GWT1_EMENI
ID GWT1_EMENI Reviewed; 474 AA.
AC Q5BF53; C8VQE8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=GPI-anchored wall transfer protein 1;
DE EC=2.3.-.-;
GN Name=gwt1; ORFNames=AN0827;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000013; EAA65657.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF88706.1; -; Genomic_DNA.
DR RefSeq; XP_658431.1; XM_653339.1.
DR AlphaFoldDB; Q5BF53; -.
DR STRING; 162425.CADANIAP00001833; -.
DR EnsemblFungi; CBF88706; CBF88706; ANIA_00827.
DR EnsemblFungi; EAA65657; EAA65657; AN0827.2.
DR GeneID; 2876604; -.
DR KEGG; ani:AN0827.2; -.
DR eggNOG; KOG0411; Eukaryota.
DR HOGENOM; CLU_020802_2_2_1; -.
DR InParanoid; Q5BF53; -.
DR OMA; GLYVMQP; -.
DR OrthoDB; 1202772at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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; 2.
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..474
FT /note="GPI-anchored wall transfer protein 1"
FT /id="PRO_0000246290"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 474 AA; 51678 MW; 0F360B80C3E5D5D7 CRC64;
MDPDYKSRKE AFVSNLTGGS ILEINAVTLV APASVFLWSV LQSRLSFFTP YGPAALITDF
LLNVLAILFA TTFYSSAPWL LNLLLVSPAF LILMNSRSRR TQTKAKPPQT ATAQHGPGAS
LPIHPFLTTY RAAMMIITCI AILAVDFRVF PRRFAKAENW GTSLMDLGVG SFVFSGGVVS
ARSVLKSRER GASPKKTLTQ RFTSSVRHSV PLLVLGLVRL YSVKNLDYAE HVTEYGVHWN
FFFTLGFLPP FVELFEGIAT LIPSYEVLSL AVAVLYQVAL ESTDLKSYIL VSPRGPDLLS
KNREGVFSFL GYLAIFLAGR ATGMRIIPGG ISPSNTPQQA RKRVLTRYGA NIPVSRRLAN
MPYVLWVAAF NNAQLFLFCL IETILFPSVH RASGSGKNDE AKRTDFATSP ILTAFNRGGL
AVFLVANLLT GAVNLTVPTL DVDKTRAMAI LVGYAALITG VALGLNKANI KISL
