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GPI15_YEAST
ID   GPI15_YEAST             Reviewed;         229 AA.
AC   P53961; D6W1E1; Q6B1G8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15;
DE            Short=GPI-GlcNAc transferase complex subunit GPI5;
DE            Short=GPI-GnT subunit GPI5;
DE            EC=2.4.1.198;
DE   AltName: Full=PIGH homolog;
GN   Name=GPI15; OrderedLocusNames=YNL038W; ORFNames=N2687;
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=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-197.
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   [4]
RP   FUNCTION.
RX   PubMed=11746600; DOI=10.1002/yea.783;
RA   Yan B.C., Westfall B.A., Orlean P.;
RT   "Ynl038wp (Gpi15p) is the Saccharomyces cerevisiae homologue of human Pig-
RT   Hp and participates in the first step in glycosylphosphatidylinositol
RT   assembly.";
RL   Yeast 18:1383-1389(2001).
RN   [5]
RP   REVISION OF GENE MODEL.
RX   PubMed=12775844; DOI=10.1126/science.1084337;
RA   Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA   Waterston R., Cohen B.A., Johnston M.;
RT   "Finding functional features in Saccharomyces genomes by phylogenetic
RT   footprinting.";
RL   Science 301:71-76(2003).
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. {ECO:0000269|PubMed:11746600}.
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.
CC       {ECO:0000305|PubMed:11746600}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PIGH family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT93131.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAA95905.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; Z71314; CAA95905.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY693112; AAT93131.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BK006947; DAA10507.1; -; Genomic_DNA.
DR   PIR; S62960; S62960.
DR   RefSeq; NP_014360.2; NM_001182877.1.
DR   AlphaFoldDB; P53961; -.
DR   BioGRID; 35786; 276.
DR   ComplexPortal; CPX-1274; Glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex.
DR   DIP; DIP-6356N; -.
DR   IntAct; P53961; 1.
DR   STRING; 4932.YNL038W; -.
DR   MaxQB; P53961; -.
DR   PaxDb; P53961; -.
DR   PRIDE; P53961; -.
DR   EnsemblFungi; YNL038W_mRNA; YNL038W; YNL038W.
DR   GeneID; 855690; -.
DR   KEGG; sce:YNL038W; -.
DR   SGD; S000004983; GPI15.
DR   VEuPathDB; FungiDB:YNL038W; -.
DR   eggNOG; ENOG502S6Z2; Eukaryota.
DR   HOGENOM; CLU_106408_0_0_1; -.
DR   InParanoid; P53961; -.
DR   OMA; NASAFWI; -.
DR   BioCyc; YEAST:G3O-33074-MON; -.
DR   UniPathway; UPA00196; -.
DR   PRO; PR:P53961; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53961; protein.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR   GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; ISA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; ISM: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; IPR019328; GPI-GlcNAc_Trfase_PIG-H_dom.
DR   InterPro; IPR044215; PIG-H.
DR   PANTHER; PTHR15231; PTHR15231; 1.
DR   Pfam; PF10181; PIG-H; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; GPI-anchor biosynthesis; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..229
FT                   /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT                   subunit GPI15"
FT                   /id="PRO_0000087556"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        10
FT                   /note="K -> E (in Ref. 3; AAT93131)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   229 AA;  26817 MW;  E89CB192B65FBF06 CRC64;
     MISKEYEFGK TSILNRKKYT LVIDEDKNGN FIRFTVLPVS NRKFKKVKQN GRVEINMGIQ
     YHQIVLILLL NILFYVICLR SRFLEHINRT FEVTIARSFQ ILIIMGLFAL GTIILVRGPS
     VETVTIFKES GLQLSRVKGM VIFPQQWNRK FFEQVEFISN ERIIDVVINE GFCRGFRVIF
     YLAAIVRKSS TLKLLFPSNL PSIDDQRLIY NISRKYLSKQ EKPLSRPKD
 
 
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