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Reviewed, UniProtKB/Swiss-Prot O59802 (GPI2_SCHPO)

Last modified November 3, 2009. Version 39. 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 GPI2 subunit
    EC=2.4.1.198
Gene names
Name: gpi2
ORF Names: SPCC550.04c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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. Ref.2

Sequence similarities

Belongs to the PIGC 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 Ref.2

Inferred from direct assay. 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 – 324324Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit
PRO_0000372382

Regions

Topological domain1 – 7979Cytoplasmic Potential
Transmembrane80 – 10021 Potential
Topological domain101 – 1077Lumenal Potential
Transmembrane108 – 12821 Potential
Topological domain129 – 14012Cytoplasmic Potential
Transmembrane141 – 16121 Potential
Topological domain162 – 17110Lumenal Potential
Transmembrane172 – 19221 Potential
Topological domain193 – 22331Cytoplasmic Potential
Transmembrane224 – 24421 Potential
Topological domain245 – 2506Lumenal Potential
Transmembrane251 – 27121 Potential
Topological domain272 – 2765Cytoplasmic Potential
Transmembrane277 – 29923 Potential
Topological domain300 – 32425Lumenal Potential

Sequences

Sequence LengthMass (Da)Tools
O59802-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 7C14AB3EA9138DD1

FASTA32436,654
        10         20         30         40         50         60 
MDEVCAAPAP KKMVAKSLVL NTFRKASVKE VVELKKPWKK VLWRKQDYPD NFIDESFLNG 

        70         80         90        100        110        120 
LQRNVNIQVT DFWSLVADSL PVSQHLSSVV IFASVFVSIY RNQLSCALVG FVSNVSAVAA 

       130        140        150        160        170        180 
FILWDFVLRK PCNNRTFPNY MGIVKSCILI VLTLAGLSPI LMSLTKSTSP DSVWAIAVWL 

       190        200        210        220        230        240 
FLANVFFHEY TTETIRPHVR LHNSLSTNAA LSASVVLASR LEKSINVFFF ILFAVHWFAL 

       250        260        270        280        290        300 
FPIFRKYIHV FSFYADMLMT LVLIISAYIA LNAVASVVIA FVFLSLIFFI SFICPIWFIK 

       310        320 
LQRFKNEIHG PWDIALPKLG PSKG 

« 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

CU329672 Genomic DNA. Translation: CAA19108.1.
PIRT41379.
RefSeqNP_588096.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO59802.

Genome annotation databases

GeneID2539262.
GenomeReviewsGene locus gpi2 in contig CU329672_GR.
KEGGspo:SPCC550.04c.
NMPDRfig|4896.1.peg.434.

Organism-specific databases

GeneDB_SpombeSPCC550.04c.

Phylogenomic databases

OMAVVIQQLC.

Gene expression databases

ArrayExpressO59802.

Family and domain databases

InterProIPR009450. Plno_GlcNAc_GPI2.
[Graphical view]
PANTHERPTHR12982. GPI2. 1 hit.
PfamPF06432. GPI2. 1 hit.
[Graphical view]
PIRSFPIRSF016104. GPI2. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGPI2_SCHPO
AccessionPrimary (citable) accession number: O59802
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: August 1, 1998
Last modified: November 3, 2009
This is version 39 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