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Database: UniProt
Entry: A0A2T7A3P3_TUBBO
LinkDB: A0A2T7A3P3_TUBBO
Original site: A0A2T7A3P3_TUBBO 
ID   A0A2T7A3P3_TUBBO        Unreviewed;       481 AA.
AC   A0A2T7A3P3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=GPI-anchored wall transfer protein {ECO:0000256|RuleBase:RU280819};
DE            EC=2.3.-.- {ECO:0000256|RuleBase:RU280819};
GN   ORFNames=B9Z19DRAFT_1041209 {ECO:0000313|EMBL:PUU82320.1};
OS   Tuber borchii (White truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=42251 {ECO:0000313|EMBL:PUU82320.1, ECO:0000313|Proteomes:UP000244722};
RN   [1] {ECO:0000313|EMBL:PUU82320.1, ECO:0000313|Proteomes:UP000244722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tbo3840 {ECO:0000313|EMBL:PUU82320.1,
RC   ECO:0000313|Proteomes:UP000244722};
RG   DOE Joint Genome Institute;
RA   Murat C., Kuo A., Barry K.W., Clum A., Dockter R.B., Fauchery L., Iotti M.,
RA   Kohler A., Labutti K., Lindquist E.A., Lipzen A., Ohm R.A., Wang M.,
RA   Grigoriev I.V., Zambonelli A., Martin F.M.;
RT   "Draft genome sequence of Tuber borchii Vittad., a whitish edible
RT   truffle.";
RL   Submitted (APR-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|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}.
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:PUU82320.1}.
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DR   EMBL; NESQ01000030; PUU82320.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7A3P3; -.
DR   STRING; 42251.A0A2T7A3P3; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000244722; 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:UP000244722};
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        24..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        53..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        77..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        129..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        167..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        206..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        269..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        346..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        383..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        422..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        450..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
SQ   SEQUENCE   481 AA;  53090 MW;  EB3D64D12360342B CRC64;
     MAQSLKNLKQ DFVSNLTGGT INEINLVTAV APATYILYAA LQTRLGFFKS YGPLQFVADF
     LLSAVAILFS ITLYSSFPLL LNLLIISPAI LLHLGQPRNT KRPAKPKPHN VEKEANSVPE
     FPKKAFLTVY RGSMMVITCC AILAVDFRVF PRRFAKVENW GTSLMDIGVG SFVFSGGMMS
     AKPVIRSYLV KRASEPLGAR LKSAMRTSLP LLVLGIVRLI MVKGVDYAEH VTEYGVHWNF
     FFTLGFLPPL LAIFESVSPA AFKMGISPTF VYTLLSLVTA VGYQIVLEKT GLKAFILVGD
     RNKYGLISQN KEGISSFAGY LSIFLAGMAT GMYTLPRAAQ SQRFGLLKKL TGWSLFWTVS
     FMIAKERWGL DIAVSRRLAN LPYILWVASF NTAQITAFYL VERGYFYGVE YSVSVPKVLE
     AFNRNGLAIF LVANLLTGLV NISINTLECG RVLAMGVLTS YILVLTLLAV GLDYKNMSIK
     L
//
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