G6PI_MACFA
ID G6PI_MACFA Reviewed; 558 AA.
AC Q4R591;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000250|UniProtKB:P06744};
DE Short=GPI {ECO:0000250|UniProtKB:P06744};
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:0000250|UniProtKB:P06744};
DE Short=NLK {ECO:0000250|UniProtKB:P06744};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000250|UniProtKB:P06744};
DE Short=PGI {ECO:0000250|UniProtKB:P06744};
DE AltName: Full=Phosphohexose isomerase;
DE Short=PHI {ECO:0000250|UniProtKB:P06744};
GN Name=GPI {ECO:0000250|UniProtKB:P06744};
GN ORFNames=QccE-13068 {ECO:0000303|Ref.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P06744}.
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; AB169653; BAE01734.1; -; mRNA.
DR AlphaFoldDB; Q4R591; -.
DR SMR; Q4R591; -.
DR STRING; 9541.XP_005588841.1; -.
DR Ensembl; ENSMFAT00000006117; ENSMFAP00000031897; ENSMFAG00000036975.
DR eggNOG; KOG2446; Eukaryota.
DR GeneTree; ENSGT00390000000707; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000233100; Chromosome 19.
DR Bgee; ENSMFAG00000036975; Expressed in skeletal muscle tissue and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
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:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Acetylation; Cytokine; Cytoplasm; Gluconeogenesis; Glycolysis;
KW Hydroxylation; 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 /id="PRO_0000226295"
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"
SQ SEQUENCE 558 AA; 63151 MW; 3545FB985529C10A CRC64;
MAALTRDPQF QKLQQWYREH GSELNLRRLF DADKDRFNHF SLTLNTNHGH ILLDYSKNLV
TEDVMRMLVD LAKSRGVEAA RERMFNGEKI NYTEGRAVLH VALRNRSNTP ILVDGKDVMP
EVNKVLDKMK SFCQRVRSGD WKGYTGKTIT DVINIGIGGS DLGPLMVTEA LKPYSSEGPR
VWYVSNIDGT HIAKTLTQLN PESSLFIIAS KTFTTQETIT NAETAKEWFL QAAKDPSAVA
KHFVALSTNT TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA
HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA YFQQGDMESN
GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL
HHKILLANFL AQTEALMRGK STDEARKELQ AAGKSPEDLE RLLPHKVFEG NRPTNSIVFT
KLTPFMLGAL VAMYEHKIFV QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSAQVTSHDA
STNGLINFIK QQREARVQ
