GWT1_YEAST
ID GWT1_YEAST Reviewed; 490 AA.
AC P47026; D6VW93;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=GPI-anchored wall transfer protein 1;
DE EC=2.3.-.-;
GN Name=GWT1; OrderedLocusNames=YJL091C; ORFNames=J0916;
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=7483841; DOI=10.1002/yea.320110709;
RA Miosga T., Schaaff-Gerstenschlaeger I., Chalwatzis N., Baur A., Boles E.,
RA Fournier C., Schmitt S., Velten C., Wilhelm N., Zimmermann F.K.;
RT "Sequence analysis of a 33.1 kb fragment from the left arm of Saccharomyces
RT cerevisiae chromosome X, including putative proteins with leucine zippers,
RT a fungal Zn(II)2-Cys6 binuclear cluster domain and a putative alpha 2-SCB-
RT alpha 2 binding site.";
RL Yeast 11:681-689(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 FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 63-TRP-VAL-64; LEU-209;
RP VAL-259; ASN-330; LEU-362 AND VAL-479.
RX PubMed=12714589; DOI=10.1074/jbc.m301044200;
RA Umemura M., Okamoto M., Nakayama K., Sagane K., Tsukahara K., Hata K.,
RA Jigami Y.;
RT "GWT1 gene is required for inositol acylation of
RT glycosylphosphatidylinositol anchors in yeast.";
RL J. Biol. Chem. 278:23639-23647(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-132 AND VAL-397.
RX PubMed=12753194; DOI=10.1046/j.1365-2958.2003.03481.x;
RA Tsukahara K., Hata K., Nakamoto K., Sagane K., Watanabe N.-A.,
RA Kuromitsu J., Kai J., Tsuchiya M., Ohba F., Jigami Y., Yoshimatsu K.,
RA Nagasu T.;
RT "Medicinal genetics approach towards identifying the molecular target of a
RT novel inhibitor of fungal cell wall assembly.";
RL Mol. Microbiol. 48:1029-1042(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 MUTAGENESIS OF LYS-8.
RX PubMed=16361252; DOI=10.1074/jbc.m504684200;
RA Okamoto M., Yoko-o T., Umemura M., Nakayama K., Jigami Y.;
RT "Glycosylphosphatidylinositol-anchored proteins are required for the
RT transport of detergent-resistant microdomain-associated membrane proteins
RT Tat2p and Fur4p.";
RL J. Biol. Chem. 281:4013-4023(2006).
RN [9]
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: Probable acetyltransferase, which acetylates the inositol
CC ring of phosphatidylinositol during biosynthesis of GPI-anchor.
CC Acetylation during GPI-anchor biosynthesis is not essential for the
CC subsequent mannosylation and is usually removed soon after the
CC attachment of GPIs to proteins. {ECO:0000269|PubMed:12714589,
CC ECO:0000269|PubMed:12753194}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12714589, ECO:0000269|PubMed:14562095}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12714589,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Target of the antifungal compound 1-[4-
CC butylbenzyl]isoquinoline that inhibits cell wall localization of GPI-
CC anchored mannoproteins.
CC -!- SIMILARITY: Belongs to the PIGW family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA58476.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA89384.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z49366; CAA89384.1; ALT_INIT; Genomic_DNA.
DR EMBL; X83502; CAA58476.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006943; DAA08709.1; -; Genomic_DNA.
DR PIR; S56868; S56868.
DR RefSeq; NP_012444.2; NM_001181524.1.
DR AlphaFoldDB; P47026; -.
DR BioGRID; 33666; 459.
DR DIP; DIP-4481N; -.
DR IntAct; P47026; 9.
DR MINT; P47026; -.
DR STRING; 4932.YJL091C; -.
DR TCDB; 9.B.315.1.5; the glycoslyphosphatidylinositol (gpi) membrane anchoring protein gwt1 (gwt1) family.
DR MaxQB; P47026; -.
DR PaxDb; P47026; -.
DR PRIDE; P47026; -.
DR EnsemblFungi; YJL091C_mRNA; YJL091C; YJL091C.
DR GeneID; 853354; -.
DR KEGG; sce:YJL091C; -.
DR SGD; S000003627; GWT1.
DR VEuPathDB; FungiDB:YJL091C; -.
DR eggNOG; KOG0411; Eukaryota.
DR GeneTree; ENSGT00390000013520; -.
DR HOGENOM; CLU_020802_2_2_1; -.
DR InParanoid; P47026; -.
DR OMA; GLYVMQP; -.
DR BioCyc; YEAST:G3O-31546-MON; -.
DR Reactome; R-SCE-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR PRO; PR:P47026; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47026; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; HDA:SGD.
DR GO; GO:0032216; F:glucosaminyl-phosphatidylinositol O-acyltransferase activity; IMP:SGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IDA:SGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR InterPro; IPR009447; PIGW/GWT1.
DR PANTHER; PTHR20661; PTHR20661; 1.
DR Pfam; PF06423; GWT1; 1.
DR PIRSF; PIRSF017321; GWT1; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..490
FT /note="GPI-anchored wall transfer protein 1"
FT /id="PRO_0000215188"
FT TOPO_DOM 1..19
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..157
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..231
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..301
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..390
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..460
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 8
FT /note="K->E: In gwt1-10; impairs the transport of
FT detergent-resistant microdomain-associated membrane
FT proteins TAT2 and FUR4."
FT /evidence="ECO:0000269|PubMed:16361252"
FT MUTAGEN 63..64
FT /note="WV->RA: In gwt1-20; temperature sensitive mutant
FT that induces a delay in export of GPI-anchored proteins."
FT /evidence="ECO:0000269|PubMed:12714589"
FT MUTAGEN 132
FT /note="G->R: Resistant to the drug 1-[4-
FT butylbenzyl]isoquinoline (BIQ)."
FT /evidence="ECO:0000269|PubMed:12753194"
FT MUTAGEN 209
FT /note="L->P: In gwt1-28; temperature sensitive mutant that
FT induces a delay in export of GPI-anchored proteins; when
FT associated with D-259."
FT /evidence="ECO:0000269|PubMed:12714589"
FT MUTAGEN 259
FT /note="V->D: In gwt1-28; temperature sensitive mutant that
FT induces a delay in export of GPI-anchored proteins; when
FT associated with P-209."
FT /evidence="ECO:0000269|PubMed:12714589"
FT MUTAGEN 330
FT /note="N->S: In gwt1-16; temperature sensitive mutant that
FT induces a delay in export of GPI-anchored proteins; when
FT associated with P-362 and A-479."
FT /evidence="ECO:0000269|PubMed:12714589"
FT MUTAGEN 362
FT /note="L->P: In gwt1-16; temperature sensitive mutant that
FT induces a delay in export of GPI-anchored proteins; when
FT associated with S-330 and A-479."
FT /evidence="ECO:0000269|PubMed:12714589"
FT MUTAGEN 397
FT /note="V->I: Resistant to the drug 1-[4-
FT butylbenzyl]isoquinoline (BIQ)."
FT /evidence="ECO:0000269|PubMed:12753194"
FT MUTAGEN 479
FT /note="V->A: In gwt1-16; temperature sensitive mutant that
FT induces a delay in export of GPI-anchored proteins; when
FT associated with S-330 and P-362."
FT /evidence="ECO:0000269|PubMed:12714589"
SQ SEQUENCE 490 AA; 55466 MW; 8BE4AE710DB93A98 CRC64;
MSTLKQRKED FVTGLNGGSI TEINAVTSIA LVTYISWNLL KNSNLMPPGI SSVQYIIDFA
LNWVALLLSI TIYASEPYLL NTLILLPCLL AFIYGKFTSS SKPSNPIYNK KKMITQRFQL
EKKPYITAYR GGMLILTAIA ILAVDFPIFP RRFAKVETWG TSLMDLGVGS FVFSNGIVSS
RALLKNLSLK SKPSFLKNAF NALKSGGTLL FLGLLRLFFV KNLEYQEHVT EYGVHWNFFI
TLSLLPLVLT FIDPVTRMVP RCSIAIFISC IYEWLLLKDD RTLNFLILAD RNCFFSANRE
GIFSFLGYCS IFLWGQNTGF YLLGNKPTLN NLYKPSTQDV VAASKKSSTW DYWTSVTPLS
GLCIWSTIFL VISQLVFQYH PYSVSRRFAN LPYTLWVITY NLLFLTGYCL TDKIFGNSSE
YYKVAECLES INSNGLFLFL LANVSTGLVN MSMVTIDSSP LKSFLVLLAY CSFIAVISVF
LYRKRIFIKL
