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Q8TGB2 (GPI7_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
GPI ethanolamine phosphate transferase 2
EC=2.-.-.-
Alternative name(s):
Glycosylphosphatidylinositol-anchor biosynthesis protein 7
Gene names
Name:LAS21
Synonyms:GPI7
ORF Names:CaO19.11547, CaO19.4064
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida ›

Protein attributes

Sequence length892 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose By similarity.

Pathway

Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Disruption phenotype

Cell-wall protein anchorage defects. Ref.3

Sequence similarities

Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 892892GPI ethanolamine phosphate transferase 2
PRO_0000246193

Regions

Transmembrane413 – 43321Helical; Potential
Transmembrane447 – 46721Helical; Potential
Transmembrane473 – 49321Helical; Potential
Transmembrane495 – 51420Helical; Potential
Transmembrane539 – 55921Helical; Potential
Transmembrane581 – 60121Helical; Potential
Transmembrane648 – 66821Helical; Potential
Transmembrane697 – 71721Helical; Potential
Transmembrane726 – 74621Helical; Potential
Transmembrane768 – 78821Helical; Potential
Transmembrane820 – 84021Helical; Potential
Transmembrane850 – 87021Helical; Potential

Amino acid modifications

Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation1551N-linked (GlcNAc...) Potential
Glycosylation1941N-linked (GlcNAc...) Potential
Glycosylation5161N-linked (GlcNAc...) Potential
Glycosylation8801N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict541Q → H in AAL83897. Ref.1
Sequence conflict571N → T in AAL83897. Ref.1
Sequence conflict941R → H in AAL83897. Ref.1
Sequence conflict4371F → L in AAL83897. Ref.1
Sequence conflict4391V → A in AAL83897. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8TGB2 [UniParc].

Last modified July 25, 2006. Version 2.
Checksum: 3A5C37241363A19A

FASTA892101,640
        10         20         30         40         50         60 
MSGSLNSRWV VQVSLTIINI IGFLVFLRGF FPSKVVLPGF NSFQDSTKSP FSDQYGNPQF 

        70         80         90        100        110        120 
NKFILMVVDA MRSDFCFSDR SNFSFLHQLI NQGRALPFTA FSNPPTVTLP RLKGITTGGT 

       130        140        150        160        170        180 
PNFLDAILNV ADDQDDSQGL HNQDSWVHQF RHSNNKTINF FGDDTWLKLF QDQFTEFEGT 

       190        200        210        220        230        240 
NSFFVSDFTE VDNNVTRHLD DQLSSNKWDG LILHYLGLDH IGHKGGPESP YMKPKQIEMD 

       250        260        270        280        290        300 
KILQRLYTYV TKNDDTLIVL MGDHGMNEIG NHGGSSPGET SAALSFISPK FNHKGESPLP 

       310        320        330        340        350        360 
YNSDYSYHHK ISQIDLVPTL AALLNFPIPK NSLGVIAKEI LEIWPENQRI KILLENCAQI 

       370        380        390        400        410        420 
MNLYEAKYGP SGEVWTQWEN LQAKQHPIAD YYEFLQDIQS EMASSATNYG YKDIYAGALI 

       430        440        450        460        470        480 
LVITVLAVIV VFNRYFFTVS NMNISSVMFY ELFVVLYSLH FHGSSLIEEE HQIWYFFTTA 

       490        500        510        520        530        540 
TLLFLAITFF DTFKSLQNFI SFGVLFACIR FMRSWNNSGQ KYSSQYNIAY YLSHSNPNLM 

       550        560        570        580        590        600 
WGLIILTYFV LTLCIYIQGS LVPTFAFSFG KRLPDVKDPG GLISFIVVFV ATSVSFSFKL 

       610        620        630        640        650        660 
LQYYIDGNTI PKWLNRFLLW IIESHHIDLS SATLEDNELK FQLQSVSIQL SKFTTIILLL 

       670        680        690        700        710        720 
LVISRVIIGK IRKIRYGTIT DITNIMTIYL IHQTRHENIP IFLALMFAKF ALSKLIYRKT 

       730        740        750        760        770        780 
NRIDQYILTV TMTVLCLQNL TFFCMGNTNS LATVDLSNAY NGVKAYNVFL VGLLTFVSNF 

       790        800        810        820        830        840 
AGPIFWSLSG LQLLYEPSLL NFNGPATTDL LHYTGLKKSI LLVKSLISLF FYTVSAVNLV 

       850        860        870        880        890 
GSCINLRFHL FIWTVFSPKL LFFGSWILFV NVLIDLYFGN NSIVVLKTNI LL

« Hide

References

« Hide 'large scale' references
[1]"Complete glycosylphosphatidylinositol anchors are required in Candida albicans for full morphogenesis, virulence and resistance to macrophages."
Richard M., Ibata-Ombetta S., Dromer F., Bordon-Pallier F., Jouault T., Gaillardin C.
Mol. Microbiol. 44:841-853(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.
[2]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.
[3]"GPI7 affects cell-wall protein anchorage in Saccharomyces cerevisiae and Candida albicans."
Richard M., De Groot P., Courtin O., Poulain D., Klis F., Gaillardin C.
Microbiology 148:2125-2133(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF348498 Genomic DNA. Translation: AAL83897.1.
AACQ01000242 Genomic DNA. Translation: EAK91495.1.
AACQ01000243 Genomic DNA. Translation: EAK91485.1.
AACQ01000231 Genomic DNA. No translation available.
AACQ01000232 Genomic DNA. No translation available.
RefSeqXP_710733.1. XM_705641.1.
XP_710743.1. XM_705651.1.

3D structure databases

ProteinModelPortalQ8TGB2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3647663.
3647672.
KEGGcal:CaO19.11547.
cal:CaO19.4064.

Phylogenomic databases

eggNOGCOG1524.
KOK05310.

Enzyme and pathway databases

UniPathwayUPA00196.

Family and domain databases

Gene3D3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR002591. Phosphodiest/P_Trfase.
[Graphical view]
PfamPF01663. Phosphodiest. 1 hit.
[Graphical view]
SUPFAMSSF53649. Alkaline_phosphatase_core. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGPI7_CANAL
AccessionPrimary (citable) accession number: Q8TGB2
Secondary accession number(s): Q59LX3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: April 3, 2013
This is version 53 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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