GPI7_YEAST
ID GPI7_YEAST Reviewed; 830 AA.
AC P40367; D6VWC0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=GPI ethanolamine phosphate transferase 2;
DE EC=2.-.-.-;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 7;
DE AltName: Full=Local anestheticum-sensitive protein 21;
DE Flags: Precursor;
GN Name=LAS21; Synonyms=GPI7; OrderedLocusNames=YJL062W;
GN ORFNames=HRC830, J1132;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7762302; DOI=10.1002/yea.320110108;
RA Vandenbol M., Durand P., Dion C., Portetelle D., Hilger F.;
RT "Sequence of a 17.1 kb DNA fragment from chromosome X of Saccharomyces
RT cerevisiae includes the mitochondrial ribosomal protein L8.";
RL Yeast 11:57-60(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PRELIMINARY FUNCTION.
RX PubMed=10734606; DOI=10.1266/ggs.74.241;
RA Toh-e A., Oguchi T.;
RT "Las21 participates in extracellular/cell surface phenomena in
RT Saccharomyces cerevisiae.";
RL Genes Genet. Syst. 74:241-256(1999).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=10329735; DOI=10.1074/jbc.274.21.15251;
RA Benachour A., Sipos G., Flury I., Reggiori F., Canivenc-Gansel E.,
RA Vionnet C., Conzelmann A., Benghezal M.;
RT "Deletion of GPI7, a yeast gene required for addition of a side chain to
RT the glycosylphosphatidylinositol (GPI) core structure, affects GPI protein
RT transport, remodeling, and cell wall integrity.";
RL J. Biol. Chem. 274:15251-15261(1999).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP FUNCTION.
RX PubMed=14985347; DOI=10.1074/jbc.m401873200;
RA Imhof I., Flury I., Vionnet C., Roubaty C., Egger D., Conzelmann A.;
RT "Glycosylphosphatidylinositol (GPI) proteins of Saccharomyces cerevisiae
RT contain ethanolamine phosphate groups on the alpha1,4-linked mannose of the
RT GPI anchor.";
RL J. Biol. Chem. 279:19614-19627(2004).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF 153-ASP-ASP-154.
RX PubMed=15452134; DOI=10.1074/jbc.m405232200;
RA Fujita M., Yoko-o T., Okamoto M., Jigami Y.;
RT "GPI7 involved in glycosylphosphatidylinositol biosynthesis is essential
RT for yeast cell separation.";
RL J. Biol. Chem. 279:51869-51879(2004).
RN [10]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC ethanolamine phosphate to the GPI second mannose. Although not
CC essential, addition of ethanolamine phosphate to the second mannose
CC plays an important role in cell separation via the GPI-based
CC modification of daughter-specific proteins.
CC {ECO:0000269|PubMed:10329735, ECO:0000269|PubMed:14985347,
CC ECO:0000269|PubMed:15452134}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10329735, ECO:0000269|PubMed:14562095}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10329735,
CC ECO:0000269|PubMed:14562095}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10329735}.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
CC {ECO:0000305}.
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DR EMBL; Z34288; CAA84061.1; -; Genomic_DNA.
DR EMBL; Z49337; CAA89353.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08736.1; -; Genomic_DNA.
DR PIR; S50810; S50810.
DR RefSeq; NP_012473.1; NM_001181495.1.
DR AlphaFoldDB; P40367; -.
DR SMR; P40367; -.
DR BioGRID; 33692; 385.
DR DIP; DIP-7713N; -.
DR IntAct; P40367; 4.
DR MINT; P40367; -.
DR STRING; 4932.YJL062W; -.
DR MaxQB; P40367; -.
DR PaxDb; P40367; -.
DR PRIDE; P40367; -.
DR EnsemblFungi; YJL062W_mRNA; YJL062W; YJL062W.
DR GeneID; 853384; -.
DR KEGG; sce:YJL062W; -.
DR SGD; S000003598; LAS21.
DR VEuPathDB; FungiDB:YJL062W; -.
DR eggNOG; KOG2125; Eukaryota.
DR GeneTree; ENSGT00910000144269; -.
DR HOGENOM; CLU_004770_0_0_1; -.
DR InParanoid; P40367; -.
DR OMA; HIGHKTG; -.
DR BioCyc; YEAST:G3O-31524-MON; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:P40367; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40367; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:SGD.
DR GO; GO:0051267; F:CP2 mannose-ethanolamine phosphotransferase activity; IMP:SGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR CDD; cd16024; GPI_EPT_2; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037674; PIG-G_N.
DR InterPro; IPR039527; PIGG/GPI7.
DR InterPro; IPR045687; PIGG/GPI7_C.
DR PANTHER; PTHR23072; PTHR23072; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF19316; PIGO_PIGG; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..830
FT /note="GPI ethanolamine phosphate transferase 2"
FT /id="PRO_0000203059"
FT TOPO_DOM 33..321
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..439
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..533
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..598
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..651
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..682
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 683..703
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 704..724
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 746..768
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 769..789
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 790..805
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 806..826
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 827..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 153..154
FT /note="DD->AA: In GPI7-2; temperature-sensitive mutant that
FT shows defects in cell separation and a daughter cell-
FT specific growth defect."
FT /evidence="ECO:0000269|PubMed:15452134"
SQ SEQUENCE 830 AA; 94851 MW; 34A6DA4B4F54F20B CRC64;
MNLKQFTCLS CAQLLAILLF IFAFFPRKIV LTGISKQDPD QDRDLQRDRP FQKLVFVIID
ALRSDFLFDS QISHFNNVHQ WLNTGEAWGY TSFANPPTVT LPRLKSITTG STPSFIDLLL
NVAQDIDSND LSEHDSWLQQ FIQHNNTIRF MGDDTWLKLF PQQWFDFADP THSFFVSDFT
QVDNNVTRNL PGKLFQEWAQ WDVAILHYLG LDHIGHKDGP HSKFMAAKHQ EMDSILKSIY
DEVLEHEDDD DTLICVLGDH GMNELGNHGG SSAGETSAGL LFLSPKLAQF ARPESQVNYT
LPINASPDWN FQYLETVQQI DIVPTIAALF GMPIPMNSVG IIIPDFLQLL PNKLASMKEN
FMHLWKLSDH HGEVALDDFT AEDIYTKMYT IQETLTKSAT NYNYPLLTLA FVGFLIITII
AIYVLLRYSG PDFWQLRVSS LSVLLVSIIL GVSTFASSFI EEEHQLWWWI VTAFSAVPLF
VYRLNVLIIV RWFIMMACVR SIKFWNNSGQ KFIYSNVMSN LLNQNPSWKW CLNMLTFLVL
IMASAGFQVL HFIVTTILVG LCFTYKISWE IVNGNQAEIP LFMHDLLAKI DFAPTESNLI
VLARVFFQAW AIVVISRLVL TKLKVLNKNY LIKDMKVYIT ILLMFQTSSQ NIGQFLVFQI
LESQIFYFFQ NIPTASLTST SKIYFSNLVS LILQNFTFFQ FGGTNSISTI DLGNAYHGVS
SDYNIYVVGI LMSVANFAPA IYWSMLPWSI NYASIPAQVK LQTFIRSKLP AFTYHCIFGT
CLMTACVVLR FHLFIWSVFS PKLCYFLGWN FVMGLLNGWL PELALLCALD
