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Database: UniProt
Entry: A0A1L8H704_XENLA
LinkDB: A0A1L8H704_XENLA
Original site: A0A1L8H704_XENLA 
ID   A0A1L8H704_XENLA        Unreviewed;       505 AA.
AC   A0A1L8H704;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Phosphatidylinositol-glycan biosynthesis class W protein {ECO:0000256|RuleBase:RU280819};
DE            EC=2.3.-.- {ECO:0000256|RuleBase:RU280819};
GN   Name=pigw.S {ECO:0000313|RefSeq:XP_018104834.1,
GN   ECO:0000313|Xenbase:XB-GENE-976537};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018104834.1};
RN   [1] {ECO:0000313|RefSeq:XP_018104834.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018104834.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018104834.1};
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_018104834.1; XM_018249345.2.
DR   AlphaFoldDB; A0A1L8H704; -.
DR   STRING; 8355.A0A1L8H704; -.
DR   PaxDb; 8355-A0A1L8H704; -.
DR   GeneID; 100380976; -.
DR   KEGG; xla:100380976; -.
DR   AGR; Xenbase:XB-GENE-976537; -.
DR   CTD; 100380976; -.
DR   Xenbase; XB-GENE-976537; pigw.S.
DR   OMA; GLYVMQP; -.
DR   OrthoDB; 228697at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 100380976; Expressed in egg cell and 19 other cell types or tissues.
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|RuleBase:RU280819};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU280819};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
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        22..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        55..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        135..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        165..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        203..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        239..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        264..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        306..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        340..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        374..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        450..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
FT   TRANSMEM        473..495
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU280819"
SQ   SEQUENCE   505 AA;  57371 MW;  FA3ACBDE6601C906 CRC64;
     MTEKLLKEAF VSNLNGTNIS EITAGLSISS LCFLFRGLIF VLYQEKYGPL NYSWKFHLLL
     DYILLVFPLV LSCTVFSDFL YVVPLSYITA CTLLFYIIYK RRTNCVKRQL FGVIKSFLNV
     HVESRTMPPV TNFRVFLNIL TAIAILAVDF PIYPRRYAKT ETYGTGVMDL GVGGFIFANA
     IVSPEAKARE NLFCNRFSNL KKQLVSVWPF LILGFGRLIS VKKADYHEHV SEYGLHWNFF
     FTLAVVRVLA SFLLAVFPTQ KSWVVAATSV SLYQVALETT GLKDFVFYGS DGKGTRVGFL
     NANREGIVSV TGYVALYMAG VQVGVYVLKK RAVLKDLITA LWTLIIIALS LFAILHLFQM
     YIEPVSRRLA NLTFFIWTIA QCLSLLCFIF LSDLLIVFAK FLVTGSRIPG TWVICNSSFS
     TKNQSIKRTE DKESIKNNFC LIQAISRNPL LFFLLSNVMT GLVNIVMNTM NTTSFLSLLV
     LVLYMFFTCL IVYFLHVNNV NVKWW
//
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