -.
DR OMA; RAQYYVT; -.
DR OrthoDB; 1009123at2759; -.
DR PhylomeDB; Q99LS3; -.
DR TreeFam; TF315024; -.
DR BRENDA; 3.1.3.3; 3474.
DR Reactome; R-MMU-977347; Serine biosynthesis.
DR UniPathway; UPA00135; UER00198.
DR BioGRID-ORCS; 100678; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Psph; mouse.
DR PRO; PR:Q99LS3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99LS3; protein.
DR Bgee; ENSMUSG00000029446; Expressed in seminal vesicle and 279 other tissues.
DR ExpressionAtlas; Q99LS3; baseline and differential.
DR Genevisible; Q99LS3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0006564; P:L-serine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006563; P:L-serine metabolic process; ISS:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR004469; PSP.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00338; serB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Reference proteome; Serine biosynthesis.
FT CHAIN 1..225
FT /note="Phosphoserine phosphatase"
FT /id="PRO_0000156880"
FT ACT_SITE 20
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT ACT_SITE 22
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 20..22
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 20
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 52
FT /ligand="O-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57524"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 53
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 109..111
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 109..111
FT /ligand="O-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57524"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 158
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 158
FT /ligand="O-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57524"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 182
FT /ligand="O-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57524"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT BINDING 182
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P78330"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P78330"
SQ SEQUENCE 225 AA; 25096 MW; CCEE55B48787D10A CRC64;
MVSHSELRKL FCSADAVCFD VDSTVIREEG IDELAKFCGV EAAVSEMTRR AMGGALPFKD
ALTQRLALIQ PSRDQVQRLL AEHPPHLTPG IRELVSRLQE RNVQVFLISG GFRSIVEHVA
AKLNIPTTNV FANRLKFYFN GEYAGFDEMQ PTAESGGKGK VIRFLKEKFH FKKIIMIGDG
ATDMEACPPA DAFIGFGGNV IRQQVKDNAK WYITDFVELL GELEE
