GPI10_DEBHA
ID GPI10_DEBHA Reviewed; 549 AA.
AC Q6BH65; B5RUW7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 84.
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=DEHA2G21010g;
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: 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; CR382139; CAR66012.1; -; Genomic_DNA.
DR RefSeq; XP_002770680.1; XM_002770634.1.
DR AlphaFoldDB; Q6BH65; -.
DR STRING; 4959.XP_002770680.1; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR EnsemblFungi; CAR66012; CAR66012; DEHA2G21010g.
DR GeneID; 8999268; -.
DR KEGG; dha:DEHA2G21010g; -.
DR VEuPathDB; FungiDB:DEHA2G21010g; -.
DR eggNOG; KOG1771; Eukaryota.
DR HOGENOM; CLU_012353_0_1_1; -.
DR InParanoid; Q6BH65; -.
DR OMA; HHMVFNN; -.
DR OrthoDB; 901894at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000000599; Chromosome G.
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; 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..549
FT /note="GPI mannosyltransferase 3"
FT /id="PRO_0000246262"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..119
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..205
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..289
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..549
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 549 AA; 64581 MW; 55F70BC55A999C38 CRC64;
MAYNNSVRKR KKDIQDANGF HRDQTIDKKS RATNKLEESL PTFKVFIVLF FIRLLNSLTI
KTFFQADEYY QCLEPAYNFV FGSGYITWEW EEGIRSSIHP LIYALGYKMV SYVHFDDKPI
ILIPKVIGAL IASIGEVYLY KFSKKFTKNE KLARLTLILS LLSPFNWYII TRSFSNSFEM
VLTTIAFTYW PWDNVISYKD ISMSCIIAFI SCIVRPTNGI IWLYLGINFM IKNYKLEKQS
GKLMKLILIL SIELILILLV NTGLDYIFYG KTTFPLYNFV EFNVIRNLSI FYGVAPWHFY
LFQGVPIILM TYLPWLLHSA IVLKKYKSLL GQVAILMIGG FSLIDHKEIR FIYPLQPIFM
LMVAYSIHET KHKFQRLYKF LVPVIIILNL IIAIFFTQVH ERGVIDIVQY LRNNPDIESF
GFLTPCHSTP WQSHINNPNL VNKSWFLTCE PPLHLTTTSL KEIKSYRDES DQFYDNPAQF
LSEHFQSFAD SRNTGASNWP SRLIIFEPLE NFMDDFLRGS NYFECERFFN SYFHWDDRRK
GDIIVYCQI
