ID G3MRD1_AMBMU Unreviewed; 487 AA. AC G3MRD1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-OCT-2020, entry version 18. DE RecName: Full=Phosphatidylinositol-glycan biosynthesis class W protein {ECO:0000256|RuleBase:RU280819}; DE EC=2.3.-.- {ECO:0000256|RuleBase:RU280819}; OS Amblyomma maculatum (Gulf Coast tick). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari; OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Amblyomminae; Amblyomma. OX NCBI_TaxID=34609 {ECO:0000313|EMBL:AEO36049.1}; RN [1] {ECO:0000313|EMBL:AEO36049.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Salivary gland {ECO:0000313|EMBL:AEO36049.1}; RX PubMed=22216098; RA Karim S., Singh P., Ribeiro J.M.; RT "A deep insight into the sialotranscriptome of the gulf coast tick, RT Amblyomma maculatum."; RL PLoS ONE 6:E28525-E28525(2011). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JO844432; AEO36049.1; -; mRNA. DR UniPathway; UPA00196; -. 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:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway. 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 {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 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..42 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU280819" FT TRANSMEM 54..71 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU280819" FT TRANSMEM 77..97 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU280819" FT TRANSMEM 138..159 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU280819" FT TRANSMEM 165..182 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..255 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU280819" FT TRANSMEM 262..284 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU280819" FT TRANSMEM 304..321 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU280819" FT TRANSMEM 333..352 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU280819" FT TRANSMEM 372..395 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU280819" FT TRANSMEM 427..447 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU280819" FT TRANSMEM 453..475 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU280819" SQ SEQUENCE 487 AA; 53463 MW; D8294698F053C2D5 CRC64; MDTSEKALHK AFVTSKDGCS PVQLLLRGGL LIYSTLLHAA LAELPVIKSR RKNVWFSATF AVAVQCVPFI LSFTLLAEYW ACVVFTVIAV TLGIRILQRL FDQHSVVKSH RKNVPGKRPI AKVAPHDYPG LTSARAQVIL MTVFGILAVD FATVPRYFAK TEKTGFSPMD LGVGAFVIIV AVSSREAKNS LPANRWKNVW KALRGSVALI ILGLVRLFMV TALNYQNPVH EYGIHWNFFF TLACTRVLTS VVYASVSIHL DLAVAVMLGC AYEACLLFTP LAAFLDSDER SGFLAANKEG LMSIVGYVAL HLAAAGTARM LGYKPRNCAR DWIMTGLQAA GISVAIFAAT YIMHTSVDPV SRRLANLSYC LWMYSLGVFA VALSVGVTLA NTALLPRSAQ VDYNLFAVSH ADSLNTDVDI LWKSINYNGM AVFLLANILT GLVNIFFHPR TASDIVCFVT LVGYTYVLCI FAVFLHRKMV KLKLPFT //