GWT1_CRYNB
ID GWT1_CRYNB Reviewed; 598 AA.
AC P0CP65; Q55MX3; Q5KBA2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=GPI-anchored wall transfer protein 1;
DE EC=2.3.-.-;
GN Name=GWT1; OrderedLocusNames=CNBH3110;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AAEY01000042; EAL19212.1; -; Genomic_DNA.
DR RefSeq; XP_773859.1; XM_768766.1.
DR AlphaFoldDB; P0CP65; -.
DR PRIDE; P0CP65; -.
DR EnsemblFungi; AAW45325; AAW45325; CNI03250.
DR EnsemblFungi; EAL19212; EAL19212; CNBH3110.
DR GeneID; 4937835; -.
DR KEGG; cnb:CNBH3110; -.
DR VEuPathDB; FungiDB:CNBH3110; -.
DR HOGENOM; CLU_020802_1_0_1; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000001435; Chromosome 8.
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_0000410190"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
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 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 95..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..165
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; 65412 MW; F8522FD378E5DF21 CRC64;
MGDYKLAKEA FVSGNPGASI WSINAVSLVA LATYALWIAL SPYIRHGLLN NYLICVLPLL
LGVTIFSTSP LVFASFLSII SLFFIAKSQK RFNFPRSPEK PKGQWLDESD SDEEPAEPAS
AAGSAAVSPA KLLPSQVAFA SGSLLSTDPT ISPMSPSSSS SSGHEDPLGI MGVNRRRSPL
EGVSLDVPSH IDSKVRISPV PSLRLKKSRA TKVQGVEEKG RLPFLTVYRA HMMLMTVICI
LAVDFEVFPR WQGKCEDFGT SLMDVGVGSF VFSLGLVSTK SLSPPPPPPT PTSPALNSHI
IPLTPSPLSF ILISLRKSVP VLVLGFIRLI MVKGSDYPEH VTEYGVHWNF FFTLALVPVL
AVGVRPLTQW LRWSVLGVII SLLHQLCLTY YLQPIIFSFG RSGIFLANKE GFSSLPGYLS
IFLIGLSIGD HVLRLSLPPR RERVVSETIE EHEQSHFERK KLDLIMELIG YSLGWWALLG
GWIWAGGEVS RRLANAPYVF WVAAYNTTFL LGYLLLTHII PSSISSQTSP SILVPRLLDA
MNKNGLAVFL AANLLTGLVN VSMETMYAPA WLSMGVLMLY SLAVSCVGWV LKGRSIKI
