ID   GPI12_ARTBC             Reviewed;         335 AA.
AC   D4B4K9;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase {ECO:0000250|UniProtKB:P23797};
DE            EC=3.5.1.89 {ECO:0000250|UniProtKB:P23797};
GN   ORFNames=ARB_03399;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- FUNCTION: Involved in the second step of GPI biosynthesis. De-N-
CC       acetylation of N-acetylglucosaminyl-phosphatidylinositol (By
CC       similarity). {ECO:0000250|UniProtKB:P23797}.
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:0000250|UniProtKB:P23797};
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000250|UniProtKB:P23797}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass type II membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PIGL family. {ECO:0000305}.
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DR   EMBL; ABSU01000034; EFE30057.1; -; Genomic_DNA.
DR   RefSeq; XP_003010697.1; XM_003010651.1.
DR   AlphaFoldDB; D4B4K9; -.
DR   STRING; 663331.D4B4K9; -.
DR   EnsemblFungi; EFE30057; EFE30057; ARB_03399.
DR   GeneID; 9524810; -.
DR   KEGG; abe:ARB_03399; -.
DR   eggNOG; KOG3332; Eukaryota.
DR   HOGENOM; CLU_034979_0_0_1; -.
DR   OMA; RWGWITI; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
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:0000225; F:N-acetylglucosaminylphosphatidylinositol deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Hydrolase;
KW   Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..335
FT                   /note="N-acetylglucosaminyl-phosphatidylinositol de-N-
FT                   acetylase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434500"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   335 AA;  36646 MW;  8199C663C110FD53 CRC64;
     MNSAFTFLSL AIFPLALFIF WTLSATGPSS PLGRGFPTLT NKRICLLIAH PDDEAMFFAP
     TLLALTKPEL GNHVKILCLS SGMCALLMVL DSASGWFLIY QITGDAAGLG HIRKQELQKS
     ALRLGLRNES DVFIVDDPSR FPDSMTATWS EENVSGLLAS AFAPQLAAQA SSQSAPMATI
     DILLTFDQSG VSYHPNHRSL YHGARAFLKA LMRGNSGHPC PVTLYTLTST TLARKYIGVF
     DAPIAMLSGV ISNAFGGSGD RDALSTSPSK KTQELRGIRE PPPANRLLFV NSVDDWLSGW
     KAMVYAHKSQ MVWFRWGWIT VGRYMVVNDL KKELV