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Q9N1E2

- G6PI_RABIT

UniProt

Q9N1E2 - G6PI_RABIT

Protein

Glucose-6-phosphate isomerase

Gene

GPI

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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.By similarity

    Catalytic activityi

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

    Pathwayi

    Sites

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

    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

    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

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 558557Glucose-6-phosphate isomerasePRO_0000180541Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei12 – 121N6-acetyllysineBy similarity
    Modified residuei109 – 1091PhosphothreonineBy similarity
    Modified residuei142 – 1421N6-acetyllysineBy similarity
    Modified residuei185 – 1851Phosphoserine; by CK2By similarity
    Modified residuei454 – 4541N6-malonyllysineBy similarity

    Post-translational modificationi

    ISGylated.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ9N1E2.

    Interactioni

    Subunit structurei

    Homodimer in the catalytically active form, monomer in the secreted form.5 Publications

    Structurei

    Secondary structure

    1
    558
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9N1E2.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GPI family.Curated

    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

    « Hide

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti223 – 2231E → K in AAF35988. (PubMed:10653639)Curated

    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: October 1, 2014
    This is version 92 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