PLPHP_MOUSE
ID PLPHP_MOUSE Reviewed; 274 AA.
AC Q9Z2Y8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000255|HAMAP-Rule:MF_03225};
DE Short=PLP homeostasis protein {ECO:0000255|HAMAP-Rule:MF_03225};
DE AltName: Full=Proline synthase co-transcribed bacterial homolog protein {ECO:0000255|HAMAP-Rule:MF_03225};
DE AltName: Full=Pyridoxal phosphate-binding protein {ECO:0000312|MGI:MGI:1891207};
GN Name=Plpbp {ECO:0000255|HAMAP-Rule:MF_03225, ECO:0000312|MGI:MGI:1891207};
GN Synonyms=Prosc {ECO:0000255|HAMAP-Rule:MF_03225,
GN ECO:0000312|MGI:MGI:1891207};
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 [GENOMIC DNA].
RX PubMed=10496079; DOI=10.1007/s100380050172;
RA Ikegawa S., Isomura M., Koshizuka Y., Nakamura Y.;
RT "Cloning and characterization of human and mouse PROSC (proline synthetase
RT co-transcribed) genes.";
RL J. Hum. Genet. 44:337-342(1999).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-69, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-125, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which may be
CC involved in intracellular homeostatic regulation of pyridoxal 5'-
CC phosphate (PLP), the active form of vitamin B6. {ECO:0000255|HAMAP-
CC Rule:MF_03225}.
CC -!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
CC YggS/PROSC family. {ECO:0000255|HAMAP-Rule:MF_03225}.
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DR EMBL; AB018567; BAA36843.1; -; Genomic_DNA.
DR CCDS; CCDS40310.1; -.
DR RefSeq; NP_473398.1; NM_054057.4.
DR AlphaFoldDB; Q9Z2Y8; -.
DR SMR; Q9Z2Y8; -.
DR BioGRID; 227885; 17.
DR STRING; 10090.ENSMUSP00000033875; -.
DR iPTMnet; Q9Z2Y8; -.
DR PhosphoSitePlus; Q9Z2Y8; -.
DR EPD; Q9Z2Y8; -.
DR jPOST; Q9Z2Y8; -.
DR MaxQB; Q9Z2Y8; -.
DR PaxDb; Q9Z2Y8; -.
DR PRIDE; Q9Z2Y8; -.
DR ProteomicsDB; 289623; -.
DR Antibodypedia; 4465; 294 antibodies from 24 providers.
DR DNASU; 114863; -.
DR Ensembl; ENSMUST00000033875; ENSMUSP00000033875; ENSMUSG00000031485.
DR GeneID; 114863; -.
DR KEGG; mmu:114863; -.
DR UCSC; uc009lht.1; mouse.
DR CTD; 11212; -.
DR MGI; MGI:1891207; Plpbp.
DR VEuPathDB; HostDB:ENSMUSG00000031485; -.
DR eggNOG; KOG3157; Eukaryota.
DR GeneTree; ENSGT00390000004928; -.
DR HOGENOM; CLU_059988_2_1_1; -.
DR InParanoid; Q9Z2Y8; -.
DR OMA; IEWHMIG; -.
DR OrthoDB; 1423577at2759; -.
DR PhylomeDB; Q9Z2Y8; -.
DR TreeFam; TF314637; -.
DR BioGRID-ORCS; 114863; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Prosc; mouse.
DR PRO; PR:Q9Z2Y8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9Z2Y8; protein.
DR Bgee; ENSMUSG00000031485; Expressed in gastrula and 256 other tissues.
DR ExpressionAtlas; Q9Z2Y8; baseline and differential.
DR Genevisible; Q9Z2Y8; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR Gene3D; 3.20.20.10; -; 1.
DR HAMAP; MF_02087; PLP_homeostasis; 1.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR029066; PLP-binding_barrel.
DR InterPro; IPR011078; PyrdxlP_homeostasis.
DR PANTHER; PTHR10146; PTHR10146; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR TIGRFAMs; TIGR00044; TIGR00044; 1.
DR PROSITE; PS01211; UPF0001; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..274
FT /note="Pyridoxal phosphate homeostasis protein"
FT /id="PRO_0000163211"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94903"
FT MOD_RES 47
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03225"
FT MOD_RES 69
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 125
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94903"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94903"
SQ SEQUENCE 274 AA; 30049 MW; 358C67207DB11113 CRC64;
MLRGGSMTAE LGVGFALRAV NERVQQSVAR RPRDLPAIQP RLVAVSKTKP ADMVIEAYGH
GQRTFGENYV QELLEKASNP KILSSCPEIK WHFIGHLQKQ NVNKLMAVPN LSMLETVDSV
KLADKVNSSW QKKGPTEPLK VMVQINTSGE DSKHGLLPSE TIAVVEHIKA SCPSLEFVGL
MTIGSFGHDL SQGPNPDFQR LLTLRRELCE KLGIPVEQVE LSMGMSMDFQ HAIEVGSTNV
RIGSTIFGER DYSKKPALDK TADAKASVPL VQGH
