PLPHP_BOVIN
ID PLPHP_BOVIN Reviewed; 273 AA.
AC Q3T0G5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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:0000250|UniProtKB:O94903};
GN Name=PLPBP {ECO:0000255|HAMAP-Rule:MF_03225};
GN Synonyms=PROSC {ECO:0000255|HAMAP-Rule:MF_03225};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; BC102405; AAI02406.1; -; mRNA.
DR RefSeq; NP_001029529.1; NM_001034357.1.
DR AlphaFoldDB; Q3T0G5; -.
DR SMR; Q3T0G5; -.
DR STRING; 9913.ENSBTAP00000039600; -.
DR PaxDb; Q3T0G5; -.
DR PeptideAtlas; Q3T0G5; -.
DR PRIDE; Q3T0G5; -.
DR Ensembl; ENSBTAT00000039812; ENSBTAP00000039600; ENSBTAG00000011075.
DR GeneID; 509643; -.
DR KEGG; bta:509643; -.
DR CTD; 11212; -.
DR VEuPathDB; HostDB:ENSBTAG00000011075; -.
DR VGNC; VGNC:33043; PLPBP.
DR eggNOG; KOG3157; Eukaryota.
DR GeneTree; ENSGT00390000004928; -.
DR HOGENOM; CLU_059988_2_1_1; -.
DR InParanoid; Q3T0G5; -.
DR OMA; IEWHMIG; -.
DR OrthoDB; 1423577at2759; -.
DR TreeFam; TF314637; -.
DR Proteomes; UP000009136; Chromosome 27.
DR Bgee; ENSBTAG00000011075; Expressed in caput epididymis and 104 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..273
FT /note="Pyridoxal phosphate homeostasis protein"
FT /id="PRO_0000249596"
FT REGION 251..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:Q9Z2Y8"
FT MOD_RES 125
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Y8"
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 273 AA; 29943 MW; 46FBEF6CEA5E41FE CRC64;
MWKAGSMSAE LGIGFALRAV NERVQQAVAR RPRDLPAIQP RLVAVSKTKP ADMVIEAYSH
GQRTFGENYV QELLEKASNP QILSSCPEIK WHFIGHLQKQ NVNKLMAVPN LSMLETVDSV
KLADKVNSAW QKKGSPERLK VMVQINTSGE ASKHGLPPAE MAALVEHINA KCPSLEFVGL
MTIGSFGHDL SQGPNPDFQV LLSLREELCR KLGAPPEQVE LSMGMSVDFQ HAIEVGSTNV
RIGSTIFGER DYSKKTDKPA AELQAPEEVA QAH