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   24-JAN-2024, entry version 119.
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}.
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; 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.ENSBTAP00000073190; -.
DR   PaxDb; 9913-ENSBTAP00000008386; -.
DR   PeptideAtlas; Q3ZBD7; -.
DR   Ensembl; ENSBTAT00000008386.4; ENSBTAP00000008386.3; ENSBTAG00000006396.5.
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; 1657888at2759; -.
DR   TreeFam; TF300436; -.
DR   Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Reactome; R-BTA-70171; Glycolysis.
DR   Reactome; R-BTA-70263; Gluconeogenesis.
DR   SABIO-RK; Q3ZBD7; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000006396; Expressed in retina and 106 other cell types or 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; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR   Pfam; PF00342; PGI; 1.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   SUPFAM; SSF53697; SIS domain; 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
//