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P50309 (G6PI_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-6-phosphate isomerase

Short name=GPI
EC=5.3.1.9
Alternative name(s):
Autocrine motility factor
Short name=AMF
Neuroleukin
Short name=NLK
Phosphoglucose isomerase
Short name=PGI
Phosphohexose isomerase
Short name=PHI
Gene names
Name:GPI
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons By similarity. HAMAP-Rule MF_00473

Catalytic activity

D-glucose 6-phosphate = D-fructose 6-phosphate. HAMAP-Rule MF_00473

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. HAMAP-Rule MF_00473

Subunit structure

Homodimer in the catalytically active form, monomer in the secreted form By similarity.

Subcellular location

Cytoplasm. Secreted By similarity HAMAP-Rule MF_00473.

Post-translational modification

ISGylated By similarity. HAMAP-Rule MF_00473

Sequence similarities

Belongs to the GPI family.

Ontologies

Keywords
   Biological processAngiogenesis
Gluconeogenesis
Glycolysis
   Cellular componentCytoplasm
Secreted
   Molecular functionCytokine
Isomerase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

gluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

glycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionglucose-6-phosphate isomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 558557Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180536

Sites

Active site3581Proton donor By similarity
Active site3891 By similarity
Active site5191 By similarity

Amino acid modifications

Modified residue121N6-acetyllysine By similarity
Modified residue1421N6-acetyllysine By similarity
Modified residue1851Phosphoserine; by CK2 By similarity
Modified residue4541N6-malonyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P50309 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 262C454F01CE047F

FASTA55863,059
        10         20         30         40         50         60 
MTSLTQNRYF QKLQDWHRDN SADINLRSLF DADPERFNNF SLNLNTTHGH ILVDYSKNLV 

        70         80         90        100        110        120 
NKEVMQMLVD LARSRGVETM RDNMFSGVKI NYTEDRAVLH VALRNRSNSP IVVDSRDVMP 

       130        140        150        160        170        180 
EVNRVLEKMR SFCQRVRSGE WKGYSGKPIT DIVNIGIGGS DLGPLMVTEA LKPYASGGPR 

       190        200        210        220        230        240 
IWFVSNIDGT HIAKTLANLT PESSLFIVAS KTFTTQETIT NAETAKEWFL GASRDPSTVA 

       250        260        270        280        290        300 
KHFIALSTNT SKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHIGF DNFEQLLSGA 

       310        320        330        340        350        360 
HWMDQHFRKT PLEKNAPVLL ALLGIWYINF YGCETHALLP YDQYMHRFAA YFQQGDMESN 

       370        380        390        400        410        420 
GKSITRSGTR VDHHTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL 

       430        440        450        460        470        480 
HHKILLANFL AQTEALMKGK SNEEAKKELQ AAGKSPEDLE KLLPHKVFEG NRPTNSIVFT 

       490        500        510        520        530        540 
KLTPFILGAL IALYEHKIFV QGVIWDINSF DQWGVELGKQ LAKNIEPELD GSAPVTSHDS 

       550 
STNGLIKFIK QQRDIRIE 

« Hide

References

[1]"Characterization of cDNAs coding for glucose phosphate isomerase and phosphoglycerate kinase in Chinese hamster ovary cell line CHO-K1 and identification of defects in R1.1.7, a glycolysis-deficient variant of CHO-K1."
Hassan A.F., Morgan M.J., Faik P.
Somat. Cell Mol. Genet. 21:75-81(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z37977 mRNA. Translation: CAA86031.1.
PIRI48073.
RefSeqNP_001233655.1. NM_001246726.1.

3D structure databases

ProteinModelPortalP50309.
SMRP50309. Positions 3-557.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP50309.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689468.
KEGGcge:100689468.

Phylogenomic databases

HOVERGENHBG002877.
KOK01810.

Enzyme and pathway databases

UniPathwayUPA00109; UER00181.

Family and domain databases

Gene3D1.10.1390.10. 1 hit.
HAMAPMF_00473. G6P_isomerase.
InterProIPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERPTHR11469. PTHR11469. 1 hit.
PfamPF00342. PGI. 1 hit.
[Graphical view]
PRINTSPR00662. G6PISOMERASE.
PROSITEPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG6PI_CRIGR
AccessionPrimary (citable) accession number: P50309
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways