GPI13_YEAST
ID GPI13_YEAST Reviewed; 1017 AA.
AC Q07830; D6VXX4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=GPI ethanolamine phosphate transferase 3;
DE EC=2.-.-.-;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 13;
GN Name=GPI13; Synonyms=MPC1; OrderedLocusNames=YLL031C;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 FUNCTION.
RX PubMed=10487931;
RX DOI=10.1002/(sici)1097-0061(19990915)15:12<1287::aid-yea458>3.0.co;2-s;
RA Zhang N., Ismail T., Wu J., Woodwark K.C., Gardner D.C.J., Walmsley R.M.,
RA Oliver S.G.;
RT "Disruption of six novel ORFs on the left arm of chromosome XII reveals one
RT gene essential for vegetative growth of Saccharomyces cerevisiae.";
RL Yeast 15:1287-1296(1999).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=10823837; DOI=10.1074/jbc.m003844200;
RA Flury I., Benachour A., Conzelmann A.;
RT "YLL031c belongs to a novel family of membrane proteins involved in the
RT transfer of ethanolaminephosphate onto the core structure of
RT glycosylphosphatidylinositol anchors in yeast.";
RL J. Biol. Chem. 275:24458-24465(2000).
RN [5]
RP FUNCTION.
RX PubMed=10793139; DOI=10.1091/mbc.11.5.1611;
RA Taron C.H., Wiedman J.M., Grimme S.J., Orlean P.;
RT "Glycosylphosphatidylinositol biosynthesis defects in Gpi11p- and Gpi13p-
RT deficient yeast suggest a branched pathway and implicate gpi13p in
RT phosphoethanolamine transfer to the third mannose.";
RL Mol. Biol. Cell 11:1611-1630(2000).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF HIS-198; LEU-231; ILE-367; ASN-411; SER-556;
RP ASP-887 AND THR-901.
RX PubMed=12441642; DOI=10.1266/ggs.77.309;
RA Toh-e A., Oguchi T.;
RT "Genetic characterization of genes encoding enzymes catalyzing addition of
RT phospho-ethanolamine to the glycosylphosphatidylinositol anchor in
RT Saccharomyces cerevisiae.";
RL Genes Genet. Syst. 77:309-322(2002).
RN [7]
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 [8]
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).
CC -!- FUNCTION: Involved in glycosylphosphatidylinositol-anchor biosynthesis.
CC Transfers ethanolamine phosphate to the GPI third mannose which links
CC the GPI-anchor to the C-terminus of the proteins by an amide bond.
CC Involved in cell wall biosynthesis. {ECO:0000269|PubMed:10487931,
CC ECO:0000269|PubMed:10793139, ECO:0000269|PubMed:10823837,
CC ECO:0000269|PubMed:12441642}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:10823837}.
CC -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily.
CC {ECO:0000305}.
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DR EMBL; Z73136; CAA97480.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09290.1; -; Genomic_DNA.
DR PIR; S64782; S64782.
DR RefSeq; NP_013069.1; NM_001181851.1.
DR AlphaFoldDB; Q07830; -.
DR SMR; Q07830; -.
DR BioGRID; 31222; 597.
DR DIP; DIP-5569N; -.
DR IntAct; Q07830; 2.
DR MINT; Q07830; -.
DR STRING; 4932.YLL031C; -.
DR MaxQB; Q07830; -.
DR PaxDb; Q07830; -.
DR PRIDE; Q07830; -.
DR EnsemblFungi; YLL031C_mRNA; YLL031C; YLL031C.
DR GeneID; 850628; -.
DR KEGG; sce:YLL031C; -.
DR SGD; S000003954; GPI13.
DR VEuPathDB; FungiDB:YLL031C; -.
DR eggNOG; KOG2126; Eukaryota.
DR GeneTree; ENSGT00910000144278; -.
DR HOGENOM; CLU_004298_1_0_1; -.
DR InParanoid; Q07830; -.
DR OMA; LGDSTWT; -.
DR BioCyc; YEAST:G3O-32134-MON; -.
DR BRENDA; 2.7.7.B26; 984.
DR UniPathway; UPA00196; -.
DR PRO; PR:Q07830; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07830; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IMP:SGD.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IMP:SGD.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR CDD; cd16023; GPI_EPT_3; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037675; PIG-O_N.
DR InterPro; IPR039524; PIGO/GPI13.
DR PANTHER; PTHR23071; PTHR23071; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1017
FT /note="GPI ethanolamine phosphate transferase 3"
FT /id="PRO_0000240363"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 685..705
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 765..785
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 806..826
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 829..849
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 903..923
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 947..967
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 981..1001
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 682
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 742
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 198
FT /note="H->R: In MCP1-5; impairs growth at 36 degrees
FT Celsius; when associated with S-231 and T-411."
FT /evidence="ECO:0000269|PubMed:12441642"
FT MUTAGEN 231
FT /note="L->S: In MCP1-5; impairs growth at 36 degrees
FT Celsius; when associated with R-198 and T-411."
FT /evidence="ECO:0000269|PubMed:12441642"
FT MUTAGEN 367
FT /note="I->T: In MCP1-4; impairs growth at 36 degrees
FT Celsius; when associated with P-556; G-887 and A-901."
FT /evidence="ECO:0000269|PubMed:12441642"
FT MUTAGEN 411
FT /note="N->T: In MCP1-5; impairs growth at 36 degrees
FT Celsius; when associated with R-198 and S-231."
FT /evidence="ECO:0000269|PubMed:12441642"
FT MUTAGEN 556
FT /note="S->P: In MCP1-4; impairs growth at 36 degrees
FT Celsius; when associated with T-367; G-887 and A-901."
FT /evidence="ECO:0000269|PubMed:12441642"
FT MUTAGEN 887
FT /note="D->G: In MCP1-4; impairs growth at 36 degrees
FT Celsius; when associated with T-367; P-556 and A-901."
FT /evidence="ECO:0000269|PubMed:12441642"
FT MUTAGEN 901
FT /note="T->A: In MCP1-4; impairs growth at 36 degrees
FT Celsius; when associated with T-367; P-556 and G-887."
FT /evidence="ECO:0000269|PubMed:12441642"
SQ SEQUENCE 1017 AA; 115634 MW; 5006E7E43E1538F6 CRC64;
MDEKTIKKSI LSSSNDEKII YKSRIKKFQK NHKFYIILLV FIAILQFISI AFFTRGFLLS
RHVLDNISSQ NETSKLPPRF NKAVILVIDA LRFDFAIPVN ESHSNYNLNY HNNILSLYDS
FASDKDASSL LLKFIADPPT TTLQRLKGLT TGSLPTFIDA GSNFDGTVIE EDNFLKQLHL
ANKTVKFAGD DTWMALFHPF LSNDSFPLES LNVWDLDTVD NGVMDYFHDH LQQDKEWDVM
IGHMLGIDHV GHKYGPDHFT MREKQIQVDQ FIDWILKSID DDTLLVILGD HGMDHTGNHG
GDSIDELEST LFLYSKKPDM WRLKETSNYN IDNLGHDYRS VRQIDLVSSL ALLMGQPIPF
NNLGWPIDEI ARNDREWSQF VNSAISQLQL YKDTMQIHHG NDEILEPLAK NISNTPPTSD
PEKFVKLGHK YQKVFLQTCE ELWAKFDYYS IATGITLLAT SLVLLISITK LIPSIVVNQM
VPEFVPGIII MVLVTNLCFH GIFYVYQQPS FVDQFWGTLL ATAIGIIIGC YITIFDRYNF
IWIAMRLGET LADYWSRIAV MFMIIHALLF TSNSFTIWED RIVAFLLSTF GMLTLYEFVF
LPKRQSTTAL LTATISEKEG TTSGVNPSTA NSNYLPLTRF ARLLGGYHSA VLIIFTRLAS
MITICREEQG EYCIPTFNNQ NNSSWWVLGL CFLMIFILPA CITGYYNLTS SYQAAAPIWI
NVFLKGILGL NFVYWSLTSL ENNSAVIAIP FLRDVTIFKF TLARIIAGFS LIASNVGWLM
GPLCIKLNIH NTDVKSHEAT ILGYTNIYGS EFFLLVINVL ISILLFNKPL AQLSYFLMCN
QLLSILEIID LLKLKENIIG PIALGLLSYQ HFFTTGHQAT IPSVQWDIGF MLSEKVTFPF
TQIAIILNTF GPHILVSLSV ALLTLWSQPP DVLKPQTLLG RIVSNCGILL TYNTILCLSS
FIWVTHFRRH LMVWKIFCPR FIFASLSLIV TQLVVTFGTI AFASGRLIKH INDIFWK
