ID   PIGL_BOVIN              Reviewed;         253 AA.
AC   A6QQ24;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the second step of GPI biosynthesis. De-N-
CC       acetylation of N-acetylglucosaminyl-phosphatidylinositol (By
CC       similarity). {ECO:0000250}.
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; BC149604; AAI49605.1; -; mRNA.
DR   RefSeq; NP_001093781.1; NM_001100311.2.
DR   AlphaFoldDB; A6QQ24; -.
DR   SMR; A6QQ24; -.
DR   STRING; 9913.ENSBTAP00000017653; -.
DR   PaxDb; A6QQ24; -.
DR   PRIDE; A6QQ24; -.
DR   Ensembl; ENSBTAT00000017653; ENSBTAP00000017653; ENSBTAG00000013273.
DR   GeneID; 507080; -.
DR   KEGG; bta:507080; -.
DR   CTD; 9487; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013273; -.
DR   VGNC; VGNC:32871; PIGL.
DR   eggNOG; KOG3332; Eukaryota.
DR   GeneTree; ENSGT00390000018434; -.
DR   HOGENOM; CLU_034979_1_0_1; -.
DR   InParanoid; A6QQ24; -.
DR   OMA; RWGWITI; -.
DR   OrthoDB; 1454301at2759; -.
DR   TreeFam; TF315150; -.
DR   Reactome; R-BTA-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000013273; Expressed in digestive system secreted substance and 109 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
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..253
FT                   /note="N-acetylglucosaminyl-phosphatidylinositol de-N-
FT                   acetylase"
FT                   /id="PRO_0000328581"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..253
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   253 AA;  28330 MW;  BBE22F6718654E8F CRC64;
     MEVAAPLLCL AAAVLVWGVL WVWGSWERMT RPEQAGLPGG GSRTLLVTAH PDDEAMFFAP
     TILGLARLRH QLFLLCFSAG NYYNQGEIRK KELLQSCDVL GIPPSNVMII ENRDFPDDPD
     VRWDPDRAAD VLLQHVEANG IKLVVTFDEG GVSGHSNHVA LNAAVRTLQA EGKLPKGCSV
     LTLQSVNLLR KYLCLLDLPC SLLLARDALF VLTQREAAQA QRAMSCHRSQ LLWFRRLYML
     FSRYMRINSL NFL