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Q9N1E2

- G6PI_RABIT

UniProt

Q9N1E2 - G6PI_RABIT

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Protein
Glucose-6-phosphate isomerase
Gene
GPI
Organism
Oryctolagus cuniculus (Rabbit)
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 donor2 Publications
Active sitei389 – 38912 Publications
Active sitei519 – 51912 Publications

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

SABIO-RKQ9N1E2.
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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: 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 – 11Removed By similarity
Chaini2 – 558557Glucose-6-phosphate isomeraseUniRule annotation
PRO_0000180541Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
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

PRIDEiQ9N1E2.

Interactioni

Subunit structurei

Homodimer in the catalytically active form, monomer in the secreted form.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64
Helixi8 – 2013
Helixi21 – 233
Helixi26 – 316
Helixi36 – 394
Beta strandi41 – 455
Beta strandi50 – 545
Beta strandi57 – 593
Helixi62 – 7413
Helixi77 – 859
Turni92 – 954
Helixi100 – 1034
Beta strandi112 – 1187
Helixi119 – 13820
Beta strandi151 – 1555
Helixi158 – 1603
Helixi162 – 1709
Helixi172 – 1743
Beta strandi180 – 1845
Helixi189 – 1968
Helixi201 – 2033
Beta strandi204 – 2096
Beta strandi211 – 2133
Helixi216 – 23318
Helixi236 – 2383
Helixi239 – 2424
Beta strandi243 – 2486
Helixi250 – 2567
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
Turni384 – 3863
Helixi387 – 3893
Helixi392 – 3976
Beta strandi398 – 4003
Beta strandi404 – 4118
Helixi417 – 4193
Helixi420 – 43819
Helixi442 – 45110
Helixi456 – 4627
Helixi463 – 4664
Beta strandi474 – 4818
Helixi484 – 50421
Helixi513 – 5153
Helixi516 – 52914
Beta strandi530 – 5334
Helixi540 – 55213

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DQRX-ray2.50A/B2-558[»]
1G98X-ray1.90A/B1-558[»]
1HM5X-ray1.80A/B1-558[»]
1HOXX-ray2.10A/B1-558[»]
1KOJX-ray1.90A/B2-558[»]
1N8TX-ray2.50A/B2-558[»]
1XTBX-ray2.00A/B1-558[»]
ProteinModelPortaliQ9N1E2.
SMRiQ9N1E2. Positions 2-558.

Miscellaneous databases

EvolutionaryTraceiQ9N1E2.

Family & Domainsi

Sequence similaritiesi

Belongs to the GPI family.

Phylogenomic databases

eggNOGiCOG0166.
HOGENOMiHOG000261370.
HOVERGENiHBG002877.

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.

Q9N1E2-1 [UniParc]FASTAAdd to Basket

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MAALTRNPQF QKLQQWHREH GSELNLRHLF DTDKERFNHF SLTLNTNHGH    50
ILLDYSKNLV TEEVMHMLLD LAKSRGVEAA RESMFNGEKI NSTEDRAVLH 100
VALRNRSNTP IVVDGKDVMP EVNKVLDKMK AFCQRVRSGD WKGYTGKTIT 150
DVINIGIGGS DLGPLMVTEA LKPYSSGGPR VWFVSNIDGT HIAKTLACLN 200
PESSLFIIAS KTFTTQETIT NAETAKDWFL LSAKDPSTVA KHFVALSTNT 250
AKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA 300
HWMDQHFRTT PLEKNAPVLL AMLGIWYINC FGCETQAVLP YDQYLHRFAA 350
YFQQGDMESN GKYITKSGAR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK 400
MIPCDFLIPV QTQHPIRKGL HHKILLANFL AQTEALMKGK STEEARKELQ 450
AAGKSPEDLM KLLPHKVFEG NRPTNSIVFT KLTPFILGAL IAMYEHKIFV 500
QGVVWDINSF DQWGVELGKQ LAKKIEPELD GSSPVTSHDS STNGLINFIK 550
QQREAKIQ 558
Length:558
Mass (Da):62,747
Last modified:January 23, 2007 - v3
Checksum:iBB4E3AB31BBD55E4
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti223 – 2231E → K in AAF35988. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF199601 mRNA. Translation: AAF13713.2.
AF222069 mRNA. Translation: AAF35988.1.
RefSeqiNP_001075538.1. NM_001082069.2.
UniGeneiOcu.278.

Genome annotation databases

GeneIDi100008744.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF199601 mRNA. Translation: AAF13713.2 .
AF222069 mRNA. Translation: AAF35988.1 .
RefSeqi NP_001075538.1. NM_001082069.2.
UniGenei Ocu.278.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DQR X-ray 2.50 A/B 2-558 [» ]
1G98 X-ray 1.90 A/B 1-558 [» ]
1HM5 X-ray 1.80 A/B 1-558 [» ]
1HOX X-ray 2.10 A/B 1-558 [» ]
1KOJ X-ray 1.90 A/B 2-558 [» ]
1N8T X-ray 2.50 A/B 2-558 [» ]
1XTB X-ray 2.00 A/B 1-558 [» ]
ProteinModelPortali Q9N1E2.
SMRi Q9N1E2. Positions 2-558.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi Q9N1E2.
ChEMBLi CHEMBL1770045.

Proteomic databases

PRIDEi Q9N1E2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100008744.

Organism-specific databases

CTDi 2821.

Phylogenomic databases

eggNOGi COG0166.
HOGENOMi HOG000261370.
HOVERGENi HBG002877.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00181 .
SABIO-RK Q9N1E2.

Miscellaneous databases

EvolutionaryTracei Q9N1E2.

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. "Rabbit phosphoglucose isomerase/neuroleukin/autocrine motility factor: cloning via interspecies identity."
    Li X., Chirgwin J.M.
    Biochim. Biophys. Acta 1476:363-367(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: New Zealand white.
    Tissue: Fast-twitch skeletal muscle.
  2. "Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukin, autocrine motility factor, and differentiation mediator."
    Jeffery C.J., Bahnson B.J., Chien W., Ringe D., Petsko G.A.
    Biochemistry 39:955-964(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    Strain: New Zealand white.
    Tissue: Muscle.
  3. "Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonate identifies the role of Glu357 in catalysis."
    Jeffery C.J., Hardre R., Salmon L.
    Biochemistry 40:1560-1566(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH 5-PHOSPHO-D-ARABINONATE, ACTIVE SITE.
  4. "Crystal structure of rabbit phosphoglucose isomerase complexed with its substrate D-fructose 6-phosphate."
    Lee J.H., Chang K.Z., Patel V., Jeffery C.J.
    Biochemistry 40:7799-7805(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH F6P, ACTIVE SITE.
  5. "Conformational changes in phosphoglucose isomerase induced by ligand binding."
    Arsenieva D., Jeffery C.J.
    J. Mol. Biol. 323:77-84(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT.
  6. "The crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid."
    Arsenieva D., Hardre R., Salmon L., Jeffery C.J.
    Proc. Natl. Acad. Sci. U.S.A. 99:5872-5877(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH 5-PHOSPHO-D-ARABINONOHYDROXAMIC ACID.
  7. "Structure of native phosphoglucose isomerase from rabbit: conformational changes associated with catalytic function."
    Davies C., Muirhead H.
    Acta Crystallogr. D 59:453-465(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  8. "The crystal structure of rabbit phosphoglucose isomerase complexed with D-sorbitol-6-phosphate, an analog of the open chain form of D-glucose-6-phosphate."
    Lee J.H., Jeffery C.J.
    Protein Sci. 14:727-734(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH D-SORBITOL-6-PHOSPHATE.

Entry informationi

Entry nameiG6PI_RABIT
AccessioniPrimary (citable) accession number: Q9N1E2
Secondary accession number(s): Q9N184
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 91 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, 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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