ID   GPI10_KLULA             Reviewed;         601 AA.
AC   Q6CN76;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
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; OrderedLocusNames=KLLA0E14762g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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: 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; CR382125; CAG99700.1; -; Genomic_DNA.
DR   RefSeq; XP_454613.1; XM_454613.1.
DR   AlphaFoldDB; Q6CN76; -.
DR   STRING; 28985.XP_454613.1; -.
DR   CAZy; GT22; Glycosyltransferase Family 22.
DR   EnsemblFungi; CAG99700; CAG99700; KLLA0_E14719g.
DR   GeneID; 2893888; -.
DR   KEGG; kla:KLLA0_E14719g; -.
DR   eggNOG; KOG1771; Eukaryota.
DR   HOGENOM; CLU_012353_2_0_1; -.
DR   InParanoid; Q6CN76; -.
DR   OMA; HEWPDYL; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000598; Chromosome E.
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:EnsemblFungi.
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; 1.
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..601
FT                   /note="GPI mannosyltransferase 3"
FT                   /id="PRO_0000246265"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        360..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        521
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   601 AA;  70166 MW;  F42FD38B0E62D2B8 CRC64;
     MSNQVPLKRL FKVILVIRCV QALLTRTFFQ ADEFWQSLEP AHYMAFGYGE LTWEWSFGLR
     SYAFPLIFQI GYTLVKYAAI SCELIVQTAT DWVLLFVANV IPNSEFGWEM VQEMRSFPEE
     IRGFIEYQGV IYAPKLIMAV LAAIGEFHVI LLAEKLYKLT MDKSDDSKGS DKKHSTVINF
     TLVATVSNFF NCFFITRSFI NSFEMILTSV SLYYWDWTSG EHIESFDFLK SLIIGTFTVL
     QRPTNAFIWL ILGGYMILNL VLSKRWRKLF SLLIKVICAS FISISTNLCI DYYFYGYITI
     PVLKFIKFNC TSSLSKFYGV APWNFHVFQS LPIVAGYSLP LLIHSFFCSL TKKRFLSPLV
     NPFLQIKTVV LLNVILYSLI PHKEFRFIYP LQPFFIILSV FDGIWLLQKY GSTATTRTME
     FFSQVMWILP VVSMVASMLL STLHESGTVA VMDYLHSIRN IDSIGFIMPC HSTPWQSHFH
     RNDVKELWAI TCSPPLHLLT DPDANAKLPF YMDESDYLYD NISKFMYQHF PPVFRKSLRS
     PGKQYTYEWP EYLVIFEDLD SQFMNDYLVD SMYIEETRFF NSLVHWDKRR SGDIIIYHKM
     P