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GPI12_YEAST
ID   GPI12_YEAST             Reviewed;         304 AA.
AC   P23797; D6W0A8;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase;
DE            EC=3.5.1.89 {ECO:0000269|PubMed:10085243};
GN   Name=GPI12; OrderedLocusNames=YMR281W; ORFNames=YM8021.07;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10085243; DOI=10.1042/bj3390185;
RA   Watanabe R., Ohishi K., Maeda Y., Nakamura N., Kinoshita T.;
RT   "Mammalian PIG-L and its yeast homologue Gpi12p are N-
RT   acetylglucosaminylphosphatidylinositol de-N-acetylases essential in
RT   glycosylphosphatidylinositol biosynthesis.";
RL   Biochem. J. 339:185-192(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1718609; DOI=10.1007/bf00312765;
RA   Payne M.J., Finnegan P.M., Keramidaris E., Lukins H.B.;
RT   "Characterization of a yeast nuclear gene, AEP2, required for accumulation
RT   of mitochondrial mRNA encoding subunit 9 of the ATP synthase.";
RL   Curr. Genet. 20:53-61(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [4]
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   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=26928762; DOI=10.1038/nmeth.3795;
RA   Yofe I., Weill U., Meurer M., Chuartzman S., Zalckvar E., Goldman O.,
RA   Ben-Dor S., Schuetze C., Wiedemann N., Knop M., Khmelinskii A.,
RA   Schuldiner M.;
RT   "One library to make them all: streamlining the creation of yeast libraries
RT   via a SWAp-Tag strategy.";
RL   Nat. Methods 13:371-378(2016).
CC   -!- FUNCTION: Involved in the second step of GPI biosynthesis. De-N-
CC       acetylation of N-acetylglucosaminyl-phosphatidylinositol.
CC       {ECO:0000269|PubMed:10085243}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-
CC         inositol + H2O = acetate + an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-
CC         glycero-3-phospho)-1D-myo-inositol; Xref=Rhea:RHEA:11660,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:57265,
CC         ChEBI:CHEBI:57997; EC=3.5.1.89;
CC         Evidence={ECO:0000269|PubMed:10085243};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11661;
CC         Evidence={ECO:0000305|PubMed:10085243};
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000305|PubMed:10085243}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:26928762}.
CC   -!- SIMILARITY: Belongs to the PIGL family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=M59860; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB017166; BAA74776.1; -; Genomic_DNA.
DR   EMBL; M59860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z49704; CAA89779.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10182.1; -; Genomic_DNA.
DR   PIR; S54588; S54588.
DR   RefSeq; NP_014008.1; NM_001182788.1.
DR   AlphaFoldDB; P23797; -.
DR   SMR; P23797; -.
DR   BioGRID; 35460; 372.
DR   IntAct; P23797; 1.
DR   STRING; 4932.YMR281W; -.
DR   iPTMnet; P23797; -.
DR   MaxQB; P23797; -.
DR   PaxDb; P23797; -.
DR   PRIDE; P23797; -.
DR   EnsemblFungi; YMR281W_mRNA; YMR281W; YMR281W.
DR   GeneID; 855324; -.
DR   KEGG; sce:YMR281W; -.
DR   SGD; S000004894; GPI12.
DR   VEuPathDB; FungiDB:YMR281W; -.
DR   eggNOG; KOG3332; Eukaryota.
DR   GeneTree; ENSGT00390000018434; -.
DR   HOGENOM; CLU_034979_0_0_1; -.
DR   InParanoid; P23797; -.
DR   OMA; RWGWITI; -.
DR   BioCyc; YEAST:YMR281W-MON; -.
DR   Reactome; R-SCE-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR   UniPathway; UPA00196; -.
DR   PRO; PR:P23797; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P23797; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR   GO; GO:0000225; F:N-acetylglucosaminylphosphatidylinositol deacetylase activity; IDA:SGD.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; ISS:SGD.
DR   Gene3D; 3.40.50.10320; -; 1.
DR   InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR   InterPro; IPR039516; GPI12.
DR   InterPro; IPR024078; LmbE-like_dom_sf.
DR   PANTHER; PTHR12993; PTHR12993; 1.
DR   PANTHER; PTHR12993:SF11; PTHR12993:SF11; 1.
DR   Pfam; PF02585; PIG-L; 1.
DR   SUPFAM; SSF102588; SSF102588; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; GPI-anchor biosynthesis; Hydrolase; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..304
FT                   /note="N-acetylglucosaminyl-phosphatidylinositol de-N-
FT                   acetylase"
FT                   /id="PRO_0000207170"
FT   TOPO_DOM        1..20
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        21..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39..304
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   304 AA;  35446 MW;  7A3B7A16D7B72DD7 CRC64;
     MKMLRRTKVN FSKLLYKITK LAIVLTILYI YFTPKIVSRN NASLQHIFPH KYGDYEINLV
     IAHPDDEVMF FSPIISQLNS YFPRTVPFNI ICLSKGNAEG LGETRVRELN ESAALLLHNE
     RAVSVQVMDF QDGMDEIWDI DSITSSLSQK IDIKNHNLNQ IIVTFDSYGV SNHINHKSCY
     AAVKKLVDDY AQPKTKRNEQ PPHVTALYLR SYKNNIVLKY NSFIWEILKI LYDLISPFRR
     IIQALPPNTA AEKDKLSLMN THAQYVLAFA TMLNAHESQV VWFRYGWWIF SRFVFVNEFD
     VYTY
 
 
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