GWT1_CANAL
ID GWT1_CANAL Reviewed; 485 AA.
AC Q873N2; A0A1D8PHG5; Q59T33;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=GPI-anchored wall transfer protein 1;
DE EC=2.3.-.-;
GN Name=GWT1; OrderedLocusNames=CAALFM_C205730CA;
GN ORFNames=CaO19.14173, CaO19.6884;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E81022;
RX PubMed=12753194; DOI=10.1046/j.1365-2958.2003.03481.x;
RA Tsukahara K., Hata K., Nakamoto K., Sagane K., Watanabe N.-A.,
RA Kuromitsu J., Kai J., Tsuchiya M., Ohba F., Jigami Y., Yoshimatsu K.,
RA Nagasu T.;
RT "Medicinal genetics approach towards identifying the molecular target of a
RT novel inhibitor of fungal cell wall assembly.";
RL Mol. Microbiol. 48:1029-1042(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; AB092481; BAC66174.1; -; Genomic_DNA.
DR EMBL; CP017624; AOW27584.1; -; Genomic_DNA.
DR RefSeq; XP_712813.2; XM_707720.2.
DR AlphaFoldDB; Q873N2; -.
DR STRING; 237561.Q873N2; -.
DR ChEMBL; CHEMBL4523379; -.
DR ChEMBL; CHEMBL4662934; -.
DR GeneID; 3645575; -.
DR KEGG; cal:CAALFM_C205730CA; -.
DR CGD; CAL0000196562; GWT1.
DR VEuPathDB; FungiDB:C2_05730C_A; -.
DR eggNOG; KOG0411; Eukaryota.
DR HOGENOM; CLU_020802_2_2_1; -.
DR InParanoid; Q873N2; -.
DR OrthoDB; 1202772at2759; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:Q873N2; -.
DR Proteomes; UP000000559; Chromosome 2.
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; IMP:CGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:CGD.
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..485
FT /note="GPI-anchored wall transfer protein 1"
FT /id="PRO_0000215184"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 268
FT /note="A -> G (in Ref. 1; BAC66174)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="T -> A (in Ref. 1; BAC66174)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 55200 MW; B7F15DDEEDC22EB6 CRC64;
MSSSLKQLKE QFVSDLTGGT IEEIYAVTSI ALSSYLSFRL LKKSLGDLAL IYDYILNVLT
ILASITVYSN SPSYLHYFIV IPSLVIYLVN YHVEKPSSPH RQNDTKEDKS DELLPRKQFI
TAYRSQMLII TNLAILAVDF PIFPRRFAKV ETWGTSMMDL GVGSFVFSMG LANSRQLIKN
HTDNYKFSWK SYLKTIKQNF IKSVPILVLG AIRFVSVKQL DYQEHETEYG IHWNFFFTLG
FLPIVLGILD PVLNLVPRFI IGIGISIAYE VALNKTGLLK FILSSENRLE SLITMNKEGI
FSFIGYLCIF IIGQSFGSFV LTGYKTKNNL ITISKIRISK KQHKKESSSF FSVATTQGLY
LACIFYHLAF SLFISNLSFL QPISRRLANF PYVMWVVSYN ATFLLCYDLI EKFIPGNLTS
TVLDSINNNG LFIFLVSNLL TGFINMSINT LETSNKMAVI ILIGYSLTWT LLALYLDKRK
IYIKL
