ID F1N3J6_BOVIN Unreviewed; 503 AA.
AC F1N3J6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Phosphatidylinositol-glycan biosynthesis class W protein {ECO:0000256|RuleBase:RU280819};
DE EC=2.3.-.- {ECO:0000256|RuleBase:RU280819};
GN Name=PIGW {ECO:0000313|Ensembl:ENSBTAP00000045720.2,
GN ECO:0000313|VGNC:VGNC:32881};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000045720.2, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000045720.2, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000045720.2,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000045720.2}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000045720.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|RuleBase:RU280819}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU280819}; Multi-pass membrane protein
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.
CC {ECO:0000256|RuleBase:RU280819}.
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DR RefSeq; XP_005220090.1; XM_005220033.3.
DR RefSeq; XP_005220094.1; XM_005220037.3.
DR RefSeq; XP_005220095.1; XM_005220038.2.
DR RefSeq; XP_005220098.1; XM_005220041.3.
DR RefSeq; XP_010814082.1; XM_010815780.2.
DR RefSeq; XP_010814083.1; XM_010815781.1.
DR RefSeq; XP_015314035.1; XM_015458549.1.
DR RefSeq; XP_015314036.1; XM_015458550.1.
DR AlphaFoldDB; F1N3J6; -.
DR Ensembl; ENSBTAT00000048729.3; ENSBTAP00000045720.2; ENSBTAG00000034396.3.
DR GeneID; 768052; -.
DR CTD; 284098; -.
DR VEuPathDB; HostDB:ENSBTAG00000034396; -.
DR VGNC; VGNC:32881; PIGW.
DR GeneTree; ENSGT00390000013520; -.
DR HOGENOM; CLU_020802_2_1_1; -.
DR InParanoid; F1N3J6; -.
DR OMA; GLYVMQP; -.
DR TreeFam; TF314687; -.
DR Reactome; R-BTA-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000034396; Expressed in conceptus and 105 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032216; F:glucosaminyl-phosphatidylinositol O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
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|RuleBase:RU280819};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280819};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
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 57..75
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 81..98
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 261..284
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 304..326
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 338..356
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 368..389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 448..465
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 471..493
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
SQ SEQUENCE 503 AA; 56312 MW; 503F65C1F368461C CRC64;
MSQKQMKEAF VSNQNGTSVL EITEGLCLPA LCILCRGLLI ILSQQLCSSL HNSRTRFLVD
FAFLIVPLVT TLTIFSSFVL LEYLVAIILG AGLLYEIYCR RTCYARMPFQ KICEKFLKVS
LESEHIPAIS CFRVVNSAFT AVAILAVDFP LFPRRYAKTE LYGTGAMDYG VGGFIFGSAM
VSPEVRRKYT KGSRFCYLTK SLYSLWPLVF LGVGRLVAIK SVDYQEHLTE YGVHWNFFFT
LIAVKLITSL LLIICPLNRS WVVAISIAAL YQLALDFTPL KSLILYGTDG SGTRVGLLNA
NREGIISILG YVAVHMAGVQ TGLYVLKKRS HIKDWIKVAC CILLTAIGLF ISLYIVQVNV
EVASRRMANL AFCIWIVASC LILLSSLLLG DIILSFAKFV IKEAAVPCSW KLIQSPTANK
KHLESIVFDA KRKEPTLCLI TAMNRNQLLF FLLSNVTTGL VNLSIDTLHS STPWALCLLN
LYMFTNCLII YVLHLQDKTI KFW
//
