GWT1_SCHPO
ID GWT1_SCHPO Reviewed; 459 AA.
AC Q9UTL4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=GPI-anchored wall transfer protein 1;
DE EC=2.3.-.-;
DE AltName: Full=Meiotically up-regulated gene 59 protein;
GN Name=gwt1; Synonyms=mug59; ORFNames=SPAC144.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
CC -!- FUNCTION: Probable acetyltransferase, which acetylates the inositol
CC ring of phosphatidylinositol during biosynthesis of GPI-anchor (By
CC similarity). Has a role in meiosis. {ECO:0000250,
CC ECO:0000269|PubMed:12714589, ECO:0000269|PubMed:16303567}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIGW family. {ECO:0000305}.
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DR EMBL; CU329670; CAB59690.1; -; Genomic_DNA.
DR PIR; T37677; T37677.
DR RefSeq; NP_594671.1; NM_001020100.2.
DR AlphaFoldDB; Q9UTL4; -.
DR BioGRID; 279272; 1.
DR STRING; 4896.SPAC144.10c.1; -.
DR PaxDb; Q9UTL4; -.
DR EnsemblFungi; SPAC144.10c.1; SPAC144.10c.1:pep; SPAC144.10c.
DR GeneID; 2542825; -.
DR KEGG; spo:SPAC144.10c; -.
DR PomBase; SPAC144.10c; gwt1.
DR VEuPathDB; FungiDB:SPAC144.10c; -.
DR eggNOG; KOG0411; Eukaryota.
DR HOGENOM; CLU_020802_2_2_1; -.
DR InParanoid; Q9UTL4; -.
DR OMA; GLYVMQP; -.
DR PhylomeDB; Q9UTL4; -.
DR Reactome; R-SPO-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR PRO; PR:Q9UTL4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032216; F:glucosaminyl-phosphatidylinositol O-acyltransferase activity; IGI:PomBase.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IGI:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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; Glycoprotein;
KW GPI-anchor biosynthesis; Meiosis; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..459
FT /note="GPI-anchored wall transfer protein 1"
FT /id="PRO_0000215187"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 459 AA; 52178 MW; 9E496B65FB7E2DBB CRC64;
MSYKLEKEAF VSNLTGSSSI ETCGLLLIGI ACNVLWVNMT ARNILPKGNL GFLVEFFIFC
LIPLFVIYVS SKVGVFTLCI ASFLPSFVLH VISPINWDVL RRKPGCCLTK KNENTFDRRI
AGVTFYRSQM MLVTVTCILA VDFTLFPRRY AKVETWGTSL MDLGVGSFMF SSGTVAGRKN
DIKKPNAFKN VLWNSFILLI LGFARMFLTK SINYQEHVSE YGMHWNFFFT LGFMALGVFF
FRRSLKKVSY FNLATFITLL HHCLLVLTPF QKWALSAPRT NILAQNREGI ASLPGYIAIY
FYGMYTGSVV LADRPLMYTR AESWKRFQRL LFPLCILLVL YLVSNFLSVG VSRRLANTPY
VANVAFINMF FLTIYILIDA YLFPSSVPYG SRVPKLLEDA NNNGLLVFLI ANVLTGVVNL
SFDTLHSSNA KGLTIMTMYL FIICYMAHWL AQHGIRFRL
