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G6PI_CRIGR
ID   G6PI_CRIGR              Reviewed;         558 AA.
AC   P50309;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000303|PubMed:7604358};
DE            Short=GPI {ECO:0000303|PubMed:7604358};
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:0000303|PubMed:7604358};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=7604358; DOI=10.1007/bf02255824;
RA   Hassan A.F., Morgan M.J., Faik P.;
RT   "Characterization of cDNAs coding for glucose phosphate isomerase and
RT   phosphoglycerate kinase in Chinese hamster ovary cell line CHO-K1 and
RT   identification of defects in R1.1.7, a glycolysis-deficient variant of CHO-
RT   K1.";
RL   Somat. Cell Mol. Genet. 21:75-81(1995).
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; Z37977; CAA86031.1; -; mRNA.
DR   PIR; I48073; I48073.
DR   RefSeq; NP_001233655.1; NM_001246726.1.
DR   AlphaFoldDB; P50309; -.
DR   SMR; P50309; -.
DR   STRING; 10029.NP_001233655.1; -.
DR   Ensembl; ENSCGRT00001002419; ENSCGRP00001001962; ENSCGRG00001001963.
DR   GeneID; 100689468; -.
DR   KEGG; cge:100689468; -.
DR   CTD; 2821; -.
DR   eggNOG; KOG2446; Eukaryota.
DR   GeneTree; ENSGT00390000000707; -.
DR   OrthoDB; 446616at2759; -.
DR   UniPathway; UPA00109; UER00181.
DR   GO; GO:0060170; C:ciliary membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0034101; P:erythrocyte homeostasis; IEA:Ensembl.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
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; IEA:UniProtKB-UniPathway.
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   2: Evidence at transcript level;
KW   Acetylation; Cytokine; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW   Phosphoprotein; Secreted; Ubl conjugation.
FT   CHAIN           1..558
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180536"
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         12
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P6V0"
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         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;  63059 MW;  262C454F01CE047F CRC64;
     MTSLTQNRYF QKLQDWHRDN SADINLRSLF DADPERFNNF SLNLNTTHGH ILVDYSKNLV
     NKEVMQMLVD LARSRGVETM RDNMFSGVKI NYTEDRAVLH VALRNRSNSP IVVDSRDVMP
     EVNRVLEKMR SFCQRVRSGE WKGYSGKPIT DIVNIGIGGS DLGPLMVTEA LKPYASGGPR
     IWFVSNIDGT HIAKTLANLT PESSLFIVAS KTFTTQETIT NAETAKEWFL GASRDPSTVA
     KHFIALSTNT SKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHIGF DNFEQLLSGA
     HWMDQHFRKT PLEKNAPVLL ALLGIWYINF YGCETHALLP YDQYMHRFAA YFQQGDMESN
     GKSITRSGTR VDHHTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL
     HHKILLANFL AQTEALMKGK SNEEAKKELQ AAGKSPEDLE KLLPHKVFEG NRPTNSIVFT
     KLTPFILGAL IALYEHKIFV QGVIWDINSF DQWGVELGKQ LAKNIEPELD GSAPVTSHDS
     STNGLIKFIK QQRDIRIE
 
 
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