ID   KPRA_RAT                Reviewed;         356 AA.
AC   Q63468; Q63417;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Phosphoribosyl pyrophosphate synthase-associated protein 1;
DE            Short=PRPP synthase-associated protein 1;
DE   AltName: Full=39 kDa phosphoribosypyrophosphate synthase-associated protein;
DE            Short=PAP39;
GN   Name=Prpsap1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8132556; DOI=10.1016/s0021-9258(17)37198-3;
RA   Kita K., Ishizuka T., Ishijima S., Sonoda T., Tatibana M.;
RT   "A novel 39-kDa phosphoribosylpyrophosphate synthetase-associated protein
RT   of rat liver. Cloning, high sequence similarity to the catalytic subunits,
RT   and a negative regulatory role.";
RL   J. Biol. Chem. 269:8334-8340(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8611622; DOI=10.1016/0167-4781(95)00226-x;
RA   Ishizuka T., Sawa K., Kita K., Ino H., Sonoda T., Suzuki N., Tatibana M.;
RT   "Promoter region of the rat phosphoribosylpyrophosphate synthetase-
RT   associated protein 39.";
RL   Biochim. Biophys. Acta 1306:34-37(1996).
CC   -!- FUNCTION: Seems to play a negative regulatory role in 5-phosphoribose
CC       1-diphosphate synthesis.
CC   -!- SUBUNIT: Binds to PRPS1 and PRPS2.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       {ECO:0000305}.
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DR   EMBL; D26073; BAA05068.1; -; mRNA.
DR   EMBL; D44609; BAA08075.1; -; Genomic_DNA.
DR   PIR; A53433; A53433.
DR   AlphaFoldDB; Q63468; -.
DR   SMR; Q63468; -.
DR   IntAct; Q63468; 1.
DR   STRING; 10116.ENSRNOP00000013573; -.
DR   jPOST; Q63468; -.
DR   PaxDb; Q63468; -.
DR   PeptideAtlas; Q63468; -.
DR   PRIDE; Q63468; -.
DR   RGD; 620206; Prpsap1.
DR   eggNOG; KOG1503; Eukaryota.
DR   InParanoid; Q63468; -.
DR   PhylomeDB; Q63468; -.
DR   SABIO-RK; Q63468; -.
DR   PRO; PR:Q63468; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IDA:RGD.
DR   GO; GO:0030234; F:enzyme regulator activity; IMP:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0019900; F:kinase binding; IPI:RGD.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IBA:GO_Central.
DR   GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0033673; P:negative regulation of kinase activity; IDA:RGD.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; TAS:RGD.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 2.
DR   InterPro; IPR029099; Pribosyltran_N.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR005946; Rib-P_diPkinase.
DR   PANTHER; PTHR10210; PTHR10210; 1.
DR   Pfam; PF14572; Pribosyl_synth; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; SSF53271; 2.
DR   TIGRFAMs; TIGR01251; ribP_PPkin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Nucleotide biosynthesis;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..356
FT                   /note="Phosphoribosyl pyrophosphate synthase-associated
FT                   protein 1"
FT                   /id="PRO_0000141081"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14558"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14558"
FT   MOD_RES         215
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14558"
SQ   SEQUENCE   356 AA;  39436 MW;  C0B9BA9B45EB28E9 CRC64;
     MNAARTGYRV FSANSTAACT ELAKRITERL GAELGKSVVY QETNGETRVE IKESVRGQDI
     FIIQTIPRDV NTAVMELLIM AYALKTACAR NIIGVIPYFP YSKQSKMRKR GSIVCKLLAS
     MLAKAGLTHI ITMDLHQKEI QGFFCFPVDN LRASPFLLQY IQEEIPNYRN AVIVAKSPDA
     AKRAQSYAER LRLGLAVIHG EAQCTELDMD DGRHSPPMVK NATVHPGLEL PLMMAKEKPP
     ITVVGDVGGR IAIIVDDIID DVESFVAAAE TLKERGAYKI YVMATHGILS AEAPRLIEES
     PIDEVVVTNT VPHELQKLQC PKIKTVDISL ILSEAIRRIH NGESMAYLFR NITVDD