ID   PIGW_BOVIN              Reviewed;         503 AA.
AC   Q1LZA4;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Phosphatidylinositol-glycan biosynthesis class W protein {ECO:0000305};
DE            Short=PIG-W {ECO:0000305};
DE            EC=2.3.-.- {ECO:0000250|UniProtKB:Q7TSN4};
GN   Name=PIGW {ECO:0000305};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for the transport of GPI-anchored proteins to the
CC       plasma membrane. Probable acetyltransferase, which acetylates the
CC       inositol ring of phosphatidylinositol during biosynthesis of GPI-
CC       anchor. Acetylation during GPI-anchor biosynthesis is not essential for
CC       the subsequent mannosylation and is usually removed soon after the
CC       attachment of GPIs to proteins. {ECO:0000250|UniProtKB:Q7TSN4}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000250|UniProtKB:Q7TSN4}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q7TSN4}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q7TSN4}.
CC   -!- SIMILARITY: Belongs to the PIGW family. {ECO:0000305}.
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DR   EMBL; BC116121; AAI16122.1; -; mRNA.
DR   RefSeq; NP_001070577.1; NM_001077109.1.
DR   AlphaFoldDB; Q1LZA4; -.
DR   STRING; 9913.ENSBTAP00000045720; -.
DR   PaxDb; Q1LZA4; -.
DR   GeneID; 768052; -.
DR   KEGG; bta:768052; -.
DR   CTD; 284098; -.
DR   eggNOG; KOG0411; Eukaryota.
DR   InParanoid; Q1LZA4; -.
DR   OrthoDB; 1202772at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:UniProt.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR   InterPro; IPR009447; PIGW/GWT1.
DR   PANTHER; PTHR20661; PTHR20661; 1.
DR   Pfam; PF06423; GWT1; 1.
DR   PIRSF; PIRSF017321; GWT1; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Endoplasmic reticulum; Glycoprotein;
KW   GPI-anchor biosynthesis; Membrane; Phosphoprotein; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..503
FT                   /note="Phosphatidylinositol-glycan biosynthesis class W
FT                   protein"
FT                   /id="PRO_0000246281"
FT   TOPO_DOM        1..56
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        473..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         415
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z7B1"
FT   CARBOHYD        15
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   503 AA;  56298 MW;  674C7C39D2F26FC5 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 LLLICPLNRS WVVAISIAAL YQLALDFTPL KSLILYGTDG SGTRVGLLNA
     NREGIISVLG YVAVHMAGVQ TGLYVLKKRS HIKDWIKVAC CILLTAIGLF ISLYIVQVNV
     EVASRRMANL AFCIWIVASC LILLSSLLLG DIILSFAKFV IKEAAVPCSW KLIQSPTANK
     KHLESIVFDA KRKEPTLCLI TAMNRNQLLF FLLSNVTTGL VNLSIDTLHS STPWALCLLN
     LYMFTNCLII YVLHLQDKTI KFW