G6PI_RAT
ID G6PI_RAT Reviewed; 558 AA.
AC Q6P6V0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000250|UniProtKB:P06745};
DE Short=GPI {ECO:0000250|UniProtKB:P06745};
DE EC=5.3.1.9 {ECO:0000269|PubMed:2709006};
DE AltName: Full=Autocrine motility factor {ECO:0000250|UniProtKB:P06744};
DE Short=AMF {ECO:0000250|UniProtKB:P06744};
DE AltName: Full=Neuroleukin {ECO:0000250|UniProtKB:P06745};
DE Short=NLK {ECO:0000250|UniProtKB:P06745};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000250|UniProtKB:P06745};
DE Short=PGI {ECO:0000250|UniProtKB:P06745};
DE AltName: Full=Phosphohexose isomerase {ECO:0000250|UniProtKB:P06745};
DE Short=PHI {ECO:0000250|UniProtKB:P06745};
GN Name=Gpi {ECO:0000312|RGD:2727};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAH62005.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate {ECO:0000312|EMBL:AAH62005.1};
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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2709006; DOI=10.1111/j.1471-4159.1989.tb09178.x;
RA Gaitonde M.K., Murray E., Cunningham V.J.;
RT "Effect of 6-phosphogluconate on phosphoglucose isomerase in rat brain in
RT vitro and in vivo.";
RL J. Neurochem. 52:1348-1352(1989).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19343716; DOI=10.1002/pmic.200800664;
RA Maurya D.K., Sundaram C.S., Bhargava P.;
RT "Proteome profile of the mature rat olfactory bulb.";
RL Proteomics 9:2593-2599(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; THR-250 AND SER-455, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-
CC phosphate to fructose-6-phosphate, the second step in glycolysis, and
CC the reverse reaction during gluconeogenesis (PubMed:2709006). Besides
CC it's role as a glycolytic enzyme, also acts as a secreted cytokine:
CC acts as an angiogenic factor (AMF) that stimulates endothelial cell
CC motility. Acts as a neurotrophic factor, neuroleukin, for spinal and
CC sensory neurons. It is secreted by lectin-stimulated T-cells and
CC induces immunoglobulin secretion (By similarity).
CC {ECO:0000250|UniProtKB:P06744, ECO:0000269|PubMed:2709006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC EC=5.3.1.9; Evidence={ECO:0000269|PubMed:2709006};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.593 mM for glucose-6-phosphate {ECO:0000269|PubMed:2709006};
CC KM=0.095 mM for fructose-6-phosphate {ECO:0000269|PubMed:2709006};
CC Vmax=2.291 nmol/min/mg enzyme with glucose-6-phosphate as substrate
CC {ECO:0000269|PubMed:2709006};
CC Vmax=98 nmol/min/mg enzyme with fructose-6-phosphate as substrate
CC {ECO:0000269|PubMed:2709006};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000269|PubMed:2709006}.
CC -!- SUBUNIT: Homodimer; in the catalytically active form. Monomer in the
CC secreted form. {ECO:0000250|UniProtKB:P06744}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19343716}. Secreted
CC {ECO:0000250|UniProtKB:P06744}.
CC -!- PTM: Phosphorylation at Ser-185 by CK2 has been shown to decrease
CC enzymatic activity and may contribute to secretion by a non-classical
CC secretory pathway. {ECO:0000250|UniProtKB:P06744}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P06744}.
CC -!- SIMILARITY: Belongs to the GPI family. {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; BC062005; AAH62005.1; -; mRNA.
DR RefSeq; NP_997475.1; NM_207592.1.
DR AlphaFoldDB; Q6P6V0; -.
DR SMR; Q6P6V0; -.
DR BioGRID; 253982; 2.
DR IntAct; Q6P6V0; 11.
DR STRING; 10116.ENSRNOP00000029515; -.
DR iPTMnet; Q6P6V0; -.
DR PhosphoSitePlus; Q6P6V0; -.
DR SwissPalm; Q6P6V0; -.
DR World-2DPAGE; 0004:Q6P6V0; -.
DR jPOST; Q6P6V0; -.
DR PaxDb; Q6P6V0; -.
DR PRIDE; Q6P6V0; -.
DR Ensembl; ENSRNOT00000032613; ENSRNOP00000029515; ENSRNOG00000023150.
DR Ensembl; ENSRNOT00000097410; ENSRNOP00000087782; ENSRNOG00000023150.
DR GeneID; 292804; -.
DR KEGG; rno:292804; -.
DR UCSC; RGD:2727; rat.
DR CTD; 2821; -.
DR RGD; 2727; Gpi.
DR eggNOG; KOG2446; Eukaryota.
DR GeneTree; ENSGT00390000000707; -.
DR HOGENOM; CLU_017947_3_0_1; -.
DR InParanoid; Q6P6V0; -.
DR OMA; IGVWYIN; -.
DR OrthoDB; 446616at2759; -.
DR PhylomeDB; Q6P6V0; -.
DR TreeFam; TF300436; -.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-70171; Glycolysis.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR SABIO-RK; Q6P6V0; -.
DR UniPathway; UPA00109; UER00181.
DR PRO; PR:Q6P6V0; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000023150; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q6P6V0; RN.
DR GO; GO:0060170; C:ciliary membrane; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IDA:RGD.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IPI:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:RGD.
DR GO; GO:0034101; P:erythrocyte homeostasis; ISO:RGD.
DR GO; GO:0006094; P:gluconeogenesis; ISO:RGD.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IDA:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0006096; P:glycolytic process; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; IEP:RGD.
DR GO; GO:0001707; P:mesoderm formation; ISO:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISO:RGD.
DR GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR GO; GO:0043278; P:response to morphine; IMP:RGD.
DR GO; GO:0035994; P:response to muscle stretch; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR Gene3D; 1.10.1390.10; -; 1.
DR HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR023096; G6P_Isomerase_C.
DR InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035476; SIS_PGI_1.
DR InterPro; IPR035482; SIS_PGI_2.
DR PANTHER; PTHR11469; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytokine; Cytoplasm; Gluconeogenesis; Glycolysis;
KW Growth factor; Isomerase; Phosphoprotein; Reference proteome; Secreted;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT CHAIN 2..558
FT /note="Glucose-6-phosphate isomerase"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT /id="PRO_0000349123"
FT ACT_SITE 358
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT ACT_SITE 389
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT ACT_SITE 519
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 159..160
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 210..215
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 354
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 358
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 389
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 519
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT MOD_RES 12
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT MOD_RES 185
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT MOD_RES 250
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 454
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT MOD_RES 454
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 454
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 558 AA; 62827 MW; 2550ACB874E0302C CRC64;
MAALTRNPEF QKLLEWHRAN SANLKLRELF EADPERFNHF SLNLNTNHGH ILLDYSKNLV
NKEVLHMLVD LAKSRGVEAA RDNMFSGLKI NSTEDRAVLH VALRNRSNRS IMMDGKDVMP
EVNKVLDKMK SFCQRVRSGD WKGYTGKAIT DIINIGIGGS DLGPLMVTEA LKPYSKGGPR
VWFVSNIDGT HIAKTLANLN PESSLFIIAS KTFTTQETIT NAETAKEWFL QAAKDPSAVA
KHFVALSTNT DKVKEFGIDP KNMFEFWDWV GGRYSLWSAI GLSIALHVGF DHFEQLLSGA
HWMDQHFMKT PLDKNAPVLL ALLGIWYINF YGCETHAMLP YDQYMHRFAA YFQQGDMESN
GKYITKSGAR VDYQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRNGL
HHKILLANFL AQTEALMKGK SPEEARKELQ AAGKSPEELE KLLPHKVFEG NRPTNSIVFT
KLTPFILGAL IAMYEHKIFV QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSSAVTSHDS
STNGLIGFIK LQRDTKID
