GPI8_YEAST
ID GPI8_YEAST Reviewed; 411 AA.
AC P49018; D6VSW3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=GPI-anchor transamidase;
DE Short=GPI transamidase;
DE EC=3.-.-.-;
DE Flags: Precursor;
GN Name=GPI8; OrderedLocusNames=YDR331W; ORFNames=D9798.2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP CHARACTERIZATION.
RX PubMed=8978684; DOI=10.1002/j.1460-2075.1996.tb01048.x;
RA Benghezal M., Benachour A., Rusconi S., Aebi M., Conzelmann A.;
RT "Yeast Gpi8p is essential for GPI anchor attachment onto proteins.";
RL EMBO J. 15:6575-6583(1996).
RN [5]
RP ACTIVE SITE, AND MUTAGENESIS OF HIS-54; SER-60; CYS-85; HIS-157 AND
RP CYS-199.
RX PubMed=10727241; DOI=10.1021/bi992186o;
RA Meyer U., Benghezal M., Imhof I., Conzelmann A.;
RT "Active site determination of Gpi8p, a caspase-related enzyme required for
RT glycosylphosphatidylinositol anchor addition to proteins.";
RL Biochemistry 39:3461-3471(2000).
RN [6]
RP ACTIVE SITE, AND MUTAGENESIS OF HIS-157 AND CYS-199.
RX PubMed=10793132; DOI=10.1091/mbc.11.5.1523;
RA Ohishi K., Inoue N., Maeda Y., Takeda J., Riezman H., Kinoshita T.;
RT "Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI)
RT transamidase that mediates attachment of GPI to proteins.";
RL Mol. Biol. Cell 11:1523-1533(2000).
RN [7]
RP SUBUNIT.
RX PubMed=11598210; DOI=10.1091/mbc.12.10.3295;
RA Fraering P., Imhof I., Meyer U., Strub J.-M., van Dorsselaer A.,
RA Vionnet C., Conzelmann A.;
RT "The GPI transamidase complex of Saccharomyces cerevisiae contains Gaa1p,
RT Gpi8p, and Gpi16p.";
RL Mol. Biol. Cell 12:3295-3306(2001).
RN [8]
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).
CC -!- FUNCTION: Mediates GPI anchoring in the endoplasmic reticulum, by
CC replacing a protein's C-terminal GPI attachment signal peptide with a
CC pre-assembled GPI. During this transamidation reaction, the GPI
CC transamidase forms a carbonyl intermediate with the substrate protein.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Forms a complex with CDC91, GPI16, GPI17 and GAA1.
CC {ECO:0000269|PubMed:11598210}.
CC -!- INTERACTION:
CC P49018; P39012: GAA1; NbExp=3; IntAct=EBI-7822, EBI-7252;
CC P49018; P38875: GPI16; NbExp=3; IntAct=EBI-7822, EBI-24869;
CC P49018; Q04080: GPI17; NbExp=4; IntAct=EBI-7822, EBI-7777;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC I membrane protein.
CC -!- PTM: The disulfide bond between GPI8 and GPI16 is important for normal
CC enzyme activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR EMBL; U32517; AAB64766.1; -; Genomic_DNA.
DR EMBL; AY557794; AAS56120.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12173.1; -; Genomic_DNA.
DR PIR; S59796; S59796.
DR RefSeq; NP_010618.1; NM_001180639.1.
DR AlphaFoldDB; P49018; -.
DR SMR; P49018; -.
DR BioGRID; 32388; 666.
DR ComplexPortal; CPX-1275; GPI-anchor transamidase complex.
DR DIP; DIP-5371N; -.
DR IntAct; P49018; 56.
DR MINT; P49018; -.
DR STRING; 4932.YDR331W; -.
DR MEROPS; C13.005; -.
DR MaxQB; P49018; -.
DR PaxDb; P49018; -.
DR PRIDE; P49018; -.
DR EnsemblFungi; YDR331W_mRNA; YDR331W; YDR331W.
DR GeneID; 851931; -.
DR KEGG; sce:YDR331W; -.
DR SGD; S000002739; GPI8.
DR VEuPathDB; FungiDB:YDR331W; -.
DR eggNOG; KOG1349; Eukaryota.
DR GeneTree; ENSGT00940000156273; -.
DR HOGENOM; CLU_044656_2_1_1; -.
DR InParanoid; P49018; -.
DR OMA; PGHTNNW; -.
DR BioCyc; YEAST:G3O-29887-MON; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:P49018; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P49018; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; IDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0003923; F:GPI-anchor transamidase activity; IGI:SGD.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IMP:UniProtKB.
DR GO; GO:0031505; P:fungal-type cell wall organization; IC:ComplexPortal.
DR GO; GO:0034394; P:protein localization to cell surface; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR028361; GPI_transamidase.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR48067; PTHR48067; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF500138; GPI8; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Hydrolase; Membrane; Protease; Reference proteome;
KW Signal; Thiol protease; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..411
FT /note="GPI-anchor transamidase"
FT /id="PRO_0000026532"
FT TOPO_DOM 23..376
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 157
FT ACT_SITE 199
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85
FT /note="Interchain (with C-194 in GPI16)"
FT /evidence="ECO:0000250"
FT MUTAGEN 54
FT /note="H->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:10727241"
FT MUTAGEN 60
FT /note="S->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:10727241"
FT MUTAGEN 60
FT /note="S->C: No loss of activity."
FT /evidence="ECO:0000269|PubMed:10727241"
FT MUTAGEN 85
FT /note="C->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:10727241"
FT MUTAGEN 157
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10727241,
FT ECO:0000269|PubMed:10793132"
FT MUTAGEN 199
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10727241,
FT ECO:0000269|PubMed:10793132"
SQ SEQUENCE 411 AA; 47402 MW; ED9F4A1C3B214E28 CRC64;
MRIAMHLPLL LLYIFLLPLS GANNTDAAHE VIATNTNNWA VLVSTSRFWF NYRHMANVLS
MYRTVKRLGI PDSQIILMLS DDVACNSRNL FPGSVFNNKD HAIDLYGDSV EVDYRGYEVT
VENFIRLLTD RWTEDHPKSK RLLTDENSNI FIYMTGHGGD DFLKFQDAEE IASEDIADAF
QQMYEKKRYN EIFFMIDTCQ ANTMYSKFYS PNILAVGSSE MDESSYSHHS DVEIGVAVID
RFTYYCLDFL EQIDKNSTLT LQDLFDSFTF EKIHSHVGVR TDLFDRNPSE VLITDFFANV
QNVIPDDSKP LSVSHYHHYK DHIDTAQYEL NNNVLDLALE TYRKNNQSSK IEKKIKDIKS
TSVLDVDIDS NECFFTSFKQ SATIILALIV TILWFMLRGN TAKATYDLYT N
