ID J8LPY0_SACAR Unreviewed; 302 AA.
AC J8LPY0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE RecName: Full=N-acetylglucosaminylphosphatidylinositol deacetylase {ECO:0000256|ARBA:ARBA00012176};
DE EC=3.5.1.89 {ECO:0000256|ARBA:ARBA00012176};
GN ORFNames=SU7_0761 {ECO:0000313|EMBL:EJS44137.1};
OS Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS44137.1, ECO:0000313|Proteomes:UP000006968};
RN [1] {ECO:0000313|EMBL:EJS44137.1, ECO:0000313|Proteomes:UP000006968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H-6 / AS 2.3317 / CBS 10644
RC {ECO:0000313|Proteomes:UP000006968};
RX PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT "High quality de novo sequencing and assembly of the Saccharomyces
RT arboricolus genome.";
RL BMC Genomics 14:69-69(2013).
CC -!- FUNCTION: Involved in the second step of GPI biosynthesis. De-N-
CC acetylation of N-acetylglucosaminyl-phosphatidylinositol.
CC {ECO:0000256|ARBA:ARBA00024639}.
CC -!- SIMILARITY: Belongs to the PIGL family.
CC {ECO:0000256|ARBA:ARBA00006066}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJS44137.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ALIE01000047; EJS44137.1; -; Genomic_DNA.
DR AlphaFoldDB; J8LPY0; -.
DR HOGENOM; CLU_034979_1_0_1; -.
DR OrthoDB; 276931at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000006968; Chromosome IV.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000225; F:N-acetylglucosaminylphosphatidylinositol deacetylase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.10320; LmbE-like; 1.
DR InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR InterPro; IPR024078; LmbE-like_dom_sf.
DR PANTHER; PTHR12993:SF11; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL DE-N-ACETYLASE; 1.
DR PANTHER; PTHR12993; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL DE-N-ACETYLASE-RELATED; 1.
DR Pfam; PF02585; PIG-L; 1.
DR SUPFAM; SSF102588; LmbE-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 302 AA; 34863 MW; 8A9D23EB57BE0460 CRC64;
MSRLAKVSFS KLLYKITKLA IVLTILYIYF TPKITTRNNE SLKHVFAHKN SDSQINLVIA
HPDDEVMFFS PVISQLHSYF PNTVPFNIIC MSKGDAEGLG ETRVKELNDS ASLLLQNGRP
VSVQVMDFED GMDKVWEINS ITSTLSKTID LNNEKLNQII ITFDSYGVSD HINHKSCHTA
VKTLINDYTQ SKTEKNEESP HITALYLKSY KNNIFLKYSS FIWEILRILY NLVSPFHKDV
QPLPPTTTTE QSRLLLTNTH AQYILALAAM LNAHKSQMVW FRYGWWILSR FVYVNDFEVY
TY
//