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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
 
 
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