G6PI_BOVIN
ID G6PI_BOVIN Reviewed; 557 AA.
AC Q3ZBD7; F1MD19; O46595;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 4.
DT 03-AUG-2022, entry version 113.
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};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 232-316.
RA Savadye D.T.;
RL Submitted (JAN-1998) 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; DAAA02046903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC103416; AAI03417.1; -; mRNA.
DR EMBL; AF043228; AAB97860.1; -; mRNA.
DR RefSeq; NP_001035561.1; NM_001040471.1.
DR AlphaFoldDB; Q3ZBD7; -.
DR SMR; Q3ZBD7; -.
DR STRING; 9913.ENSBTAP00000008386; -.
DR PaxDb; Q3ZBD7; -.
DR PeptideAtlas; Q3ZBD7; -.
DR PRIDE; Q3ZBD7; -.
DR Ensembl; ENSBTAT00000008386; ENSBTAP00000008386; ENSBTAG00000006396.
DR GeneID; 280808; -.
DR KEGG; bta:280808; -.
DR CTD; 2821; -.
DR VEuPathDB; HostDB:ENSBTAG00000006396; -.
DR VGNC; VGNC:29534; GPI.
DR eggNOG; KOG2446; Eukaryota.
DR GeneTree; ENSGT00390000000707; -.
DR HOGENOM; CLU_017947_3_0_1; -.
DR InParanoid; Q3ZBD7; -.
DR OrthoDB; 446616at2759; -.
DR TreeFam; TF300436; -.
DR SABIO-RK; Q3ZBD7; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000006396; Expressed in retina and 106 other tissues.
DR ExpressionAtlas; Q3ZBD7; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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; Isomerase;
KW Phosphoprotein; Reference proteome; Secreted; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT CHAIN 2..557
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000247641"
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 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:0000250|UniProtKB:Q6P6V0"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT CONFLICT 170
FT /note="A -> S (in Ref. 1; AAI03417)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="L -> WRRTP (in Ref. 3; AAB97860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 62855 MW; D932716D85FB2185 CRC64;
MAALTQNPQF KKLKTWYEQH GSDLNLRRLF EGDRDRFNRF SLNLNTNHGH ILVDYSKNLV
TETVMQMLVD VAKSRGVEAA RERMFTGEKI NFTEDRAVLH VALRNRSNAP ILVDGKDVMP
EVNRVLEKMK SFCQRVRSGE WKGYSGKAIT DVINIGIGGS DLGPLMVTEA LKPYSSEGPR
VWFVSNIDGT HIAKTLATLN PESSLFIIAS KTFTTQETIT NAETAKEWFL LSAKDPSAVA
KHFVALSTNT AKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA
HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA YFQQGDMESN
GKYITKSGTR VNYQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QSQHPIRNGL
HHKILLANFL AQTEALMRGK STEEARKELQ AAGRSPEDFE KLLPHKVFEG NRPTNSIVFT
KLTPFILGAL IAMYEHKIFV QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSSPVTSHDS
STNGLINFIK QEREARS
