GenomeNet

Database: UniProt
Entry: A0A421JBQ3_9ASCO
LinkDB: A0A421JBQ3_9ASCO
Original site: A0A421JBQ3_9ASCO 
ID   A0A421JBQ3_9ASCO        Unreviewed;       465 AA.
AC   A0A421JBQ3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=GPI-anchored wall transfer protein {ECO:0000256|RuleBase:RU280819};
DE            EC=2.3.-.- {ECO:0000256|RuleBase:RU280819};
GN   ORFNames=JA9_004493 {ECO:0000313|EMBL:RLV86248.1};
OS   Meyerozyma sp. JA9.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=2028340 {ECO:0000313|EMBL:RLV86248.1, ECO:0000313|Proteomes:UP000286412};
RN   [1] {ECO:0000313|EMBL:RLV86248.1, ECO:0000313|Proteomes:UP000286412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA9 {ECO:0000313|EMBL:RLV86248.1,
RC   ECO:0000313|Proteomes:UP000286412};
RA   Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT   "Physiological and comparative genomic analysis of newly identified yeasts
RT   Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT   production.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable acetyltransferase, which acetylates the inositol
CC       ring of phosphatidylinositol during biosynthesis of GPI-anchor.
CC       {ECO:0000256|RuleBase:RU280819}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004687,
CC       ECO:0000256|RuleBase:RU280819}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU280819}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU280819}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the PIGW family. {ECO:0000256|ARBA:ARBA00007559,
CC       ECO:0000256|RuleBase:RU280819}.
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:RLV86248.1}.
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; NSDU01000010; RLV86248.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A421JBQ3; -.
DR   STRING; 2028340.A0A421JBQ3; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000286412; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR009447; PIGW/GWT1.
DR   PANTHER; PTHR20661; PHOSPHATIDYLINOSITOL-GLYCAN BIOSYNTHESIS CLASS W PROTEIN; 1.
DR   PANTHER; PTHR20661:SF0; PHOSPHATIDYLINOSITOL-GLYCAN BIOSYNTHESIS CLASS W PROTEIN; 1.
DR   Pfam; PF06423; GWT1; 1.
DR   PIRSF; PIRSF017321; GWT1; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU280819};
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU280819};
KW   GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502,
KW   ECO:0000256|RuleBase:RU280819};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280819};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286412};
KW   Transferase {ECO:0000256|RuleBase:RU280819};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU280819};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU280819}.
FT   TRANSMEM        22..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        72..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        222..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        293..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        372..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        411..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        434..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
SQ   SEQUENCE   465 AA;  51554 MW;  3FDF5D81297193EF CRC64;
     MSLKQQKENF VSGLTGGSVS EIYWVTSVAL SGYLAYNMVR GTNRDVPFVV DFSLQVIAIL
     LAVTLYSSSI GTLHGLVLGP AVLVMFLGAS RTAQKSKNVN SSSELLPQKP FLTAYRAQML
     ILTNLAILAV DFKVFPRRFA KVETWGTSMM DIGVGSFVFS MGLASSRLLI KQSLQQNHKR
     GSYVGLVFRS TVKSMPVLGL GLVRLISVKT LEYQEHVTEY GIHWNFFITL GLLPICLALL
     NPIIEIVPRV FLAFFVSICH EIALQKGLQE FVLRSDNRMA NVVTMNKEGI CSLPGYFSIF
     LFGQCFGYFV LPGRKTRNNL FGASQGSIQT KWTVTTNQGL IIATLMFHGC FWYCQNSFLV
     SSVSRRLANI SYVMWVVSYN SSMLLAYHWI NRAFPNASMS PILQAINKNG LAIFLLANVT
     TGLVNMTVNT LECGPIIAVA ILAIYGLSWV VAAMELDERK VYIKL
//
DBGET integrated database retrieval system