PIGW_DICDI
ID PIGW_DICDI Reviewed; 492 AA.
AC Q54MC0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Phosphatidylinositol-glycan biosynthesis class W protein {ECO:0000305};
DE EC=2.3.-.- {ECO:0000250|UniProtKB:Q7TSN4};
GN Name=pigw {ECO:0000305};
GN ORFNames=DDB_G0286111 {ECO:0000312|dictyBase:DDB_G0286111};
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Probable acetyltransferase, which acetylates the inositol
CC ring of phosphatidylinositol during biosynthesis of GPI-anchor.
CC {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; AAFI02000085; EAL64434.2; -; Genomic_DNA.
DR RefSeq; XP_637914.2; XM_632822.2.
DR AlphaFoldDB; Q54MC0; -.
DR STRING; 44689.DDB0235223; -.
DR TCDB; 9.B.315.1.4; the glycoslyphosphatidylinositol (gpi) membrane anchoring protein gwt1 (gwt1) family.
DR PaxDb; Q54MC0; -.
DR PRIDE; Q54MC0; -.
DR EnsemblProtists; EAL64434; EAL64434; DDB_G0286111.
DR GeneID; 8625425; -.
DR KEGG; ddi:DDB_G0286111; -.
DR dictyBase; DDB_G0286111; pigW.
DR eggNOG; KOG0411; Eukaryota.
DR HOGENOM; CLU_020802_2_2_1; -.
DR InParanoid; Q54MC0; -.
DR OMA; GLYVMQP; -.
DR PhylomeDB; Q54MC0; -.
DR Reactome; R-DDI-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR PRO; PR:Q54MC0; -.
DR Proteomes; UP000002195; Chromosome 4.
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:0032216; F:glucosaminyl-phosphatidylinositol O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR InterPro; IPR009447; PIGW/GWT1.
DR PANTHER; PTHR20661; PTHR20661; 1.
DR Pfam; PF06423; GWT1; 1.
DR PIRSF; PIRSF017321; GWT1; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..492
FT /note="Phosphatidylinositol-glycan biosynthesis class W
FT protein"
FT /id="PRO_0000330931"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 185..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 492 AA; 56091 MW; 689B46054666D8C6 CRC64;
MDDQYKNDHQ NFVSGNDGST FFETCFILTL MPISVLFQRV VFATFFNNDK FPLPLALRFI
LEFFFIIVPF ISAITFTELT PFLIVGMLIT CLVVPMFAQK NVTIYFKNPK ETLLNLNSMR
KGFLEEYRAF VMAATCICIL AVDFQVFPRR LGKTETYGIS LMDIGVGSVV LSGALVSRQS
RSSLIEKQQK KKREEEEDDN DKINKTSSSS SSSSSALKQQ QQQVLSRSSL MWHQVKAQAP
LMILGFVRMI LTKSINYQEH VSEYGLHWNF FFTLGFVSIS LAFLKFNANI SAILGVVLIC
VYQFLLNSFG LTDYILNHPR DNLISMNKEG ICSFVGYLAI YLIGTKIGTE LFKVRSSLTE
WRKFATKLLI SSIVFYILWI LCEIYIDKTS RRMANLGYVL AILSINLFNF SINILITLIT
GNHNASVIAK SINRNQLFIF LLGNILTGLI NFSMKTIYAP VEQSMIIITS YTFALCLLAF
ILDYKNINIK FW
