GWT1_CRYNH
ID GWT1_CRYNH Reviewed; 598 AA.
AC Q873N0; J9VWF9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=GPI-anchored wall transfer protein 1;
DE EC=2.3.-.-;
GN Name=GWT1; ORFNames=CNAG_04187;
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=12714589; DOI=10.1074/jbc.m301044200;
RA Umemura M., Okamoto M., Nakayama K., Sagane K., Tsukahara K., Hata K.,
RA Jigami Y.;
RT "GWT1 gene is required for inositol acylation of
RT glycosylphosphatidylinositol anchors in yeast.";
RL J. Biol. Chem. 278:23639-23647(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
CC -!- FUNCTION: Probable acetyltransferase, which acetylates the inositol
CC ring of phosphatidylinositol during biosynthesis of GPI-anchor.
CC {ECO:0000250}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIGW family. {ECO:0000305}.
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DR EMBL; AB092505; BAC66176.1; -; Genomic_DNA.
DR EMBL; CP003828; AFR96919.1; -; Genomic_DNA.
DR RefSeq; XP_012051648.1; XM_012196258.1.
DR AlphaFoldDB; Q873N0; -.
DR EnsemblFungi; AFR96919; AFR96919; CNAG_04187.
DR GeneID; 23887626; -.
DR VEuPathDB; FungiDB:CNAG_04187; -.
DR HOGENOM; CLU_020802_1_0_1; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000010091; Chromosome 9.
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:0008374; F:O-acyltransferase activity; IEA:UniProt.
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.
PE 3: Inferred from homology;
KW Acyltransferase; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..598
FT /note="GPI-anchored wall transfer protein 1"
FT /id="PRO_0000215186"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 94..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 598 AA; 65657 MW; B9F4AC6ADC0B530D CRC64;
MGDYKSAKEA FVSDNPGASI WSINAVSLVA LATYALWIAL SPYIRHGLLN NYLICVLPLL
FGVTIFSTSP LVFTSFLSII SLAFITKSQK CFKSVSSPEK PKGQWLDESD SDEEPAEPAS
AAGSAAVSPV KLLPSQVAFA SGSLLSPDPT TSPMSPSSSS ASGHEDPLGI MGVNRRRSLL
EGVSLDVPSH IDSKVRISPV PYLRLKKSRA TKAQWVKEKG RLPFLTVYRA HMMLMTVICI
LAVDFEVFPR WQGKCEDFGT SLMDVGVGSF VFSLGLVSTK SLSPPPPTPT PSSPALNSHI
IPLTPSPFTS ILISLRKSIP ILVLGFIRLI MVKGSDYPEH VTEYGVHWNF FFTLALVPVL
AVGIRPLTQW LRWSVLGVII SLLHQLWLTY YLQSIVFSFG RSGIFLANKE GFSSLPGYLS
IFLIGLSIGD HVLRLSLPPR RERVVSETNE EHEQSHFERK KLDLIMELIG YSLGWWALLG
GWIWAGGEVS RRLANAPYVF WVAAYNTTFL LGYLLLTHII PSPTSSQTSP SILVPPLLDA
MNKNGLAIFL AANLLTGLVN VSMKTMYAPA WLSMGVLMLY TLTISCVGWI LKGRRIKI
