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Reviewed, UniProtKB/Swiss-Prot Q9Y7L7 (GPI15_SCHPO)

Last modified January 19, 2010. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphatidylinositol N-acetylglucosaminyltransferase subunit gpi15
    EC=2.4.1.198
Alternative name(s):
    PIGH homolog
Gene names
Name: gpi15
ORF Names: SPBC685.05
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis By similarity.

Catalytic activity

UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol.

Pathway

Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Potential Ref.2.

Sequence similarities

Belongs to the PIGH family.

Ontologies

Keywords
   Biological processGPI-anchor biosynthesis
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processGPI anchor biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum membrane

Inferred by curator. Source: GeneDB_SPombe

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionphosphatidylinositol N-acetylglucosaminyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 160160Phosphatidylinositol N-acetylglucosaminyltransferase subunit gpi15
PRO_0000351441

Regions

Transmembrane22 – 4221 Potential
Transmembrane48 – 6821 Potential

Sequences

Sequence LengthMass (Da)Tools
Q9Y7L7-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 1043101E5F375F08

FASTA16018,036
        10         20         30         40         50         60 
MLTIKRYPGA IEFTVHTSKS YGTQMFALCF ISFVIGATSL AIGRSPKIII TLVELSFLLS 

        70         80         90        100        110        120 
LFHIISGVNH ESLFVIRDLG VQTNCHSIVP WKSSSKLIPL DSIRDIFINE GFRKFDVCYY 

       130        140        150        160 
MGIAIESETE IHVVFPTLLP RHDVLQKVYK ETVILLANNS 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAB39362.1.
PIRT40636.
RefSeqNP_596139.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9Y7L7.

Genome annotation databases

GeneID2540532.
GenomeReviewsGene locus gpi15 in contig CU329671_GR.
KEGGspo:SPBC685.05.
NMPDRfig|4896.1.peg.2005.

Organism-specific databases

GeneDB_SpombeSPBC685.05.

Phylogenomic databases

eggNOGfuNOG13474.
OrthoDBEOG9CZCZJ.
PhylomeDBQ9Y7L7.

Gene expression databases

ArrayExpressQ9Y7L7.

Family and domain databases

InterProIPR019328. GPI-GlcNAc_cplx_Trfase_PIG-H.
[Graphical view]
PfamPF10181. PIG-H. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGPI15_SCHPO
AccessionPrimary (citable) accession number: Q9Y7L7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: November 1, 1999
Last modified: January 19, 2010
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents