ID   GPI10_ASPOR             Reviewed;         728 AA.
AC   Q2UH15;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=AO090023000629;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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; AP007157; BAE59150.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UH15; -.
DR   STRING; 510516.Q2UH15; -.
DR   CAZy; GT22; Glycosyltransferase Family 22.
DR   PRIDE; Q2UH15; -.
DR   EnsemblFungi; BAE59150; BAE59150; AO090023000629.
DR   HOGENOM; CLU_012353_1_0_1; -.
DR   OMA; HEWPDYL; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000006564; Chromosome 3.
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:0000026; F:alpha-1,2-mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
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; Glycoprotein; Glycosyltransferase;
KW   GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..728
FT                   /note="GPI mannosyltransferase 3"
FT                   /id="PRO_0000246259"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        429..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        365
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   728 AA;  81947 MW;  04C4053BD5A3AAF7 CRC64;
     MSTSSRRRRS PLELSSSRSS SSSSSSYASW ASTTSPSTST STPPSLSRTT TVSTSHVFLF
     LLAFRLLNAL SLRTFFQPDE FFQSLEPAWQ TAFGETHGAN GDTICGLPSI LCYLLQFILS
     PTLPRALFVS PPHSAILSAI GDLYTWKLAR YVYGRRSHEA WAALALTVLS PWQWFCSTRT
     LSNCLETTIT IVALNLWPWE WSSESTPTVQ PRRNTRSTTR DTGLDNTGDG AVVVRLRKCL
     TLAALACILR PTNILIWMGL AGVAWFRSAW RERTILCREV LLCGVSVLTG SVVLDRLYYG
     LWTFPPLKFL YFNIAQSLAV YYGRNDWHYY ATQGYPLLLT TALPFTLVGL YRTLSQSQST
     INTRNVSVQT QLAAICLLMP LVLSLISHKE VRFIYPLLPS LHVLTAPPLV DFFLPAVSRS
     NGAYMPRRLS LVFLLLVNIT VAIYTSVYHA SGTLNVLSYL RDQQQAHTTV DKSAYSPGSS
     QRITAGFLMP CHSTPWRSHL VDPNIHAWAL SCEPPVDLTE PQKAVYVDEA DQFYNDPSQF
     LRENMVGGLR HLPRKPSYLA SSKSLEASPQ AYQQATPHEW PDYLIFFAQL EPTLHSFLRS
     SSYGECWRTW NTAWHDDSRR RGDIIVWCLD PTEQAAWRSA TRKRTLEHRD HQFDRIVETL
     RKNAPAEILP LDSMDILSVR AIGLLNLVLV LALGTTQTVL VRNPVTSLEE VLMDPSDMDL
     AKIFQEEN