G6PI_PIG
ID G6PI_PIG Reviewed; 558 AA.
AC P08059; Q29556;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000303|PubMed:6115414};
DE Short=GPI {ECO:0000303|PubMed:6115414};
DE EC=5.3.1.9 {ECO:0000250|UniProtKB:P06745};
DE AltName: Full=Autocrine motility factor {ECO:0000250|UniProtKB:P06744};
DE Short=AMF {ECO:0000250|UniProtKB:P06744};
DE AltName: Full=Neuroleukin {ECO:0000303|PubMed:3352744};
DE Short=NLK {ECO:0000303|PubMed:3352744};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000303|PubMed:7821788};
DE Short=PGI {ECO:0000303|PubMed:7821788};
DE AltName: Full=Phosphohexose isomerase {ECO:0000303|PubMed:3352744};
DE Short=PHI {ECO:0000303|PubMed:3352744};
GN Name=GPI {ECO:0000303|PubMed:6115414};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3352744; DOI=10.1038/332454a0;
RA Chaput M., Claes V., Portetelle D., Clutdts I., Cravador A., Burny A.,
RA Gras H., Tartar A.;
RT "The neurotrophic factor neuroleukin is 90% homologous with phosphohexose
RT isomerase.";
RL Nature 332:454-455(1988).
RN [2]
RP SEQUENCE REVISION.
RA Burny A.;
RL Submitted (AUG-1988) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7821788; DOI=10.1016/0378-1119(94)90432-4;
RA Claes V., Kettmann R., Burny A.;
RT "Structure of the gene encoding pig phosphoglucose isomerase.";
RL Gene 150:235-241(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-17.
RC STRAIN=Belgian Landrace;
RX PubMed=2248981; DOI=10.1016/0167-4781(90)90009-q;
RA Claes V., Taquet A.N., Kettmann R., Burny A.;
RT "Sequence analysis of the pig phosphoglucose isomerase gene promoter
RT region.";
RL Biochim. Biophys. Acta 1087:339-340(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 238-357.
RX PubMed=2889410; DOI=10.1111/j.1365-2052.1987.tb00763.x;
RA Davies W., Harbitz I., Hauge J.G.;
RT "A partial cDNA clone for porcine glucosephosphate isomerase: isolation,
RT characterization and use in detection of restriction fragment length
RT polymorphisms.";
RL Anim. Genet. 18:233-240(1987).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS).
RX PubMed=4475113; DOI=10.1016/0022-2836(74)90170-3;
RA Muirhead H., Shaw P.J.;
RT "Three-dimensional structure of pig muscle phosphoglucose isomerase at 6-A
RT resolution.";
RL J. Mol. Biol. 89:195-203(1974).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND PROTEIN SEQUENCE OF 554-558.
RX PubMed=6115414; DOI=10.1098/rstb.1981.0068;
RA Achari A., Marshall S.E., Muirhead H., Palmieri R.H., Noltmann E.A.;
RT "Glucose-6-phosphate isomerase.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 293:145-157(1981).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) ALONE AND IN COMPLEX WITH
RP 5-PHOSPHOARABINONATE.
RX PubMed=12402366; DOI=10.1002/prot.10255;
RA Davies C., Muirhead H.;
RT "Crystal structure of phosphoglucose isomerase from pig muscle and its
RT complex with 5-phosphoarabinonate.";
RL Proteins 49:577-579(2002).
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 (By similarity). 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:0000250|UniProtKB:P06745}.
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:0000250|UniProtKB:P06744};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000250|UniProtKB:P06744}.
CC -!- SUBUNIT: Homodimer in the catalytically active form, monomer in the
CC secreted form. {ECO:0000269|PubMed:12402366}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06744}.
CC Secreted {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}.
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DR EMBL; X07382; CAA30295.1; -; mRNA.
DR EMBL; Z28396; CAA82246.1; -; Genomic_DNA.
DR EMBL; Z28397; CAA82246.1; JOINED; Genomic_DNA.
DR EMBL; Z28398; CAA82246.1; JOINED; Genomic_DNA.
DR EMBL; Z28399; CAA82246.1; JOINED; Genomic_DNA.
DR EMBL; Z28400; CAA82246.1; JOINED; Genomic_DNA.
DR EMBL; Z28401; CAA82246.1; JOINED; Genomic_DNA.
DR EMBL; Z28402; CAA82246.1; JOINED; Genomic_DNA.
DR EMBL; Z28403; CAA82246.1; JOINED; Genomic_DNA.
DR EMBL; Z28404; CAA82246.1; JOINED; Genomic_DNA.
DR EMBL; X53719; CAA37755.1; -; mRNA.
DR EMBL; M54975; AAA31048.1; -; mRNA.
DR PIR; I47142; I47142.
DR PIR; S00895; NUPG.
DR RefSeq; NP_999495.1; NM_214330.1.
DR PDB; 1GZD; X-ray; 2.50 A; A=2-558.
DR PDB; 1GZV; X-ray; 3.51 A; A=2-558.
DR PDBsum; 1GZD; -.
DR PDBsum; 1GZV; -.
DR AlphaFoldDB; P08059; -.
DR SMR; P08059; -.
DR STRING; 9823.ENSSSCP00000003094; -.
DR PaxDb; P08059; -.
DR PeptideAtlas; P08059; -.
DR PRIDE; P08059; -.
DR Ensembl; ENSSSCT00000003175; ENSSSCP00000003094; ENSSSCG00000002873.
DR Ensembl; ENSSSCT00025047497; ENSSSCP00025020351; ENSSSCG00025034806.
DR Ensembl; ENSSSCT00035108133; ENSSSCP00035046820; ENSSSCG00035079108.
DR Ensembl; ENSSSCT00040087102; ENSSSCP00040038243; ENSSSCG00040063535.
DR Ensembl; ENSSSCT00045030938; ENSSSCP00045021461; ENSSSCG00045018132.
DR Ensembl; ENSSSCT00050068357; ENSSSCP00050029323; ENSSSCG00050050209.
DR Ensembl; ENSSSCT00055037281; ENSSSCP00055029618; ENSSSCG00055019026.
DR Ensembl; ENSSSCT00060052940; ENSSSCP00060022543; ENSSSCG00060039122.
DR Ensembl; ENSSSCT00065071617; ENSSSCP00065031218; ENSSSCG00065052281.
DR GeneID; 397602; -.
DR KEGG; ssc:397602; -.
DR CTD; 2821; -.
DR VGNC; VGNC:97068; GPI.
DR eggNOG; KOG2446; Eukaryota.
DR GeneTree; ENSGT00390000000707; -.
DR InParanoid; P08059; -.
DR OMA; IGVWYIN; -.
DR OrthoDB; 446616at2759; -.
DR UniPathway; UPA00109; UER00181.
DR EvolutionaryTrace; P08059; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000002873; Expressed in semimembranosus muscle and 43 other tissues.
DR ExpressionAtlas; P08059; baseline and differential.
DR GO; GO:0060170; C:ciliary membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0034101; P:erythrocyte homeostasis; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IEA:Ensembl.
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 3D-structure; Acetylation; Cytokine; Cytoplasm; Direct protein sequencing;
KW Gluconeogenesis; Glycolysis; Hydroxylation; Isomerase; Phosphoprotein;
KW Reference proteome; Secreted; 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 /id="PRO_0000180540"
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 34
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT MOD_RES 109
FT /note="Phosphothreonine"
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:0000250|UniProtKB:Q6P6V0"
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:0000250|UniProtKB:P06744"
FT CONFLICT 156..157
FT /note="Missing (in Ref. 3; CAA82246)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="Y -> H (in Ref. 5; AAA31048)"
FT /evidence="ECO:0000305"
FT CONFLICT 347..398
FT /note="RFAAYFQQGDMESNGKYITKSGTRVDHQTGPIVWGEPGTNGQHAFYQLIHQG
FT -> ALLPTSSRVTWSPTGSTSPSPAPVWTTRRAPLCGGSQGPMASMPSTSSS (in
FT Ref. 3; CAA82246)"
FT /evidence="ECO:0000305"
FT CONFLICT 481..482
FT /note="KL -> NV (in Ref. 3; CAA82246)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="K -> M (in Ref. 3; CAA82246)"
FT /evidence="ECO:0000305"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 8..20
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 62..74
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:1GZD"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 119..138
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 216..233
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1GZD"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 282..288
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 290..309
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 316..329
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 348..360
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 392..397
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 404..411
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 416..438
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 442..451
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:1GZD"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 463..466
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 474..481
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 484..505
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 516..528
FT /evidence="ECO:0007829|PDB:1GZD"
FT STRAND 530..533
FT /evidence="ECO:0007829|PDB:1GZD"
FT HELIX 540..554
FT /evidence="ECO:0007829|PDB:1GZD"
SQ SEQUENCE 558 AA; 63126 MW; 84DA1B15CF0C702F CRC64;
MAALTQNPQF KKLQTWYHEH RSDLNLRRLF EGDKDRFNHF SLNLNTNHGR ILLDYSKNLV
TEAVMQMLVD LAKSRGVEAA RERMFNGEKI NFTEDRAVLH VALRNRSNTP ILVDGKDVMP
EVNRVLEKMK SFCKRVRSGE WKGYSGKSIT DVINIGIGGS DLGPLMVTEA LKPYSAEGPR
VWFVSNIDGT HIAKTLATLN PESSLFIIAS KTFTTQETIT NAETAKEWFL QSAKDPSAVA
KHFVALSTNT TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA
HWMDQHFRTT PLEKNAPVLL ALLGIWYINF FGCETHAMLP YDQYLHRFAA YFQQGDMESN
GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL
HHKILLANFL AQTEALMKGK STEEARKELQ AAGKSPEDFE KLLPHKVFEG NRPTNSIVFT
KLTPFILGAL IAMYEHKIFV QGVIWDINSF DQWGVELGKQ LAKKIEPELD GSSPVTSHDS
STNGLINFIK QEREARSQ
