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P08059

- G6PI_PIG

UniProt

P08059 - G6PI_PIG

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Protein
Glucose-6-phosphate isomerase
Gene
GPI
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

D-glucose 6-phosphate = D-fructose 6-phosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei358 – 3581Proton donor By similarity
Active sitei389 – 3891 By similarity
Active sitei519 – 5191 By similarity

GO - Molecular functioni

  1. glucose-6-phosphate isomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. gluconeogenesis Source: UniProtKB-KW
  3. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Isomerase

Keywords - Biological processi

Angiogenesis, Gluconeogenesis, Glycolysis

Enzyme and pathway databases

UniPathwayiUPA00109; UER00181.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphate isomerase (EC:5.3.1.9)
Short name:
GPI
Alternative name(s):
Autocrine motility factor
Short name:
AMF
Neuroleukin
Short name:
NLK
Phosphoglucose isomerase
Short name:
PGI
Phosphohexose isomerase
Short name:
PHI
Gene namesi
Name:GPI
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular space Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 558557Glucose-6-phosphate isomeraseUniRule annotation
PRO_0000180540Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineUniRule annotation
Modified residuei12 – 121N6-acetyllysine By similarity
Modified residuei109 – 1091Phosphothreonine By similarity
Modified residuei142 – 1421N6-acetyllysine By similarity
Modified residuei185 – 1851Phosphoserine; by CK2 By similarity
Modified residuei454 – 4541N6-malonyllysine By similarity

Post-translational modificationi

ISGylated By similarity.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP08059.
PRIDEiP08059.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000003094.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64
Helixi8 – 2013
Helixi21 – 233
Helixi26 – 327
Helixi36 – 394
Beta strandi40 – 456
Beta strandi50 – 545
Helixi62 – 7413
Helixi77 – 8610
Turni92 – 954
Helixi100 – 1034
Beta strandi116 – 1183
Helixi119 – 13820
Beta strandi151 – 1555
Helixi159 – 17012
Helixi172 – 1754
Beta strandi180 – 1845
Helixi189 – 1968
Helixi201 – 2033
Beta strandi204 – 2096
Beta strandi211 – 2133
Helixi216 – 23318
Helixi236 – 2416
Beta strandi243 – 2486
Helixi250 – 2556
Helixi260 – 2623
Beta strandi263 – 2653
Helixi272 – 2743
Turni276 – 2783
Helixi279 – 2813
Helixi282 – 2887
Helixi290 – 30920
Helixi312 – 3143
Helixi316 – 32914
Beta strandi335 – 3417
Helixi343 – 3453
Helixi348 – 36013
Beta strandi378 – 3803
Helixi386 – 3894
Helixi392 – 3976
Beta strandi398 – 4003
Beta strandi404 – 4118
Helixi416 – 43823
Helixi442 – 45110
Helixi456 – 4594
Turni460 – 4623
Helixi463 – 4664
Beta strandi474 – 4818
Helixi484 – 50522
Helixi513 – 5153
Helixi516 – 52813
Beta strandi530 – 5334
Helixi540 – 55415

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GZDX-ray2.50A2-558[»]
1GZVX-ray3.51A2-558[»]
ProteinModelPortaliP08059.
SMRiP08059. Positions 2-555.

Miscellaneous databases

EvolutionaryTraceiP08059.

Family & Domainsi

Sequence similaritiesi

Belongs to the GPI family.

Phylogenomic databases

eggNOGiCOG0166.
HOGENOMiHOG000261370.
HOVERGENiHBG002877.
KOiK01810.

Family and domain databases

Gene3Di1.10.1390.10. 1 hit.
HAMAPiMF_00473. G6P_isomerase.
InterProiIPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERiPTHR11469. PTHR11469. 1 hit.
PfamiPF00342. PGI. 1 hit.
[Graphical view]
PRINTSiPR00662. G6PISOMERASE.
PROSITEiPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08059-1 [UniParc]FASTAAdd to Basket

« Hide

MAALTQNPQF KKLQTWYHEH RSDLNLRRLF EGDKDRFNHF SLNLNTNHGR    50
ILLDYSKNLV TEAVMQMLVD LAKSRGVEAA RERMFNGEKI NFTEDRAVLH 100
VALRNRSNTP ILVDGKDVMP EVNRVLEKMK SFCKRVRSGE WKGYSGKSIT 150
DVINIGIGGS DLGPLMVTEA LKPYSAEGPR VWFVSNIDGT HIAKTLATLN 200
PESSLFIIAS KTFTTQETIT NAETAKEWFL QSAKDPSAVA KHFVALSTNT 250
TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA 300
HWMDQHFRTT PLEKNAPVLL ALLGIWYINF FGCETHAMLP YDQYLHRFAA 350
YFQQGDMESN GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK 400
MIPCDFLIPV QTQHPIRKGL HHKILLANFL AQTEALMKGK STEEARKELQ 450
AAGKSPEDFE KLLPHKVFEG NRPTNSIVFT KLTPFILGAL IAMYEHKIFV 500
QGVIWDINSF DQWGVELGKQ LAKKIEPELD GSSPVTSHDS STNGLINFIK 550
QEREARSQ 558
Length:558
Mass (Da):63,126
Last modified:January 23, 2007 - v3
Checksum:i84DA1B15CF0C702F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1572Missing in CAA82246. 1 Publication
Sequence conflicti344 – 3441Y → H in AAA31048. 1 Publication
Sequence conflicti347 – 39852RFAAY…LIHQG → ALLPTSSRVTWSPTGSTSPS PAPVWTTRRAPLCGGSQGPM ASMPSTSSS in CAA82246. 1 Publication
Add
BLAST
Sequence conflicti481 – 4822KL → NV in CAA82246. 1 Publication
Sequence conflicti550 – 5501K → M in CAA82246. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07382 mRNA. Translation: CAA30295.1.
Z28396
, Z28397, Z28398, Z28399, Z28400, Z28401, Z28402, Z28403, Z28404 Genomic DNA. Translation: CAA82246.1.
X53719 mRNA. Translation: CAA37755.1.
M54975 mRNA. Translation: AAA31048.1.
PIRiI47142.
S00895. NUPG.
RefSeqiNP_999495.1. NM_214330.1.
UniGeneiSsc.81817.

Genome annotation databases

GeneIDi397602.
KEGGissc:397602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07382 mRNA. Translation: CAA30295.1 .
Z28396
, Z28397 , Z28398 , Z28399 , Z28400 , Z28401 , Z28402 , Z28403 , Z28404 Genomic DNA. Translation: CAA82246.1 .
X53719 mRNA. Translation: CAA37755.1 .
M54975 mRNA. Translation: AAA31048.1 .
PIRi I47142.
S00895. NUPG.
RefSeqi NP_999495.1. NM_214330.1.
UniGenei Ssc.81817.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GZD X-ray 2.50 A 2-558 [» ]
1GZV X-ray 3.51 A 2-558 [» ]
ProteinModelPortali P08059.
SMRi P08059. Positions 2-555.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000003094.

Proteomic databases

PaxDbi P08059.
PRIDEi P08059.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397602.
KEGGi ssc:397602.

Organism-specific databases

CTDi 2821.

Phylogenomic databases

eggNOGi COG0166.
HOGENOMi HOG000261370.
HOVERGENi HBG002877.
KOi K01810.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00181 .

Miscellaneous databases

EvolutionaryTracei P08059.

Family and domain databases

Gene3Di 1.10.1390.10. 1 hit.
HAMAPi MF_00473. G6P_isomerase.
InterProi IPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view ]
PANTHERi PTHR11469. PTHR11469. 1 hit.
Pfami PF00342. PGI. 1 hit.
[Graphical view ]
PRINTSi PR00662. G6PISOMERASE.
PROSITEi PS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The neurotrophic factor neuroleukin is 90% homologous with phosphohexose isomerase."
    Chaput M., Claes V., Portetelle D., Clutdts I., Cravador A., Burny A., Gras H., Tartar A.
    Nature 332:454-455(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Burny A.
    Submitted (AUG-1988) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Structure of the gene encoding pig phosphoglucose isomerase."
    Claes V., Kettmann R., Burny A.
    Gene 150:235-241(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Sequence analysis of the pig phosphoglucose isomerase gene promoter region."
    Claes V., Taquet A.N., Kettmann R., Burny A.
    Biochim. Biophys. Acta 1087:339-340(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-17.
    Strain: Belgian Landrace.
  5. "A partial cDNA clone for porcine glucosephosphate isomerase: isolation, characterization and use in detection of restriction fragment length polymorphisms."
    Davies W., Harbitz I., Hauge J.G.
    Anim. Genet. 18:233-240(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 238-357.
  6. "Three-dimensional structure of pig muscle phosphoglucose isomerase at 6-A resolution."
    Muirhead H., Shaw P.J.
    J. Mol. Biol. 89:195-203(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS).
  7. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), PROTEIN SEQUENCE OF 554-558.
  8. "Crystal structure of phosphoglucose isomerase from pig muscle and its complex with 5-phosphoarabinonate."
    Davies C., Muirhead H.
    Proteins 49:577-579(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) ALONE AND IN COMPLEX WITH 5-PHOSPHOARABINONATE.

Entry informationi

Entry nameiG6PI_PIG
AccessioniPrimary (citable) accession number: P08059
Secondary accession number(s): Q29556
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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