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   27-MAR-2024, entry version 163.
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; 170.
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; 4932-YJR013W; -.
DR   PeptideAtlas; P47088; -.
DR   EnsemblFungi; YJR013W_mRNA; YJR013W; YJR013W.
DR   GeneID; 853470; -.
DR   KEGG; sce:YJR013W; -.
DR   AGR; SGD:S000003774; -.
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; LINCWIL; -.
DR   OrthoDB; 1973610at2759; -.
DR   BioCyc; YEAST:G3O-31658-MONOMER; -.
DR   UniPathway; UPA00196; -.
DR   BioGRID-ORCS; 853470; 7 hits in 10 CRISPR screens.
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; NAS:ComplexPortal.
DR   GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IPI:SGD.
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; NAS:ComplexPortal.
DR   InterPro; IPR007704; PIG-M.
DR   PANTHER; PTHR12886:SF0; GPI MANNOSYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR12886; PIG-M MANNOSYLTRANSFERASE; 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
//