GPI19_YEAST
ID GPI19_YEAST Reviewed; 140 AA.
AC Q04082; D6VT64;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI19;
DE Short=GPI-GlcNAc transferase complex subunit GPI19;
DE Short=GPI-GnT subunit GPI19;
DE EC=2.4.1.198;
GN Name=GPI19; OrderedLocusNames=YDR437W; ORFNames=D9461.23;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 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 [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION, TOPOLOGY, INTERACTION WITH GPI2, AND IDENTIFICATION IN THE
RP GPI-GLCNAC TRANSFERASE COMPLEX.
RX PubMed=16278447; DOI=10.1128/ec.4.11.1801-1807.2005;
RA Newman H.A., Romeo M.J., Lewis S.E., Yan B.C., Orlean P., Levin D.E.;
RT "Gpi19, the Saccharomyces cerevisiae homologue of mammalian PIG-P, is a
RT subunit of the initial enzyme for glycosylphosphatidylinositol anchor
RT biosynthesis.";
RL Eukaryot. Cell 4:1801-1807(2005).
CC -!- FUNCTION: Part of the complex catalyzing the transfer of N-
CC acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol,
CC the first step of GPI biosynthesis. Involved in cell wall biosynthesis.
CC {ECO:0000269|PubMed:16278447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + UDP-N-
CC acetyl-alpha-D-glucosamine = a 6-(N-acetyl-alpha-D-glucosaminyl)-1-
CC phosphatidyl-1D-myo-inositol + H(+) + UDP; Xref=Rhea:RHEA:14789,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57265, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58223; EC=2.4.1.198;
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Component of the phosphatidylinositol N-
CC acetylglucosaminyltransferase (GPI-GlcNAc transferase) complex composed
CC of at least GPI1, GPI2, GPI3, GPI15, GPI19 and ERI1 (Probable).
CC Interacts with GPI2 (PubMed:16278447). {ECO:0000269|PubMed:16278447,
CC ECO:0000305|PubMed:16278447}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GPI19 family. {ECO:0000305}.
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DR EMBL; U33007; AAB64854.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12274.1; -; Genomic_DNA.
DR PIR; S69717; S69717.
DR RefSeq; NP_010725.3; NM_001180745.3.
DR AlphaFoldDB; Q04082; -.
DR BioGRID; 32493; 701.
DR ComplexPortal; CPX-1274; Glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex.
DR IntAct; Q04082; 12.
DR STRING; 4932.YDR437W; -.
DR PaxDb; Q04082; -.
DR EnsemblFungi; YDR437W_mRNA; YDR437W; YDR437W.
DR GeneID; 852047; -.
DR KEGG; sce:YDR437W; -.
DR SGD; S000002845; GPI19.
DR VEuPathDB; FungiDB:YDR437W; -.
DR eggNOG; KOG2257; Eukaryota.
DR HOGENOM; CLU_081616_4_0_1; -.
DR InParanoid; Q04082; -.
DR OMA; RYWIICI; -.
DR BioCyc; YEAST:G3O-29971-MON; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:Q04082; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04082; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IPI:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; HDA:SGD.
DR GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031505; P:fungal-type cell wall organization; IC:ComplexPortal.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR InterPro; IPR013717; PIG-P.
DR InterPro; IPR016542; PIG-P_GPI19.
DR Pfam; PF08510; PIG-P; 1.
DR PIRSF; PIRSF008765; PIG-P_GPI19; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..140
FT /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT subunit GPI19"
FT /id="PRO_0000240380"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16278447"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..52
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16278447"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16278447"
SQ SEQUENCE 140 AA; 16090 MW; EFA63AAB82665B79 CRC64;
MYTKEYYWFS QYMIITSTLV LTIIWSILPS SLGEAAPKQF INTLLDIFPQ RRWIITLESI
MLMGMLCTYI GLLMYNEDTL TPPLDSLSTV TDAGGQLVIE DDPDVFVKKW AFKETSGIYD
LSLMDACQLL YLYDNDHTST
