6PGL_HUMAN
ID 6PGL_HUMAN Reviewed; 258 AA.
AC O95336;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=6-phosphogluconolactonase {ECO:0000305};
DE Short=6PGL;
DE EC=3.1.1.31 {ECO:0000269|PubMed:10518023};
GN Name=PGLS {ECO:0000312|HGNC:HGNC:8903};
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], CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=10518023; DOI=10.1016/s0014-5793(99)01247-8;
RA Collard F., Collet J.-F., Gerin I., Veiga-da-Cunha M., van Schaftingen E.;
RT "Identification of the cDNA encoding human 6-phosphogluconolactonase, the
RT enzyme catalyzing the second step of the pentose phosphate pathway.";
RL FEBS Lett. 459:223-226(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 PROTEIN SEQUENCE OF 41-72 AND 82-96, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-242.
RA Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.;
RT "Full-insert sequence of mapped XREF EST.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-180, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
CC {ECO:0000269|PubMed:10518023}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
CC + H(+); Xref=Rhea:RHEA:12556, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57955, ChEBI:CHEBI:58759; EC=3.1.1.31;
CC Evidence={ECO:0000269|PubMed:10518023};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 2/3. {ECO:0000269|PubMed:10518023}.
CC -!- INTERACTION:
CC O95336; Q13867: BLMH; NbExp=3; IntAct=EBI-11307753, EBI-718504;
CC O95336; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-11307753, EBI-750109;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. 6-phosphogluconolactonase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72960.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ243972; CAB57866.1; -; mRNA.
DR EMBL; BC014006; AAH14006.1; -; mRNA.
DR EMBL; AF091091; AAC72960.1; ALT_INIT; mRNA.
DR CCDS; CCDS12361.1; -.
DR RefSeq; NP_036220.1; NM_012088.2.
DR AlphaFoldDB; O95336; -.
DR SMR; O95336; -.
DR BioGRID; 117328; 58.
DR IntAct; O95336; 6.
DR STRING; 9606.ENSP00000252603; -.
DR GlyGen; O95336; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; O95336; -.
DR PhosphoSitePlus; O95336; -.
DR SwissPalm; O95336; -.
DR BioMuta; PGLS; -.
DR OGP; O95336; -.
DR REPRODUCTION-2DPAGE; IPI00029997; -.
DR EPD; O95336; -.
DR jPOST; O95336; -.
DR MassIVE; O95336; -.
DR MaxQB; O95336; -.
DR PaxDb; O95336; -.
DR PeptideAtlas; O95336; -.
DR PRIDE; O95336; -.
DR ProteomicsDB; 50807; -.
DR TopDownProteomics; O95336; -.
DR Antibodypedia; 27708; 214 antibodies from 30 providers.
DR DNASU; 25796; -.
DR Ensembl; ENST00000252603.7; ENSP00000252603.1; ENSG00000130313.7.
DR GeneID; 25796; -.
DR KEGG; hsa:25796; -.
DR MANE-Select; ENST00000252603.7; ENSP00000252603.1; NM_012088.3; NP_036220.1.
DR UCSC; uc002ngw.4; human.
DR CTD; 25796; -.
DR DisGeNET; 25796; -.
DR GeneCards; PGLS; -.
DR HGNC; HGNC:8903; PGLS.
DR HPA; ENSG00000130313; Low tissue specificity.
DR MIM; 604951; gene.
DR neXtProt; NX_O95336; -.
DR OpenTargets; ENSG00000130313; -.
DR PharmGKB; PA33240; -.
DR VEuPathDB; HostDB:ENSG00000130313; -.
DR eggNOG; KOG3147; Eukaryota.
DR GeneTree; ENSGT00550000075110; -.
DR HOGENOM; CLU_053947_0_2_1; -.
DR InParanoid; O95336; -.
DR OMA; YQLFEFE; -.
DR OrthoDB; 1420529at2759; -.
DR PhylomeDB; O95336; -.
DR TreeFam; TF318609; -.
DR BioCyc; MetaCyc:HS05370-MON; -.
DR BRENDA; 3.1.1.31; 2681.
DR PathwayCommons; O95336; -.
DR Reactome; R-HSA-71336; Pentose phosphate pathway.
DR SignaLink; O95336; -.
DR SIGNOR; O95336; -.
DR UniPathway; UPA00115; UER00409.
DR BioGRID-ORCS; 25796; 72 hits in 1073 CRISPR screens.
DR ChiTaRS; PGLS; human.
DR GenomeRNAi; 25796; -.
DR Pharos; O95336; Tbio.
DR PRO; PR:O95336; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O95336; protein.
DR Bgee; ENSG00000130313; Expressed in granulocyte and 192 other tissues.
DR ExpressionAtlas; O95336; baseline and differential.
DR Genevisible; O95336; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:UniProtKB.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
DR CDD; cd01400; 6PGL; 1.
DR InterPro; IPR005900; 6-phosphogluconolactonase_DevB.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR039104; PGLS.
DR PANTHER; PTHR11054; PTHR11054; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR01198; pgl; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..258
FT /note="6-phosphogluconolactonase"
FT /id="PRO_0000090078"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 180
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
SQ SEQUENCE 258 AA; 27547 MW; A753FB7E662116DD CRC64;
MAAPAPGLIS VFSSSQELGA ALAQLVAQRA ACCLAGARAR FALGLSGGSL VSMLARELPA
AVAPAGPASL ARWTLGFCDE RLVPFDHAES TYGLYRTHLL SRLPIPESQV ITINPELPVE
EAAEDYAKKL RQAFQGDSIP VFDLLILGVG PDGHTCSLFP DHPLLQEREK IVAPISDSPK
PPPQRVTLTL PVLNAARTVI FVATGEGKAA VLKRILEDQE ENPLPAALVQ PHTGKLCWFL
DEAAARLLTV PFEKHSTL
