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Database: UniProt
Entry: Q61753
LinkDB: Q61753
Original site: Q61753 
ID   SERA_MOUSE              Reviewed;         533 AA.
AC   Q61753; Q3TEE5; Q75SV9; Q8C603;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   13-FEB-2019, entry version 165.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase;
DE            Short=3-PGDH;
DE            EC=1.1.1.95 {ECO:0000250|UniProtKB:O08651};
DE   AltName: Full=A10;
GN   Name=Phgdh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=14645240; DOI=10.1074/jbc.C300507200;
RA   Yoshida K., Furuya S., Osuka S., Mitoma J., Shinoda Y., Watanabe M.,
RA   Azuma N., Tanaka H., Hashikawa T., Itohara S., Hirabayashi Y.;
RT   "Targeted disruption of the mouse 3-phosphoglycerate dehydrogenase
RT   gene causes severe neurodevelopmental defects and results in embryonic
RT   lethality.";
RL   J. Biol. Chem. 279:3573-3577(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Testis, and 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 39-54; 248-268; 365-380 AND 523-533, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 49-533.
RA   Miller I.J., Bieker J.J.;
RT   "Sequences and expression patterns of murine erythroleukemia cDNAs
RT   isolated by subtractive cloning.";
RL   Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19114063; DOI=10.1016/j.neures.2008.12.002;
RA   Kawakami Y., Yoshida K., Yang J.H., Suzuki T., Azuma N., Sakai K.,
RA   Hashikawa T., Watanabe M., Yasuda K., Kuhara S., Hirabayashi Y.,
RA   Furuya S.;
RT   "Impaired neurogenesis in embryonic spinal cord of Phgdh knockout
RT   mice, a serine deficiency disorder model.";
RL   Neurosci. Res. 63:184-193(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-78, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21 AND LYS-58, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
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.,
RA   Zhang Y., 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).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-
CC       glycerate to 3-phosphonooxypyruvate, the first step of the
CC       phosphorylated L-serine biosynthesis pathway. Does not catalyze
CC       the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate
CC       and the reversible oxidation of (S)-malate to oxaloacetate.
CC       {ECO:0000250|UniProtKB:O08651}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phospho-D-glycerate + NAD(+) = 3-phosphooxypyruvate +
CC         H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58272; EC=1.1.1.95;
CC         Evidence={ECO:0000250|UniProtKB:O08651};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O08651}.
CC   -!- DISRUPTION PHENOTYPE: Decreased level of free serine, glycine,
CC       taurine, GABA, glutamine, and threonine in spinal cord and head.
CC       Impaired central nervous system (CNS) with shorter neural tube
CC       length and overall growth retardation. Severe atrophy at the
CC       thoracic level, particularly in the dorsal spinal cord. Poorly
CC       developed dorsal horn and adjacent mantle zone. Neurons fail to
CC       develop neurites, particularly commissural axonal fibers.
CC       {ECO:0000269|PubMed:19114063}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; AB128936; BAD08449.1; -; Genomic_DNA.
DR   EMBL; AK076815; BAC36494.1; -; mRNA.
DR   EMBL; AK169684; BAE41303.1; -; mRNA.
DR   EMBL; BC086668; AAH86668.1; -; mRNA.
DR   EMBL; BC110673; AAI10674.1; -; mRNA.
DR   EMBL; L21027; AAB67986.1; -; mRNA.
DR   CCDS; CCDS17663.1; -.
DR   RefSeq; NP_058662.2; NM_016966.3.
DR   UniGene; Mm.16898; -.
DR   UniGene; Mm.371997; -.
DR   ProteinModelPortal; Q61753; -.
DR   SMR; Q61753; -.
DR   BioGrid; 231770; 6.
DR   IntAct; Q61753; 8.
DR   MINT; Q61753; -.
DR   STRING; 10090.ENSMUSP00000064755; -.
DR   iPTMnet; Q61753; -.
DR   PhosphoSitePlus; Q61753; -.
DR   SwissPalm; Q61753; -.
DR   COMPLUYEAST-2DPAGE; Q61753; -.
DR   REPRODUCTION-2DPAGE; IPI00225961; -.
DR   REPRODUCTION-2DPAGE; Q61753; -.
DR   SWISS-2DPAGE; Q61753; -.
DR   EPD; Q61753; -.
DR   jPOST; Q61753; -.
DR   MaxQB; Q61753; -.
DR   PaxDb; Q61753; -.
DR   PeptideAtlas; Q61753; -.
DR   PRIDE; Q61753; -.
DR   Ensembl; ENSMUST00000065793; ENSMUSP00000064755; ENSMUSG00000053398.
DR   GeneID; 236539; -.
DR   KEGG; mmu:236539; -.
DR   UCSC; uc008qps.1; mouse.
DR   CTD; 26227; -.
DR   MGI; MGI:1355330; Phgdh.
DR   eggNOG; KOG0068; Eukaryota.
DR   eggNOG; COG0111; LUCA.
DR   GeneTree; ENSGT00940000155863; -.
DR   HOGENOM; HOG000136693; -.
DR   HOVERGEN; HBG054241; -.
DR   InParanoid; Q61753; -.
DR   KO; K00058; -.
DR   OMA; NIAGMQV; -.
DR   OrthoDB; 911009at2759; -.
DR   PhylomeDB; Q61753; -.
DR   TreeFam; TF314548; -.
DR   BRENDA; 1.1.1.95; 3474.
DR   Reactome; R-MMU-977347; Serine biosynthesis.
DR   UniPathway; UPA00135; UER00196.
DR   PRO; PR:Q61753; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000053398; Expressed in 255 organ(s), highest expression level in pancreas.
DR   ExpressionAtlas; Q61753; baseline and differential.
DR   Genevisible; Q61753; MM.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; ISO:MGI.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR   GO; GO:0070314; P:G1 to G0 transition; IMP:MGI.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IMP:MGI.
DR   GO; GO:0021782; P:glial cell development; IMP:MGI.
DR   GO; GO:0006541; P:glutamine metabolic process; IMP:MGI.
DR   GO; GO:0006544; P:glycine metabolic process; IMP:MGI.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006563; P:L-serine metabolic process; IMP:MGI.
DR   GO; GO:0021915; P:neural tube development; IMP:MGI.
DR   GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR   GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0021510; P:spinal cord development; IMP:MGI.
DR   GO; GO:0019530; P:taurine metabolic process; IMP:MGI.
DR   GO; GO:0006566; P:threonine metabolic process; IMP:MGI.
DR   Gene3D; 3.30.1330.90; -; 1.
DR   InterPro; IPR029009; ASB_dom_sf.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006236; PGDH.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF143548; SSF143548; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01327; PGDH; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Amino-acid biosynthesis; Complete proteome;
KW   Direct protein sequencing; Isopeptide bond; NAD; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Serine biosynthesis;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:O43175}.
FT   CHAIN         2    533       D-3-phosphoglycerate dehydrogenase.
FT                                /FTId=PRO_0000076014.
FT   NP_BIND     155    156       NAD. {ECO:0000250|UniProtKB:O43175}.
FT   NP_BIND     234    236       NAD. {ECO:0000250|UniProtKB:O43175}.
FT   NP_BIND     283    286       NAD. {ECO:0000250|UniProtKB:O43175}.
FT   ACT_SITE    236    236       {ECO:0000250}.
FT   ACT_SITE    265    265       {ECO:0000250}.
FT   ACT_SITE    283    283       Proton donor. {ECO:0000250}.
FT   BINDING      78     78       NAD. {ECO:0000250|UniProtKB:O43175}.
FT   BINDING     175    175       NAD. {ECO:0000250|UniProtKB:O43175}.
FT   BINDING     207    207       NAD; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:O43175}.
FT   BINDING     260    260       NAD. {ECO:0000250|UniProtKB:O43175}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:O43175}.
FT   MOD_RES      14     14       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O43175}.
FT   MOD_RES      21     21       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES      58     58       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES      78     78       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CROSSLNK     21     21       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:O43175}.
FT   CROSSLNK     21     21       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:O43175}.
FT   CONFLICT     77     77       G -> V (in Ref. 5; AAB67986).
FT                                {ECO:0000305}.
FT   CONFLICT     87     88       AA -> PP (in Ref. 5; AAB67986).
FT                                {ECO:0000305}.
FT   CONFLICT    124    124       A -> T (in Ref. 5; AAB67986).
FT                                {ECO:0000305}.
FT   CONFLICT    369    369       C -> W (in Ref. 5; AAB67986).
FT                                {ECO:0000305}.
FT   CONFLICT    377    377       G -> A (in Ref. 5; AAB67986).
FT                                {ECO:0000305}.
FT   CONFLICT    447    447       M -> K (in Ref. 2; BAC36494).
FT                                {ECO:0000305}.
SQ   SEQUENCE   533 AA;  56586 MW;  49CBF125AD6A12A5 CRC64;
     MAFANLRKVL ISDSLDPCCR KILQDGGLQV VEKQNLSKEE LIAELQDCEG LIVRSATKVT
     ADVINAAEKL QVVGRAGTGV DNVDLEAATR KGILVMNTPN GNSLSAAELT CGMIMCLARQ
     IPQATASMKD GKWDRKKFMG TELNGKTLGI LGLGRIGREV ATRMQSFGMK TVGYDPIISP
     EVAASFGVQQ LPLEEIWPLC DFITVHTPLL PSTTGLLNDS TFAQCKKGVR VVNCARGGIV
     DEGALLRALQ SGQCAGAALD VFTEEPPRDR ALVDHENVIS CPHLGASTKE AQSRCGEEIA
     VQFVDMVKGK SLTGVVNAQA LTSAFSPHTK PWIGLAEAMG TLMHAWAGSP KGTIQVVTQG
     TSLKNAGTCL SPAVIVGLLR EASKQADVNL VNAKLLVKEA GLNVTTSHNP GVPGEQGSGE
     CLLTVALAGA PYQAVGLVQG TTPMLQMLNG AVFRPEVPLR RGQPLLVFRA QPSDPGMLPT
     MIGLLAEAGV QLLSYQTSMV SDGEPWHVMG LSSLLPSLET WKQHVLEAFQ FCF
//
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