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Database: UniProt
Entry: A0A3Q7T9Z4_VULVU
LinkDB: A0A3Q7T9Z4_VULVU
Original site: A0A3Q7T9Z4_VULVU 
ID   A0A3Q7T9Z4_VULVU        Unreviewed;       502 AA.
AC   A0A3Q7T9Z4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
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|RefSeq:XP_025851869.1,
GN   ECO:0000313|RefSeq:XP_025851870.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025851870.1};
RN   [1]
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025851869.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025851869.1};
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025851870.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025851870.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025851870.1};
RG   RefSeq;
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_025851869.1; XM_025996084.1.
DR   RefSeq; XP_025851870.1; XM_025996085.1.
DR   STRING; 9627.ENSVVUP00000025073; -.
DR   Ensembl; ENSVVUT00000033146; ENSVVUP00000025073; ENSVVUG00000018383.
DR   KEGG; vvp:112917960; -.
DR   OMA; GLYVMQP; -.
DR   OrthoDB; 228697at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000286640; Unplaced.
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   GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
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:UP000286640};
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        28..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        56..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        124..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        160..181
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..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        303..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        337..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        367..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        447..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        470..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
SQ   SEQUENCE   502 AA;  56664 MW;  94BD3A0DA757E3E5 CRC64;
     MSQKQMKEAF VSNHNGTSVL EVTQGLCLPA FCILCRGLLI ILSQYLCSSH TWRTRLFIDF
     VFLIVPLVAT LTILSSFVLL EHLAVIILGA GLFYQIYCRR TYYARIPVQK ILEKFLKISL
     ESEYVPAISC FRVINSAFTA VAILAVDFPL FPRRFAKTEL YGTGAMDFGV GGFIFGTAMV
     CPEVRRKYAE GSRFYYLTKS LYSVWPLVFL GIGRLVIIKS IGYQEHLTEY GVHWNFFFTL
     MVVKLITSLL LIIFPLNKSW IVAISIIVLY QLALDFTPLK RLILYGTDGS GTRIGLLNAN
     REGIISTLGY VAIHMAGVQT GSYMFKKRSH VKDWIKVTYC ILLTAISLFI SLYIVQVNVE
     VVSRRMANLA FCIWIVASSL ILLSSLLLGD IILSFAKFLT KGAIVPCSWK PVQPSATSKK
     HSESLVSEAE RKEPSLCLIT AMNRNQLVFF LLSNITTGLI NLMVDTLHSS TLWALIVLNL
     YMFTNCLIIF VLHLQDKTIK FW
//
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