P53961 (GPI15_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15
EC=2.4.1.198

Alternative name(s):
PIGH homolog

Gene names

Name:	GPI15
Ordered Locus Names:	YNL038W
ORF Names:	N2687

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	229 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.4
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.
Subunit structure	Component of a complex with GPI1, GPI2, GPI3, GPI15 and ERI1 Probable.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Sequence similarities	Belongs to the PIGH family.
Sequence caution	The sequence AAT93131.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA95905.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	GPI-anchor biosynthesis
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	GPI anchor biosynthetic process Inferred from mutant phenotype Ref.4. Source: SGD
Cellular component	glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex Traceable author statement. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	phosphatidylinositol N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 229	229	Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15		PRO_0000087556
Regions
	Transmembrane	59 – 79	21	Helical; Potential
	Transmembrane	101 – 121	21	Helical; Potential
Experimental info
	Sequence conflict	10	1	K → E in AAT93131. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P53961 [UniParc]. Last modified December 20, 2005. Version 2. Checksum: E89CB192B65FBF06	FASTA	229	26,817
	10 20 30 40 50 60 MISKEYEFGK TSILNRKKYT LVIDEDKNGN FIRFTVLPVS NRKFKKVKQN GRVEINMGIQ 70 80 90 100 110 120 YHQIVLILLL NILFYVICLR SRFLEHINRT FEVTIARSFQ ILIIMGLFAL GTIILVRGPS 130 140 150 160 170 180 VETVTIFKES GLQLSRVKGM VIFPQQWNRK FFEQVEFISN ERIIDVVINE GFCRGFRVIF 190 200 210 220 YLAAIVRKSS TLKLLFPSNL PSIDDQRLIY NISRKYLSKQ EKPLSRPKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-197. Strain: ATCC 204508 / S288c.
[4]	"Ynl038wp (Gpi15p) is the Saccharomyces cerevisiae homologue of human Pig-Hp and participates in the first step in glycosylphosphatidylinositol assembly." Yan B.C., Westfall B.A., Orlean P. Yeast 18:1383-1389(2001) [PubMed: 11746600] [Abstract] Cited for: FUNCTION.
[5]	"Finding functional features in Saccharomyces genomes by phylogenetic footprinting." Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M. Science 301:71-76(2003) [PubMed: 12775844] [Abstract] Cited for: REVISION OF GENE MODEL.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z71314 Genomic DNA. Translation: CAA95905.1. Sequence problems. AY693112 Genomic DNA. Translation: AAT93131.1. Sequence problems. BK006947 Genomic DNA. Translation: DAA10507.1.
PIR	S62960.
RefSeq	NP_014360.2. NM_001182877.1.
3D structure databases
ProteinModelPortal	P53961.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6356N.
IntAct	P53961. 1 interaction.
MINT	MINT-701877.
STRING	P53961.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL038W; YNL038W; YNL038W.
GeneID	855690.
KEGG	sce:YNL038W.
NMPDR	fig|4932.3.peg.5437.
Organism-specific databases
CYGD	YNL038w.
SGD	S000004983. GPI15.
Phylogenomic databases
eggNOG	fuNOG13474.
OrthoDB	EOG4B5SFR.
Gene expression databases
ArrayExpress	P53961.
Genevestigator	P53961.
GermOnline	YNL038W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR019328. GPI-GlcNAc_Trfase_PIG-H_dom. [Graphical view]
KO	K03858.
Pfam	PF10181. PIG-H. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	980004.

Entry information

Entry name

GPI15_YEAST

Accession

Primary (citable) accession number: P53961
Secondary accession number(s): D6W1E1, Q6B1G8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 20, 2005
Last modified:	December 14, 2011
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program