RPEL1_HUMAN
ID RPEL1_HUMAN Reviewed; 228 AA.
AC Q2QD12;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Ribulose-phosphate 3-epimerase-like protein 1;
DE EC=5.1.3.1 {ECO:0000250|UniProtKB:Q96AT9};
DE AltName: Full=Ribulose-5-phosphate-3-epimerase-like protein 1;
GN Name=RPEL1;
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 [GENOMIC DNA].
RX PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT "Emergence of young human genes after a burst of retroposition in
RT primates.";
RL PLoS Biol. 3:E357-E357(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 reversible epimerization of D-ribulose 5-
CC phosphate to D-xylulose 5-phosphate. {ECO:0000250|UniProtKB:Q96AT9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:13677, ChEBI:CHEBI:57737, ChEBI:CHEBI:58121;
CC EC=5.1.3.1; Evidence={ECO:0000250|UniProtKB:Q96AT9};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q96AT9};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q96AT9};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q96AT9};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q96AT9};
CC Note=Binds 1 divalent metal cation per subunit. Active with Fe(2+), and
CC probably also with Mn(2+), Zn(2+) and Co(2+).
CC {ECO:0000250|UniProtKB:Q96AT9};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000250|UniProtKB:Q96AT9}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96AT9}.
CC -!- MISCELLANEOUS: According to some authors, RPEL1 is a RPE retrogene on
CC chromosome 2 which is likely to be functional.
CC {ECO:0000305|PubMed:16201836}.
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000305}.
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DR EMBL; DQ120706; ABC40667.1; -; Genomic_DNA.
DR EMBL; AL360001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49655.1; -; Genomic_DNA.
DR EMBL; BC137242; AAI37243.1; -; mRNA.
DR EMBL; BC137243; AAI37244.1; -; mRNA.
DR EMBL; BC157829; AAI57830.1; -; mRNA.
DR EMBL; BC157875; AAI57876.1; -; mRNA.
DR EMBL; BC171806; AAI71806.1; -; mRNA.
DR EMBL; BC171885; AAI71885.1; -; mRNA.
DR CCDS; CCDS65929.1; -.
DR RefSeq; NP_001137381.1; NM_001143909.1.
DR AlphaFoldDB; Q2QD12; -.
DR SMR; Q2QD12; -.
DR BioGRID; 609427; 3.
DR IntAct; Q2QD12; 1.
DR STRING; 9606.ENSP00000476672; -.
DR iPTMnet; Q2QD12; -.
DR PhosphoSitePlus; Q2QD12; -.
DR BioMuta; RPEL1; -.
DR jPOST; Q2QD12; -.
DR MassIVE; Q2QD12; -.
DR MaxQB; Q2QD12; -.
DR PeptideAtlas; Q2QD12; -.
DR PRIDE; Q2QD12; -.
DR Antibodypedia; 71379; 28 antibodies from 14 providers.
DR DNASU; 729020; -.
DR Ensembl; ENST00000441178.2; ENSP00000476672.1; ENSG00000235376.5.
DR GeneID; 729020; -.
DR KEGG; hsa:729020; -.
DR MANE-Select; ENST00000441178.2; ENSP00000476672.1; NM_001143909.1; NP_001137381.1.
DR UCSC; uc009xxi.2; human.
DR CTD; 729020; -.
DR DisGeNET; 729020; -.
DR GeneCards; RPEL1; -.
DR HGNC; HGNC:45241; RPEL1.
DR HPA; ENSG00000235376; Not detected.
DR neXtProt; NX_Q2QD12; -.
DR OpenTargets; ENSG00000235376; -.
DR VEuPathDB; HostDB:ENSG00000235376; -.
DR eggNOG; KOG3111; Eukaryota.
DR GeneTree; ENSGT00390000001447; -.
DR HOGENOM; CLU_054856_0_1_1; -.
DR OMA; SPWFIEE; -.
DR OrthoDB; 1554029at2759; -.
DR PathwayCommons; Q2QD12; -.
DR Reactome; R-HSA-71336; Pentose phosphate pathway.
DR SignaLink; Q2QD12; -.
DR SIGNOR; Q2QD12; -.
DR BioGRID-ORCS; 729020; 25 hits in 957 CRISPR screens.
DR GenomeRNAi; 729020; -.
DR Pharos; Q2QD12; Tbio.
DR PRO; PR:Q2QD12; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q2QD12; protein.
DR Bgee; ENSG00000235376; Expressed in superior frontal gyrus and 2 other tissues.
DR Genevisible; Q2QD12; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_02227; RPE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR026019; Ribul_P_3_epim.
DR InterPro; IPR000056; Ribul_P_3_epim-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR11749; PTHR11749; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR PIRSF; PIRSF001461; RPE; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cobalt; Iron; Isomerase; Manganese; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..228
FT /note="Ribulose-phosphate 3-epimerase-like protein 1"
FT /id="PRO_0000425564"
FT ACT_SITE 37
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 35
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 37
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 70
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 146..149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 175..177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 175
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 197..198
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
SQ SEQUENCE 228 AA; 25023 MW; 231D8799E36AD588 CRC64;
MASGCKIGPS ILNSDLANLG AKCLQMLDSG ADYLHLDVMD GHFVPNITFG HPVVESLRKQ
LGQDPFFDMH MMVSKPEQWV KPMAVAEANQ YTFHLEATEN PGTLIKDIRE NGMKVGLAIK
PGTSVEYLAP WANQIDMALV MTVEPGFGEQ KFMEDMMPKV HWLRTQFPSL DIEGDGGVGS
DTVHKCAEAG ANMTVSGSAI MRSEDPRSVI NLLRNICSEA AQKRSLDR
