ID   PIGL_RAT                Reviewed;         252 AA.
AC   O35790;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase;
DE            EC=3.5.1.89;
DE   AltName: Full=Phosphatidylinositol-glycan biosynthesis class L protein;
DE            Short=PIG-L;
GN   Name=Pigl;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Glial tumor;
RX   PubMed=9188481; DOI=10.1074/jbc.272.25.15834;
RA   Nakamura N., Inoue N., Watanabe R., Takahashi M., Takeda J., Stevens V.L.,
RA   Kinoshita T.;
RT   "Expression cloning of PIG-L, a candidate N-acetylglucosaminyl-
RT   phosphatidylinositol deacetylase.";
RL   J. Biol. Chem. 272:15834-15840(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION.
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).
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   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PIGL family. {ECO:0000305}.
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DR   EMBL; D88364; BAA20869.1; -; mRNA.
DR   EMBL; BC074020; AAH74020.1; -; mRNA.
DR   RefSeq; NP_620256.1; NM_138901.2.
DR   AlphaFoldDB; O35790; -.
DR   SMR; O35790; -.
DR   STRING; 10116.ENSRNOP00000004113; -.
DR   SwissLipids; SLP:000001963; -.
DR   PaxDb; O35790; -.
DR   Ensembl; ENSRNOT00000004113; ENSRNOP00000004113; ENSRNOG00000003070.
DR   GeneID; 192263; -.
DR   KEGG; rno:192263; -.
DR   UCSC; RGD:620437; rat.
DR   CTD; 9487; -.
DR   RGD; 620437; Pigl.
DR   eggNOG; KOG3332; Eukaryota.
DR   GeneTree; ENSGT00390000018434; -.
DR   HOGENOM; CLU_034979_1_0_1; -.
DR   InParanoid; O35790; -.
DR   OMA; RWGWITI; -.
DR   OrthoDB; 1454301at2759; -.
DR   PhylomeDB; O35790; -.
DR   TreeFam; TF315150; -.
DR   BRENDA; 3.5.1.89; 5301.
DR   Reactome; R-RNO-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR   UniPathway; UPA00196; -.
DR   PRO; PR:O35790; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000003070; Expressed in pancreas and 20 other tissues.
DR   Genevisible; O35790; RN.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
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; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IDA:RGD.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; GPI-anchor biosynthesis; Hydrolase;
KW   Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..252
FT                   /note="N-acetylglucosaminyl-phosphatidylinositol de-N-
FT                   acetylase"
FT                   /id="PRO_0000207168"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        23..252
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   252 AA;  27984 MW;  73AD9AA7A79DBFCB CRC64;
     MEVVGLLCVA VAVLTWGFLR VWNSAERMRS PEQAGLPGAG SRALVVIAHP DDEAMFFAPT
     ILGLARLKQQ VSLLCFSSGN YYNQGEIRKK ELLQSCAVLG IPPSRVMIID KREFPDDPEV
     QWDTEHVAST ILQHIHANAT DLVVTFDAEG VSGHSNHIAL YKAVRALHSG GKLPEGCSVL
     TLQSVNVLRK YVFLLDLPWT LLSPQGVLFV LTSKEVAQAK KAMSCHRSQL LWFRHLYTVF
     SRYMSVNSLQ LL