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O42154 (G6PC_HAPXE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 61. 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 attributes

Sequence length277 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

D-glucose 6-phosphate + H2O = D-glucose + phosphate.

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the glucose-6-phosphatase family.

Ontologies

Keywords
   Biological processGluconeogenesis
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological_processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionglucose-6-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 277›277Glucose-6-phosphatase
PRO_0000087412

Regions

Transmembrane39 – 5921Helical; Potential
Transmembrane67 – 8721Helical; Potential
Transmembrane131 – 15121Helical; Potential
Transmembrane215 – 23521Helical; Potential
Transmembrane250 – 27021Helical; Potential
Motif274 – 2774Prevents secretion from ER Potential

Sites

Active site401Proton donor Potential
Active site971Nucleophile By similarity
Binding site41Substrate Potential
Binding site911Substrate Potential

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
O42154 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 9A05E82DFE1DA4A0

FASTA27730,971
        10         20         30         40         50         60 
FGERPYWWVH ETKFYGAGPA PSLQQFPITC ETGPGSPSGH AMGAAGVWYV MVTALLSIAR 

        70         80         90        100        110        120 
EKQCPPLLYR FLYIGLWMLM GLVELVVCIS RVYMAAHFPH QVIAGIITGT LVAEVVSKEK 

       130        140        150        160        170        180 
WIYSASLKKY FLITLFLTSF AVGFYVLLKA LDVDLLWTME KAQKWCIRPE WVHLDSAPFA 

       190        200        210        220        230        240 
SLLRNMGSLF GLGLGLHSPF YKTTKMRIMS APLRIGCIVI SVSLLHLLDG WTFSPENHMT 

       250        260        270 
FYALSFGKSA VALLIPTTLV PWALSKIYPV KTEGKNL 

« Hide

References

[1]"Isolation and sequencing of cDNA clones coding for the catalytic unit of glucose-6-phosphatase from two haplochromine cichlid fishes."
Nagl S., Mayer W.E., Klein J.
DNA Seq. 10:25-29(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF008946 mRNA. Translation: AAB69286.1.

3D structure databases

ProteinModelPortalO42154.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG003560.

Enzyme and pathway databases

UniPathwayUPA00138.

Family and domain databases

Gene3D1.20.144.10. 1 hit.
InterProIPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamPF01569. PAP2. 1 hit.
[Graphical view]
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMSSF48317. SSF48317. 1 hit.
ProtoNetSearch...

Entry information

Entry nameG6PC_HAPXE
AccessionPrimary (citable) accession number: O42154
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 61 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