RPIA_HUMAN
ID RPIA_HUMAN Reviewed; 311 AA.
AC P49247; Q541P9; Q96BJ6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Ribose-5-phosphate isomerase {ECO:0000305};
DE EC=5.3.1.6 {ECO:0000269|PubMed:14988808};
DE AltName: Full=Phosphoriboisomerase;
GN Name=RPIA {ECO:0000312|HGNC:HGNC:10297}; Synonyms=RPI;
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].
RA Guo J.H., Yu L.;
RT "Cloning and characterization of human ribose 5-phosphate isomerase (RPI)
RT gene.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 186-311.
RC TISSUE=B-cell;
RX PubMed=7758956; DOI=10.1016/0378-1119(94)00901-4;
RA Apel T.W., Scherer A., Adachi T., Auch D., Ayane M., Reth M.;
RT "The ribose 5-phosphate isomerase-encoding gene is located immediately
RT downstream from that encoding murine immunoglobulin kappa.";
RL Gene 156:191-197(1995).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-52, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [7]
RP VARIANT RPIAD VAL-135, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14988808; DOI=10.1086/383204;
RA Huck J.H.J., Verhoeven N.M., Struys E.A., Salomons G.S., Jakobs C.,
RA van der Knaap M.S.;
RT "Ribose-5-phosphate isomerase deficiency: new inborn error in the pentose
RT phosphate pathway associated with a slowly progressive
RT leukoencephalopathy.";
RL Am. J. Hum. Genet. 74:745-751(2004).
CC -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to
CC ribulose 5-phosphate and participates in the first step of the non-
CC oxidative branch of the pentose phosphate pathway.
CC {ECO:0000269|PubMed:14988808}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273;
CC EC=5.3.1.6; Evidence={ECO:0000269|PubMed:14988808};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14658;
CC Evidence={ECO:0000305|PubMed:14988808};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14659;
CC Evidence={ECO:0000305|PubMed:14988808};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose
CC 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step
CC 1/1. {ECO:0000269|PubMed:14988808}.
CC -!- INTERACTION:
CC P49247; Q8N5M1: ATPAF2; NbExp=12; IntAct=EBI-744831, EBI-1166928;
CC P49247; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-744831, EBI-725606;
CC P49247; Q6IPU0: CENPP; NbExp=8; IntAct=EBI-744831, EBI-10250303;
CC P49247; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-744831, EBI-742054;
CC P49247; Q75MZ5: FOXP2; NbExp=4; IntAct=EBI-744831, EBI-10255915;
CC P49247; Q9H8Y8: GORASP2; NbExp=8; IntAct=EBI-744831, EBI-739467;
CC P49247; Q9UJY1: HSPB8; NbExp=3; IntAct=EBI-744831, EBI-739074;
CC P49247; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-744831, EBI-739832;
CC P49247; Q96HA8: NTAQ1; NbExp=8; IntAct=EBI-744831, EBI-741158;
CC P49247; P22061: PCMT1; NbExp=3; IntAct=EBI-744831, EBI-353343;
CC P49247; P22061-2: PCMT1; NbExp=4; IntAct=EBI-744831, EBI-12386584;
CC P49247; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-744831, EBI-79165;
CC P49247; Q06124: PTPN11; NbExp=4; IntAct=EBI-744831, EBI-297779;
CC P49247; Q9H0X6: RNF208; NbExp=3; IntAct=EBI-744831, EBI-751555;
CC P49247; P49247: RPIA; NbExp=4; IntAct=EBI-744831, EBI-744831;
CC P49247; O00560: SDCBP; NbExp=3; IntAct=EBI-744831, EBI-727004;
CC P49247; O75716: STK16; NbExp=4; IntAct=EBI-744831, EBI-749295;
CC P49247; Q99757: TXN2; NbExp=6; IntAct=EBI-744831, EBI-2932492;
CC -!- DISEASE: Ribose 5-phosphate isomerase deficiency (RPIAD) [MIM:608611]:
CC An autosomal recessive inborn error of polyols metabolism characterized
CC by highly elevated level of ribitol and arabitol in brain and body
CC fluids. Clinical features include leukoencephalopathy, psychomotor
CC retardation from early life, neurologic regression, and a mild
CC sensorimotor neuropathy. {ECO:0000269|PubMed:14988808}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK95569.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY050633; AAK95569.1; ALT_FRAME; mRNA.
DR EMBL; BC015529; AAH15529.2; -; mRNA.
DR EMBL; L35035; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS2004.2; -.
DR RefSeq; NP_653164.2; NM_144563.2.
DR AlphaFoldDB; P49247; -.
DR SMR; P49247; -.
DR BioGRID; 116594; 60.
DR IntAct; P49247; 32.
DR MINT; P49247; -.
DR STRING; 9606.ENSP00000283646; -.
DR DrugBank; DB01756; 4-phospho-L-threonic acid.
DR GlyGen; P49247; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P49247; -.
DR PhosphoSitePlus; P49247; -.
DR BioMuta; RPIA; -.
DR DMDM; 156637353; -.
DR EPD; P49247; -.
DR jPOST; P49247; -.
DR MassIVE; P49247; -.
DR MaxQB; P49247; -.
DR PaxDb; P49247; -.
DR PeptideAtlas; P49247; -.
DR PRIDE; P49247; -.
DR ProteomicsDB; 55976; -.
DR Antibodypedia; 32248; 165 antibodies from 26 providers.
DR DNASU; 22934; -.
DR Ensembl; ENST00000283646.5; ENSP00000283646.3; ENSG00000153574.9.
DR GeneID; 22934; -.
DR KEGG; hsa:22934; -.
DR MANE-Select; ENST00000283646.5; ENSP00000283646.3; NM_144563.3; NP_653164.2.
DR UCSC; uc002ste.4; human.
DR CTD; 22934; -.
DR DisGeNET; 22934; -.
DR GeneCards; RPIA; -.
DR HGNC; HGNC:10297; RPIA.
DR HPA; ENSG00000153574; Tissue enhanced (bone).
DR MalaCards; RPIA; -.
DR MIM; 180430; gene.
DR MIM; 608611; phenotype.
DR neXtProt; NX_P49247; -.
DR OpenTargets; ENSG00000153574; -.
DR Orphanet; 440706; Ribose-5-P isomerase deficiency.
DR PharmGKB; PA34659; -.
DR VEuPathDB; HostDB:ENSG00000153574; -.
DR eggNOG; KOG3075; Eukaryota.
DR GeneTree; ENSGT00390000004352; -.
DR HOGENOM; CLU_056590_0_2_1; -.
DR InParanoid; P49247; -.
DR OMA; YDWDEVN; -.
DR OrthoDB; 1074761at2759; -.
DR PhylomeDB; P49247; -.
DR TreeFam; TF105758; -.
DR BRENDA; 5.3.1.6; 2681.
DR PathwayCommons; P49247; -.
DR Reactome; R-HSA-5659996; RPIA deficiency: failed conversion of R5P to RU5P.
DR Reactome; R-HSA-6791461; RPIA deficiency: failed conversion of RU5P to R5P.
DR Reactome; R-HSA-71336; Pentose phosphate pathway.
DR SignaLink; P49247; -.
DR SIGNOR; P49247; -.
DR UniPathway; UPA00115; UER00412.
DR BioGRID-ORCS; 22934; 223 hits in 1093 CRISPR screens.
DR ChiTaRS; RPIA; human.
DR GenomeRNAi; 22934; -.
DR Pharos; P49247; Tbio.
DR PRO; PR:P49247; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P49247; protein.
DR Bgee; ENSG00000153574; Expressed in secondary oocyte and 204 other tissues.
DR Genevisible; P49247; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0048029; F:monosaccharide binding; IEA:Ensembl.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; EXP:Reactome.
DR GO; GO:0006014; P:D-ribose metabolic process; IBA:GO_Central.
DR GO; GO:0006098; P:pentose-phosphate shunt; TAS:Reactome.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR GO; GO:0019693; P:ribose phosphate metabolic process; IEA:Ensembl.
DR CDD; cd01398; RPI_A; 1.
DR HAMAP; MF_00170; Rib_5P_isom_A; 1.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR020672; Ribose5P_isomerase_typA_subgr.
DR InterPro; IPR004788; Ribose5P_isomerase_type_A.
DR PANTHER; PTHR11934; PTHR11934; 1.
DR Pfam; PF06026; Rib_5-P_isom_A; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00021; rpiA; 1.
PE 1: Evidence at protein level;
KW Disease variant; Isomerase; Methylation; Neuropathy; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..311
FT /note="Ribose-5-phosphate isomerase"
FT /id="PRO_0000158521"
FT REGION 22..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 135
FT /note="A -> V (in RPIAD; dbSNP:rs121918591)"
FT /evidence="ECO:0000269|PubMed:14988808"
FT /id="VAR_019122"
FT CONFLICT 207
FT /note="D -> V (in Ref. 3; L35035)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="L -> V (in Ref. 3; L35035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 33269 MW; 4ED587A40F10223D CRC64;
MQRPGPFSTL YGRVLAPLPG RAGGAASGGG GNSWDLPGSH VRLPGRAQSG TRGGAGNTST
SCGDSNSICP APSTMSKAEE AKKLAGRAAV ENHVRNNQVL GIGSGSTIVH AVQRIAERVK
QENLNLVCIP TSFQARQLIL QYGLTLSDLD RHPEIDLAID GADEVDADLN LIKGGGGCLT
QEKIVAGYAS RFIVIADFRK DSKNLGDQWH KGIPIEVIPM AYVPVSRAVS QKFGGVVELR
MAVNKAGPVV TDNGNFILDW KFDRVHKWSE VNTAIKMIPG VVDTGLFINM AERVYFGMQD
GSVNMREKPF C
