GPI18_YEAST
ID GPI18_YEAST Reviewed; 433 AA.
AC P38211; D6VQ05; P89496;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=GPI mannosyltransferase 2;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase II;
DE Short=GPI-MT-II;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 18;
GN Name=GPI18; OrderedLocusNames=YBR004C; ORFNames=YBR0110;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 187.
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 FUNCTION.
RX PubMed=15720390; DOI=10.1111/j.1742-4658.2005.04551.x;
RA Fabre A.-L., Orlean P., Taron C.H.;
RT "Saccharomyces cerevisiae Ybr004c and its human homologue are required for
RT addition of the second mannose during glycosylphosphatidylinositol
RT precursor assembly.";
RL FEBS J. 272:1160-1168(2005).
RN [4]
RP FUNCTION.
RX PubMed=15623507; DOI=10.1074/jbc.m413867200;
RA Kang J.Y., Hong Y., Ashida H., Shishioh N., Murakami Y., Morita Y.S.,
RA Maeda Y., Kinoshita T.;
RT "PIG-V involved in transferring the second mannose in
RT glycosylphosphatidylinositol.";
RL J. Biol. Chem. 280:9489-9497(2005).
RN [5]
RP FUNCTION, INTERACTION WITH PGA1, AND SUBCELLULAR LOCATION.
RX PubMed=17615295; DOI=10.1091/mbc.e07-03-0258;
RA Sato K., Noda Y., Yoda K.;
RT "Pga1 is an essential component of glycosylphosphatidylinositol-
RT mannosyltransferase II of Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 18:3472-3485(2007).
CC -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC anchor biosynthesis. Responsible for the transfer of the second mannose
CC to the glycosylphosphatidylinositol during GPI precursor assembly.
CC {ECO:0000269|PubMed:15623507, ECO:0000269|PubMed:15720390,
CC ECO:0000269|PubMed:17615295}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Part of the GPI mannosyltransferase 2 complex composed of
CC GPI18 and PGA1.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17615295}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17615295}.
CC -!- SIMILARITY: Belongs to the PIGV family. {ECO:0000305}.
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DR EMBL; Z35873; CAA84940.1; -; Genomic_DNA.
DR EMBL; Z35874; CAA84942.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07125.2; -; Genomic_DNA.
DR PIR; S45856; S45856.
DR RefSeq; NP_009558.2; NM_001178352.2.
DR AlphaFoldDB; P38211; -.
DR BioGRID; 32705; 137.
DR ComplexPortal; CPX-1269; Glycosylphosphatidylinositol-mannosyltransferase II complex.
DR DIP; DIP-3954N; -.
DR IntAct; P38211; 3.
DR MINT; P38211; -.
DR STRING; 4932.YBR004C; -.
DR CAZy; GT76; Glycosyltransferase Family 76.
DR MaxQB; P38211; -.
DR PaxDb; P38211; -.
DR PRIDE; P38211; -.
DR EnsemblFungi; YBR004C_mRNA; YBR004C; YBR004C.
DR GeneID; 852289; -.
DR KEGG; sce:YBR004C; -.
DR SGD; S000000208; GPI18.
DR VEuPathDB; FungiDB:YBR004C; -.
DR eggNOG; KOG2647; Eukaryota.
DR GeneTree; ENSGT00390000013174; -.
DR HOGENOM; CLU_029048_0_0_1; -.
DR InParanoid; P38211; -.
DR OMA; RWDSIYY; -.
DR BioCyc; YEAST:G3O-28992-MON; -.
DR Reactome; R-SCE-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR PRO; PR:P38211; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38211; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0120097; C:glycosylphosphatidylinositol-mannosyltransferase II complex; IPI:ComplexPortal.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0031501; C:mannosyltransferase complex; IGI:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IMP:SGD.
DR GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0000030; F:mannosyltransferase activity; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IC:ComplexPortal.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR GO; GO:0035268; P:protein mannosylation; IC:ComplexPortal.
DR InterPro; IPR007315; PIG-V/Gpi18.
DR PANTHER; PTHR12468; PTHR12468; 1.
DR Pfam; PF04188; Mannosyl_trans2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..433
FT /note="GPI mannosyltransferase 2"
FT /id="PRO_0000014309"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..109
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..215
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..318
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..409
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 187
FT /note="S -> T (in Ref. 1; CAA84940/CAA84942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 50759 MW; 9C81918DF1A37B44 CRC64;
MIVGLTLYFV LFRSIQYLLV FLTPIRQFDT STSLLLNELC SSPSEINSYW NKYFWNKLLS
WDSVFFIKNI TSKNGKPQFE HEYAFSQLWT FFVRLFIKSN NDSIYHALRV GVAIENVLFY
LSGIVLYFLT KKIFSQNIRQ SQFARTIAKK TSLLFFLTSA AGFLTSIYSE PLSFFFAFVG
IWSRECSISV PVLGQFDISW RYWFPYSFIS MACFTLASLN RSNCVLLGIY FIFDLIELTK
NRKFVKAICF PLLSGSLMFS ALLYQQYYLP YKTFCPQRGE WCKSQLFSSI FITKTSLYSY
IQSHYWGVGL LKYWTPNNIP NFLFAVPNII ILIYSSIYFS KIYPSYNLKA LVWITRALVV
IVCFFAHVQI LNRIASFLPL HLWYLADRLV KTSDPKKMEN PKGDDKIVKF YIYWLAFWIP
LQTILFAAFL PPA
