GPI10_EMENI
ID GPI10_EMENI Reviewed; 663 AA.
AC Q5BCB9; C8VPH0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=AN1811;
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: 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; AACD01000029; EAA64976.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF85606.1; -; Genomic_DNA.
DR RefSeq; XP_659415.1; XM_654323.1.
DR AlphaFoldDB; Q5BCB9; -.
DR STRING; 162425.CADANIAP00008459; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR EnsemblFungi; CBF85606; CBF85606; ANIA_01811.
DR EnsemblFungi; EAA64976; EAA64976; AN1811.2.
DR GeneID; 2875187; -.
DR KEGG; ani:AN1811.2; -.
DR eggNOG; KOG1771; Eukaryota.
DR HOGENOM; CLU_012353_1_0_1; -.
DR InParanoid; Q5BCB9; -.
DR OMA; HEWPDYL; -.
DR OrthoDB; 901894at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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: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; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..663
FT /note="GPI mannosyltransferase 3"
FT /id="PRO_0000246263"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 75503 MW; 5A3DC5E22F51F02C CRC64;
MPMSARSRRS NPRLPPSPSS SSSSDAVRAS PHSSPPSRLR PPSANPDVSS NILLFLIGFR
LVNALTVRTF FQPDEFFQSL EPAWKIAFGT NQGPWITWEW EHQLRSSLHP LIFAAVYTVA
DLVARTLGLT PTSRAELLIA GPGITQAVIA AVGDFYTWKL ARYIYGDRSH ESWATVRIRS
NAIEADADQL QLALTVVSLA SVALYRSAWG ERQTLAREAL ICGSSVLAVS TVVDRFFYGF
WTFPPLRFLY FNVAQSLAAF YGRNDWSYYA SQGYPLLLTT ALPFTLVGLY RTLKTPPKLE
KQKGSILVQL ASISLAMPAT LSVITHKEVR FIYPLLPALH ILSASPLVEF FIPALTTTNR
EYISRRLTLI FLLWANVAIA IYTTLFHASG VISVLSYIRE QHQIHGTANI PSLPKESPAS
YGGITTGFLM PCHSTPWRSH LVEPTIHAWA LSCEPPVGLT AEEKAAYRDE ADQFYDNPTQ
FLQDNMVGGL RHIPRRPSYA TPPSSQRQPT QLFPPHEWPD YLVFFAQLEP TLKDALRGSS
YGECWRTFNS AWHDDSRRRG DVVVWCLDHA KQQAWQSQKH QRELEDRDRQ FDHIIKRFQR
DATPSKSWHW SHWTSPFSSQ SKSWSWPWER KKRTLFGYEL PDLPQWGWFG KRKKKTLLSD
FWF
