GPI14_YEAST
ID GPI14_YEAST Reviewed; 403 AA.
AC P47088; D6VWI9; E9P8R4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=GPI mannosyltransferase 1;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase I;
DE Short=GPI-MT-I;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 14;
GN Name=GPI14; Synonyms=PMH1; OrderedLocusNames=YJR013W;
GN ORFNames=J1444, YJR83.11;
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=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 [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] OF 14-73, AND IDENTIFICATION OF
RP FRAMESHIFT.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-403.
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=16134120; DOI=10.1002/yea.1286;
RA Davydenko S.G., Feng D., Jaentti J., Keraenen S.;
RT "Characterization of GPI14/YJR013w mutation that induces the cell wall
RT integrity signalling pathway and results in increased protein production in
RT Saccharomyces cerevisiae.";
RL Yeast 22:993-1009(2005).
RN [7]
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: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-
CC acyl-PI during GPI precursor assembly. Required for cell wall
CC integrity. {ECO:0000269|PubMed:16134120}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the PIGM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA60935.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA89537.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X87611; CAA60935.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z49513; CAA89537.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY260895; AAP21763.1; -; Genomic_DNA.
DR EMBL; AY557910; AAS56236.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08805.1; -; Genomic_DNA.
DR PIR; S55201; S55201.
DR RefSeq; NP_012547.2; NM_001181671.1.
DR AlphaFoldDB; P47088; -.
DR SMR; P47088; -.
DR BioGRID; 33769; 166.
DR ComplexPortal; CPX-1270; Glycosylphosphatidylinositol-mannosyltransferase I complex.
DR IntAct; P47088; 54.
DR STRING; 4932.YJR013W; -.
DR CAZy; GT50; Glycosyltransferase Family 50.
DR iPTMnet; P47088; -.
DR MaxQB; P47088; -.
DR PaxDb; P47088; -.
DR PRIDE; P47088; -.
DR EnsemblFungi; YJR013W_mRNA; YJR013W; YJR013W.
DR GeneID; 853470; -.
DR KEGG; sce:YJR013W; -.
DR SGD; S000003774; GPI14.
DR VEuPathDB; FungiDB:YJR013W; -.
DR eggNOG; KOG3893; Eukaryota.
DR GeneTree; ENSGT00390000017728; -.
DR HOGENOM; CLU_024220_1_0_1; -.
DR InParanoid; P47088; -.
DR OMA; VTSQYFI; -.
DR BioCyc; YEAST:G3O-31658-MON; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:P47088; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47088; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IPI:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051751; F:alpha-1,4-mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR GO; GO:0035268; P:protein mannosylation; IC:ComplexPortal.
DR InterPro; IPR007704; PIG-M.
DR PANTHER; PTHR12886; PTHR12886; 1.
DR Pfam; PF05007; Mannosyl_trans; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum;
KW Glycosyltransferase; GPI-anchor biosynthesis; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..403
FT /note="GPI mannosyltransferase 1"
FT /id="PRO_0000203084"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..78
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..193
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..310
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..361
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 403 AA; 47166 MW; D1017701557FDB0F CRC64;
MTGEEWGLTV LSFLVRVGFF LFGIYQDANF KVRYTDIDYF VFHDAAKYVY EGKSPYARDT
YRYTPLLSWL LVPNHYFGWF HLGKVIFVIF DLVTGLIIMK LLNQAISRKR ALILESIWLL
NPMVITISTR GNAESVLCCL IMFTLFFLQK SRYTLAGILY GLSIHFKIYP IIYCIPIAIF
IYYNKRNQGP RTQLTSLLNI GLSTLTTLLG CGWAMYKIYG YEFLDQAYLY HLYRTDHRHN
FSVWNMLLYL DSANKENGES NLSRYAFVPQ LLLVLVTGCL EWWNPTFDNL LRVLFVQTFA
FVTYNKVCTS QYFVWYLIFL PFYLSRTHIG WKKGLLMATL WVGTQGIWLS QGYYLEFEGK
NVFYPGLFIA SVLFFVTNVW LLGQFITDIK IPTQPTVSNK KNN
