GPI10_ASPFU
ID GPI10_ASPFU Reviewed; 771 AA.
AC Q4WPG0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=GPI mannosyltransferase 3;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase III;
DE Short=GPI-MT-III;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 10;
GN Name=gpi10; ORFNames=AFUA_4G09130;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI
CC during GPI precursor assembly (By similarity). {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 glycosyltransferase 22 family. PIGB
CC subfamily. {ECO:0000305}.
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DR EMBL; AAHF01000005; EAL89874.1; -; Genomic_DNA.
DR RefSeq; XP_751912.1; XM_746819.1.
DR AlphaFoldDB; Q4WPG0; -.
DR STRING; 746128.CADAFUBP00006447; -.
DR EnsemblFungi; EAL89874; EAL89874; AFUA_4G09130.
DR GeneID; 3509380; -.
DR KEGG; afm:AFUA_4G09130; -.
DR VEuPathDB; FungiDB:Afu4g09130; -.
DR eggNOG; KOG1771; Eukaryota.
DR HOGENOM; CLU_012353_1_0_1; -.
DR InParanoid; Q4WPG0; -.
DR OMA; HEWPDYL; -.
DR OrthoDB; 901894at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0043295; F:glutathione binding; IDA:AspGD.
DR GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR InterPro; IPR039521; PIG-B/GPI10.
DR PANTHER; PTHR22760; PTHR22760; 1.
DR PANTHER; PTHR22760:SF4; PTHR22760:SF4; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..771
FT /note="GPI mannosyltransferase 3"
FT /id="PRO_0000246258"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 87863 MW; 9FB0B48C20FF0487 CRC64;
MSSSRRRKSF TSSSSSSSPS FHSPPPTSRL RPRSPPSSNT KTSPTSTTPL ATNILLSLIA
FRLVNAFTVR TFFQPDEFFQ SLEPAWQIAF GENQGAWITW EWRHQLRSSI HPLLFAAVYS
AADVVAQLLR LSLASRADLL VAAPKTAQAV IAGLGDFYTW KLARYVYGAR SYEAWATLAL
TVVSPWQWFC STRTLSNCLE TTITIVALYL WPWSWSFETP VRKKATRAAS RERAQRGPEG
SDSLQRLRQC LSLAAVACIL RPTNILIWMG LASVAWFRTS WDRRAILVRE VLLCGCAVLG
LSCVVDRLFY GSWTFPPLRF LYFNIAQSLA VFYGRNDWHY YVSQGFPLLL TTALPFALVG
LYRALAQVRT FGLGHLQSLV QAQLALICVI MPFVLSLVSH KEVRFIYPLL PSLHILSAPP
LVDYFLPAVI RSSRSYTPRR LTLIFLLLVN IVIALYTTIY HASGPSNILS YLRQQHELHA
PAAQTPSNLR PSVKDPSPHG ITAGFLMPCH STPWRSHLIY PTIHAWALTC EPPVDQTAAQ
KATYIDEADQ FYANPARFLR EHMAGGLRHI SRKPSYLSAQ PRPQHPSTTS TNDASHEWPD
YLIFFAQLEP TLQSLLRASS YAECYRTFNT AWHDDWRRKG DIVAWCLDPA EQQAWRSATR
QRDLENRERQ FDRIIESFRK EASGKRDGKL SPFRRWFSSS SSVAPSSSLS LSWPTSWRWP
WGQRKRTAWL GVQIPQWTRT RPSWTAWGGD WFGGWRQKKK TKKLLERDLW S
