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GPI10_YEAST
ID   GPI10_YEAST             Reviewed;         616 AA.
AC   P30777; D6VU07;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=GPI mannosyltransferase 3;
DE            EC=2.4.1.-;
DE   AltName: Full=GPI mannosyltransferase III;
DE            Short=GPI-MT-III;
DE   AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 10;
GN   Name=GPI10; OrderedLocusNames=YGL142C;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=9046099;
RX   DOI=10.1002/(sici)1097-0061(199702)13:2<177::aid-yea62>3.0.co;2-2;
RA   Voet M., Defoor E., Verhasselt P., Riles L., Robben J., Volckaert G.;
RT   "The sequence of a nearly unclonable 22.8 kb segment on the left arm
RT   chromosome VII from Saccharomyces cerevisiae reveals ARO2, RPL9A, TIP1,
RT   MRF1 genes and six new open reading frames.";
RL   Yeast 13:177-182(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 339-616.
RX   PubMed=1475194; DOI=10.1093/nar/20.23.6339;
RA   Pel H.J., Maat M.J., Rep M., Grivell L.A.;
RT   "The yeast nuclear gene MRF1 encodes a mitochondrial peptide chain release
RT   factor and cures several mitochondrial RNA splicing defects.";
RL   Nucleic Acids Res. 20:6339-6346(1992).
RN   [5]
RP   FUNCTION.
RX   PubMed=9576863; DOI=10.1042/bj3320153;
RA   Suetterlin C., Escribano M.V., Gerold P., Maeda Y., Mazon M.J.,
RA   Kinoshita T., Schwarz R.T., Riezman H.;
RT   "Saccharomyces cerevisiae GPI10, the functional homologue of human PIG-B,
RT   is required for glycosylphosphatidylinositol-anchor synthesis.";
RL   Biochem. J. 332:153-159(1998).
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF ALA-48.
RX   PubMed=9639537; DOI=10.1093/glycob/8.8.761;
RA   Canivenc-Gansel E., Imhof I., Reggiori F., Burda P., Conzelmann A.,
RA   Benachour A.;
RT   "GPI anchor biosynthesis in yeast: phosphoethanolamine is attached to the
RT   alpha1,4-linked mannose of the complete precursor glycophospholipid.";
RL   Glycobiology 8:761-770(1998).
RN   [7]
RP   FUNCTION.
RX   PubMed=11159918; DOI=10.1093/glycob/10.12.1271;
RA   Imhof I., Canivenc-Gansel E., Meyer U., Conzelmann A.;
RT   "Phosphatidylethanolamine is the donor of the phosphorylethanolamine linked
RT   to the alpha1,4-linked mannose of yeast GPI structures.";
RL   Glycobiology 10:1271-1275(2000).
RN   [8]
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 third mannose to Man2-GlcN-acyl-PI
CC       during GPI precursor assembly. {ECO:0000269|PubMed:11159918,
CC       ECO:0000269|PubMed:9576863, ECO:0000269|PubMed:9639537}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X99960; CAA68220.1; -; Genomic_DNA.
DR   EMBL; Z72664; CAA96854.1; -; Genomic_DNA.
DR   EMBL; X60381; CAA42931.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07968.1; -; Genomic_DNA.
DR   PIR; S64156; S64156.
DR   RefSeq; NP_011373.1; NM_001181007.1.
DR   AlphaFoldDB; P30777; -.
DR   BioGRID; 33110; 449.
DR   DIP; DIP-6707N; -.
DR   IntAct; P30777; 2.
DR   STRING; 4932.YGL142C; -.
DR   CAZy; GT22; Glycosyltransferase Family 22.
DR   MaxQB; P30777; -.
DR   PaxDb; P30777; -.
DR   PRIDE; P30777; -.
DR   EnsemblFungi; YGL142C_mRNA; YGL142C; YGL142C.
DR   GeneID; 852735; -.
DR   KEGG; sce:YGL142C; -.
DR   SGD; S000003110; GPI10.
DR   VEuPathDB; FungiDB:YGL142C; -.
DR   eggNOG; KOG1771; Eukaryota.
DR   GeneTree; ENSGT00950000183090; -.
DR   HOGENOM; CLU_012353_2_0_1; -.
DR   InParanoid; P30777; -.
DR   OMA; HEWPDYL; -.
DR   BioCyc; YEAST:YGL142C-MON; -.
DR   Reactome; R-SCE-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR   UniPathway; UPA00196; -.
DR   PRO; PR:P30777; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P30777; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS: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:0000026; F:alpha-1,2-mannosyltransferase activity; IMP:SGD.
DR   GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR   InterPro; IPR005599; GPI_mannosylTrfase.
DR   InterPro; IPR039521; PIG-B/GPI10.
DR   PANTHER; PTHR22760; PTHR22760; 1.
DR   PANTHER; PTHR22760:SF4; PTHR22760:SF4; 1.
DR   Pfam; PF03901; Glyco_transf_22; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..616
FT                   /note="GPI mannosyltransferase 3"
FT                   /id="PRO_0000202736"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..86
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..188
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..240
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..278
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        300..338
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        360..392
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        414..423
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        424..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        445..616
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         48
FT                   /note="A->T: In gpi10-1; accumulate M2, an abnormal GPI-
FT                   anchor intermediate due to the absence of third mannose."
FT                   /evidence="ECO:0000269|PubMed:9639537"
FT   CONFLICT        339
FT                   /note="S -> A (in Ref. 4; CAA42931)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   616 AA;  72566 MW;  141ABF6A01B008ED CRC64;
     MAHEVHRIKP KLGRTQIFWV FLAFRVLNAV LTRTFFQADE FWQALEPAHW KAFKYGELTW
     EWKFGVRSYL FPMIFELTYR LVSLSSILLH YALLLLSTIG SDLLILLLPK YELSWQVAED
     LKRLPFDVTR SFEYYGVIYA PKIVMAVLAS IGEYYIVRFV QKLYLLTLDK RNEKEEEERR
     SGLSEITKFA LLLSLTNFFN CFFITRTFIN SFEMILTSIA LYYWDWTGGQ MIKESSFTKS
     LIFAFLACLQ RPSSGLIWVI PSISLILNLV GKKQYHLLFI TFSKVLRSFF LVFTANAIID
     MYFYEKVTFP FFRFLKFNFT TPLSKFYGVA PWHFHFFQSL PIVLGASIPA FAFGLFFPLS
     KRSFPKKYLN PFFQVKLTIL LNLLVYSTLP HKEFRFIFPL QPLFILISSF GLLRLDRDYW
     KRLSGLKSLL WLVPFVSVFI ALLLDTFHES GSIEVMKFLH EEPEIDSLGF IMPCHSTPGQ
     SYLHRSDIQD LWSITCNPPL HLLGDPEAYS KLETYMDESD HLYDDISAFI YKNFPPPFRK
     DLRSPGKTYS HEWPTYLVVF EHMENAFLKD FLKDSSYIEY NRFFNSLAHW DSRRSGDIII
     YYKLPFDYSD IPAADI
 
 
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