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GWT1_DEBHA
ID   GWT1_DEBHA              Reviewed;         493 AA.
AC   Q6BTT3;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=GPI-anchored wall transfer protein 1;
DE            EC=2.3.-.-;
GN   Name=GWT1; OrderedLocusNames=DEHA2C16082g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382135; CAG86468.2; -; Genomic_DNA.
DR   RefSeq; XP_458386.2; XM_458386.1.
DR   AlphaFoldDB; Q6BTT3; -.
DR   STRING; 4959.XP_458386.2; -.
DR   EnsemblFungi; CAG86468; CAG86468; DEHA2C16082g.
DR   GeneID; 2900457; -.
DR   KEGG; dha:DEHA2C16082g; -.
DR   VEuPathDB; FungiDB:DEHA2C16082g; -.
DR   eggNOG; KOG0411; Eukaryota.
DR   HOGENOM; CLU_020802_2_2_1; -.
DR   InParanoid; Q6BTT3; -.
DR   OMA; GLYVMQP; -.
DR   OrthoDB; 1202772at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000599; Chromosome C.
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.
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..493
FT                   /note="GPI-anchored wall transfer protein 1"
FT                   /id="PRO_0000246289"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        464..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   493 AA;  55211 MW;  F0C4AD27D94B765D CRC64;
     MSSLKEQKEL FVSNLLGGSI SETYNVTAVA LSAYLSYNLI SSYLDYKITF PVDFILNCMT
     ILLSITLYSN STNTLHLLIL VPGILAAIVG RWGQKDVKKS RSKKPRDAKG TKTEKQLLVK
     KPFITAYRSH MLVITNFAIL AVDFRMFPRR FAKVETWGTS LMDLGVGSFV FSMGLASSRA
     IIKQRFDSSK STDYRFKLSQ YVSLIMKNSI KTLPVLALGL IRLVSVKTLE YQEHVTEYGV
     HWNFFITLGL LPIFFGIIDP VLNFVPRFVV ALVICIGYEV LMVKTDLLSF ILRSDNRMES
     LVTMNKEGIF SFIGYFSIFI FGQSFGSFVL TGFKTPNNLF RMCSYQQYKK AGAKSGLFTV
     TSTQGLLIAT LFSQALFWYV QEAYFVSSIS RRLANLSYVL WVVSYNSTLL LGYNLIESVV
     AKPEAADSKI LNAFNNNGLL SFLLGNLLTG LTNMTINTLG CNAPVTFAIL VTYGLVLSII
     AVTLDRYGIY IKL
 
 
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