PRPS3_HUMAN
ID PRPS3_HUMAN Reviewed; 318 AA.
AC P21108; Q6P5P6;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 3;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 1-like 1;
DE Short=PRPS1-like 1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase III;
DE Short=PRS-III;
GN Name=PRPS1L1; Synonyms=PRPS3, PRPSL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-11.
RC TISSUE=Testis;
RX PubMed=2168892; DOI=10.1016/s0021-9258(17)46249-1;
RA Taira M., Iizasa T., Shimada H., Kudoh J., Shimizu N., Tatibana M.;
RT "A human testis-specific mRNA for phosphoribosylpyrophosphate synthetase
RT that initiates from a non-AUG codon.";
RL J. Biol. Chem. 265:16491-16497(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-279.
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP)
CC that is essential for nucleotide synthesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC ChEBI:CHEBI:456215; EC=2.7.6.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Activated by magnesium and inorganic phosphate.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC D-ribose 5-phosphate (route I): step 1/1.
CC -!- SUBUNIT: Homodimer. The active form is probably a hexamer composed of 3
CC homodimers (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
CC -!- CAUTION: According to PubMed:2168892, this sequence initiates from a
CC non-AUG codon; N-terminal ACG codon did serve as a start codon.
CC {ECO:0000305}.
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DR EMBL; M57423; AAB59463.1; -; mRNA.
DR EMBL; BC062797; AAH62797.2; -; mRNA.
DR CCDS; CCDS47552.1; -.
DR PIR; A37893; KIHUR3.
DR RefSeq; NP_787082.1; NM_175886.2.
DR AlphaFoldDB; P21108; -.
DR SMR; P21108; -.
DR BioGRID; 128758; 72.
DR IntAct; P21108; 6.
DR STRING; 9606.ENSP00000424595; -.
DR GlyGen; P21108; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P21108; -.
DR PhosphoSitePlus; P21108; -.
DR BioMuta; PRPS1L1; -.
DR DMDM; 125585; -.
DR SWISS-2DPAGE; P21108; -.
DR EPD; P21108; -.
DR jPOST; P21108; -.
DR MassIVE; P21108; -.
DR MaxQB; P21108; -.
DR PaxDb; P21108; -.
DR PeptideAtlas; P21108; -.
DR PRIDE; P21108; -.
DR ProteomicsDB; 53835; -.
DR Antibodypedia; 25318; 153 antibodies from 21 providers.
DR DNASU; 221823; -.
DR Ensembl; ENST00000506618.5; ENSP00000424595.3; ENSG00000229937.9.
DR GeneID; 221823; -.
DR KEGG; hsa:221823; -.
DR MANE-Select; ENST00000506618.5; ENSP00000424595.3; NM_175886.3; NP_787082.1.
DR CTD; 221823; -.
DR GeneCards; PRPS1L1; -.
DR HGNC; HGNC:9463; PRPS1L1.
DR HPA; ENSG00000229937; Tissue enriched (testis).
DR MIM; 611566; gene.
DR neXtProt; NX_P21108; -.
DR OpenTargets; ENSG00000229937; -.
DR PharmGKB; PA33818; -.
DR VEuPathDB; HostDB:ENSG00000229937; -.
DR eggNOG; KOG1448; Eukaryota.
DR GeneTree; ENSGT00950000182803; -.
DR InParanoid; P21108; -.
DR OMA; CVISHFA; -.
DR OrthoDB; 1043963at2759; -.
DR PhylomeDB; P21108; -.
DR BioCyc; MetaCyc:HS11931-MON; -.
DR PathwayCommons; P21108; -.
DR Reactome; R-HSA-73843; 5-Phosphoribose 1-diphosphate biosynthesis.
DR SignaLink; P21108; -.
DR UniPathway; UPA00087; UER00172.
DR BioGRID-ORCS; 221823; 5 hits in 1000 CRISPR screens.
DR GenomeRNAi; 221823; -.
DR Pharos; P21108; Tdark.
DR PRO; PR:P21108; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P21108; protein.
DR Bgee; ENSG00000229937; Expressed in sperm and 25 other tissues.
DR ExpressionAtlas; P21108; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; ISS:UniProtKB.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR InterPro; IPR037515; Rib-P_diPkinase_bac.
DR PANTHER; PTHR10210; PTHR10210; 1.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2168892"
FT CHAIN 2..318
FT /note="Ribose-phosphate pyrophosphokinase 3"
FT /id="PRO_0000141078"
FT REGION 212..227
FT /note="Binding of phosphoribosylpyrophosphate"
FT /evidence="ECO:0000255"
FT BINDING 96..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT VARIANT 279
FT /note="E -> D (in dbSNP:rs3800962)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_050062"
SQ SEQUENCE 318 AA; 34839 MW; 6A4EDC798FB3B296 CRC64;
MPNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIDESVRG EDVYIVQSGC
GEINDSLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK DKSRSPISAK LVANMLSIAG
ADHIITMDLH ASQIQGFFDI PVDNLYAEPT VLKWIRENIP EWKNCIIVSP DAGGAKRVTS
IADQLNVDFA LIHKERKKAN EVDCIVLVGD VNDRVAILVD DMADTCVTIC LAADKLLSAG
ATRVYAILTH GIFSGPAISR INTACFEAVV VTNTIPQDEK MKHCSKIRVI DISMILAEAI
RRTHNGESVS YLFSHVPL
