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   24-JAN-2024, entry version 184.
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; 71.
DR   IntAct; O95336; 6.
DR   STRING; 9606.ENSP00000252603; -.
DR   GlyCosmos; O95336; 1 site, 2 glycans.
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   CPTAC; CPTAC-2712; -.
DR   EPD; O95336; -.
DR   jPOST; O95336; -.
DR   MassIVE; O95336; -.
DR   MaxQB; O95336; -.
DR   PaxDb; 9606-ENSP00000252603; -.
DR   PeptideAtlas; O95336; -.
DR   ProteomicsDB; 50807; -.
DR   Pumba; O95336; -.
DR   TopDownProteomics; O95336; -.
DR   Antibodypedia; 27708; 233 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   AGR; HGNC:8903; -.
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; 296373at2759; -.
DR   PhylomeDB; O95336; -.
DR   TreeFam; TF318609; -.
DR   BioCyc; MetaCyc:HS05370-MONOMER; -.
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; 76 hits in 1151 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 194 other cell types or tissues.
DR   ExpressionAtlas; O95336; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   Gene3D; 3.40.50.1360; -; 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   NCBIfam; TIGR01198; pgl; 1.
DR   PANTHER; PTHR11054; 6-PHOSPHOGLUCONOLACTONASE; 1.
DR   PANTHER; PTHR11054:SF0; 6-PHOSPHOGLUCONOLACTONASE; 1.
DR   Pfam; PF01182; Glucosamine_iso; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
DR   Genevisible; O95336; HS.
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
//