ID A0A182E792_ONCOC Unreviewed; 502 AA.
AC A0A182E792;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, 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 ORFNames=NOO_LOCUS3883 {ECO:0000313|EMBL:VDK70917.1};
OS Onchocerca ochengi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t03883-RA};
RN [1] {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t03883-RA}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
RN [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t03883-RA}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [3] {ECO:0000313|EMBL:VDK70917.1, ECO:0000313|Proteomes:UP000271087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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 EMBL; UYRW01000797; VDK70917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A182E792; -.
DR STRING; 42157.A0A182E792; -.
DR WBParaSite; nOo.2.0.1.t03883-RA; nOo.2.0.1.t03883-RA; nOo.2.0.1.g03883.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000077448; Unassembled WGS sequence.
DR Proteomes; UP000271087; Unassembled WGS sequence.
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.
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:UP000271087};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 44..62
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 68..89
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 126..143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 155..174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 195..217
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 292..314
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 345..366
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT TRANSMEM 448..470
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU280819"
FT REGION 483..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 58161 MW; B6761D6E512CD981 CRC64;
MGNGTTQAEI LFLQFVGPMS LLLRNIAVPR IFHIFSCIFQ INNWLIFIFD LLFIMMPVLL
ILTLLSDYIP LLLLVEAIII LIFVIVLICD HYFVKQRLRT YCDWFYQIND AHYLPTKFVT
YMRSHGLICT AIAILAVDFN VFPNRFAKTS TFGRSLMDLG TATFVYCFAV TDIFRHYPGR
VKHNIQEQKK RFCSLKPSSS ILLILLGIAR TVLLNSINYH YSVIEYGVHW NFFITLGMLR
LIVEFLGRRC HLLLGIVIGF TYQYFLTKQN LQEYLLSNET ERTDFISKNR EGIFSLFGYL
SLYYFASAIS SFLFTGTSDQ DYCDSHINFS LTEKRKRIKI WFNRFYQLLL LTVIIFGVQQ
LVVKLVGLPS RRIANMPYVL EMINLNKEAS TEKNVKKILL NDDENSLEML KPFLMDSINQ
YGLAFFLVAN ILTGLVNKSI NTSSVKNHYT ATAIITAYMF TCITIIHLFA RLRKKMKHKK
SLPSKIRPSW DSNSLPDPVV SI
//
