RPIA_MOUSE
ID RPIA_MOUSE Reviewed; 303 AA.
AC P47968; Q3UVI8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ribose-5-phosphate isomerase;
DE EC=5.3.1.6 {ECO:0000269|PubMed:7758956};
DE AltName: Full=Phosphoriboisomerase;
GN Name=Rpia; Synonyms=Rpi;
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 [MRNA], CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Pre-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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-303.
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 52-303.
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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).
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:7758956};
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:7758956}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in testis.
CC {ECO:0000269|PubMed:7758956}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC42060.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE23281.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L35034; AAC42060.1; ALT_INIT; mRNA.
DR EMBL; AK137235; BAE23281.1; ALT_INIT; mRNA.
DR EMBL; BC053526; AAH53526.2; -; mRNA.
DR CCDS; CCDS39504.1; -.
DR PIR; I53951; I53951.
DR RefSeq; NP_033101.2; NM_009075.2.
DR AlphaFoldDB; P47968; -.
DR SMR; P47968; -.
DR BioGRID; 202965; 12.
DR STRING; 10090.ENSMUSP00000064158; -.
DR iPTMnet; P47968; -.
DR PhosphoSitePlus; P47968; -.
DR SwissPalm; P47968; -.
DR EPD; P47968; -.
DR MaxQB; P47968; -.
DR PaxDb; P47968; -.
DR PeptideAtlas; P47968; -.
DR PRIDE; P47968; -.
DR ProteomicsDB; 300481; -.
DR Antibodypedia; 32248; 165 antibodies from 26 providers.
DR DNASU; 19895; -.
DR Ensembl; ENSMUST00000066134; ENSMUSP00000064158; ENSMUSG00000053604.
DR GeneID; 19895; -.
DR KEGG; mmu:19895; -.
DR UCSC; uc009cfy.1; mouse.
DR CTD; 22934; -.
DR MGI; MGI:103254; Rpia.
DR VEuPathDB; HostDB:ENSMUSG00000053604; -.
DR eggNOG; KOG3075; Eukaryota.
DR GeneTree; ENSGT00390000004352; -.
DR HOGENOM; CLU_056590_0_2_1; -.
DR InParanoid; P47968; -.
DR OMA; YDWDEVN; -.
DR OrthoDB; 1074761at2759; -.
DR PhylomeDB; P47968; -.
DR TreeFam; TF105758; -.
DR Reactome; R-MMU-71336; Pentose phosphate pathway.
DR UniPathway; UPA00115; UER00412.
DR BioGRID-ORCS; 19895; 24 hits in 75 CRISPR screens.
DR PRO; PR:P47968; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P47968; protein.
DR Bgee; ENSMUSG00000053604; Expressed in gastrula and 252 other tissues.
DR Genevisible; P47968; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0048029; F:monosaccharide binding; ISO:MGI.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IDA:MGI.
DR GO; GO:0006014; P:D-ribose metabolic process; IBA:GO_Central.
DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:MGI.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; ISO:MGI.
DR GO; GO:0019693; P:ribose phosphate metabolic process; ISO:MGI.
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 Isomerase; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..303
FT /note="Ribose-5-phosphate isomerase"
FT /id="PRO_0000158522"
FT REGION 22..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P49247"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49247"
FT CONFLICT 84
FT /note="E -> D (in Ref. 2; BAE23281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 303 AA; 32451 MW; F8535B80A9D823C8 CRC64;
MQRPGPFSTL YGRVLAPLPG RAGGAASGGG GNNWGLSGSH VQLPGRAHSE TRGDKGGSSA
GGPAPSTMSK AEEAKKLASH TAVENHVKNN QVLGIGSGST IVHAVQRIAE RVKQENLDLI
CIPTSFQARQ LILQYGLTLS DLDQHPEIDL AIDGADEVDA ELNLIKGGGG CLTQEKIVAG
YASRFIVIAD FRKDSKNLGD RWHKGIPIEV IPMAYVPVSR AVAQKFGGEV ELRMAVNKAG
PVVTDNGNFI LDWKFDRVHK WSEVNTAIKM TPGVVDTGLF INMAERVYFG MQDGSVNVRE
KPF