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Database: UniProt
Entry: G4UA92_NEUT9
LinkDB: G4UA92_NEUT9
Original site: G4UA92_NEUT9 
ID   G4UA92_NEUT9            Unreviewed;       511 AA.
AC   G4UA92;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=GPI-anchored wall transfer protein {ECO:0000256|RuleBase:RU280819};
DE            EC=2.3.-.- {ECO:0000256|RuleBase:RU280819};
GN   ORFNames=NEUTE2DRAFT_161797 {ECO:0000313|EMBL:EGZ76950.1};
OS   Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ76950.1, ECO:0000313|Proteomes:UP000008513};
RN   [1] {ECO:0000313|EMBL:EGZ76950.1, ECO:0000313|Proteomes:UP000008513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX   PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Genetics 189:55-69(2011).
CC   -!- FUNCTION: Probable acetyltransferase, which acetylates the inositol
CC       ring of phosphatidylinositol during biosynthesis of GPI-anchor.
CC       {ECO:0000256|ARBA:ARBA00002531, 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}.
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DR   EMBL; GL890999; EGZ76950.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4UA92; -.
DR   STRING; 510952.G4UA92; -.
DR   eggNOG; KOG0411; Eukaryota.
DR   HOGENOM; CLU_020802_2_2_1; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000008513; 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:UP000008513};
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        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        85..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        143..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        172..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        215..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        245..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        269..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        315..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        357..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        395..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        445..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        475..495
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
SQ   SEQUENCE   511 AA;  56022 MW;  FAD1FE1FFC890EC3 CRC64;
     MAIDSTTTQS YKQLKEDFVS NLSGGSVSEI AQVCAVAPVV SLVWSVLQAR QSFFRPYTPL
     GYAIDFLLNV GALLLSVTLY SSAPLLLNLL LLTVAAFVYL VPAHTRKKKP QLPPNAQSKK
     SSSEQPLGVL STKPFLTNYR GNMLIVTCIC ILAVDFRLFP RRFAKVETWG TSLMDMGVGS
     FVFSAGVVAS RPVLKERAEG KAAPLSIRLK KSLRHSLPLL VLGFIRLLSV KGLDYAEHVT
     EYGVHWNFFF TLGFLPPFVA LFQSALKVLP SYAGLALLLG VVYQVLLETT SLKAYILTGP
     RNDLLSMNRE GVFSFFGYLA IFLAGQDTGM LVLPRSLSRS ISGSNNKTSG TTQRRSLLLN
     MTGWSLVWIA LYFFATDYKY GFGLSVSRRM ANLPYMLWVA ASNAVLLLAF YLVDALLFPS
     FYSAQDVKTE KELYDMATSK VLRAYNRNGL AIFLLANLFT GLVNMTVPTL DVGRVATVGI
     LVAYMGALTA VAVGLDEYNV TIKLIITVGE G
//
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