ID   B5RTD2_DEBHA            Unreviewed;       632 AA.
AC   B5RTD2;
DT   04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 1.
DT   02-SEP-2026, entry version 79.
DE   RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN   OrderedLocusNames=DEHA2C17270g {ECO:0000313|EMBL:CAR65594.1};
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; Pichiomycetes;
OC   Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAR65594.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAR65594.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC   2968 {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
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., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Mannosyltransferase that operates in the biosynthetic pathway
CC       of dolichol-linked oligosaccharides, the glycan precursors employed in
CC       protein asparagine (N)-glycosylation. The assembly of dolichol-linked
CC       oligosaccharides begins on the cytosolic side of the endoplasmic
CC       reticulum membrane and finishes in its lumen. The sequential addition
CC       of sugars to dolichol pyrophosphate produces dolichol-linked
CC       oligosaccharides containing fourteen sugars, including two GlcNAcs,
CC       nine mannoses and three glucoses. Once assembled, the oligosaccharide
CC       is transferred from the lipid to nascent proteins by
CC       oligosaccharyltransferases. In the lumen of the endoplasmic reticulum,
CC       adds the eighth mannose residue in an alpha-1,6 linkage onto
CC       Man(7)GlcNAc(2)-PP-dolichol to produce Man(8)GlcNAc(2)-PP-dolichol.
CC       {ECO:0000256|ARBA:ARBA00044721}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC         [alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-
CC         Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-
CC         trans,poly-cis-dolichol + a di-trans,poly-cis-dolichyl beta-D-
CC         mannosyl phosphate = an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-
CC         D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC         (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC         alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + a di-
CC         trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:29535,
CC         Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19501, Rhea:RHEA-COMP:19518,
CC         Rhea:RHEA-COMP:19519, ChEBI:CHEBI:15378, ChEBI:CHEBI:57683,
CC         ChEBI:CHEBI:58211, ChEBI:CHEBI:132517, ChEBI:CHEBI:132519;
CC         EC=2.4.1.260; Evidence={ECO:0000256|ARBA:ARBA00048899};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29536;
CC         Evidence={ECO:0000256|ARBA:ARBA00048899};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363075}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU363075}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC       {ECO:0000256|ARBA:ARBA00007063, ECO:0000256|RuleBase:RU363075}.
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DR   EMBL; CR382135; CAR65594.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5RTD2; -.
DR   FunCoup; B5RTD2; 416.
DR   STRING; 284592.B5RTD2; -.
DR   KEGG; dha:DEHA2C17270g; -.
DR   VEuPathDB; FungiDB:DEHA2C17270g; -.
DR   eggNOG; KOG2516; Eukaryota.
DR   HOGENOM; CLU_008917_4_0_1; -.
DR   InParanoid; B5RTD2; -.
DR   OMA; WWVEVRM; -.
DR   OrthoDB; 19039at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000599; Chromosome C.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0052917; F:dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:TreeGrafter.
DR   InterPro; IPR005599; GPI_mannosylTrfase.
DR   PANTHER; PTHR22760:SF1; DOL-P-MAN:MAN(7)GLCNAC(2)-PP-DOL ALPHA-1,6-MANNOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF03901; Glyco_transf_22; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU363075};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU363075};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363075};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU363075};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU363075}.
FT   TRANSMEM        101..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        141..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        226..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        356..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        389..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
SQ   SEQUENCE   632 AA;  71898 MW;  5E5F9A5046A2C640 CRC64;
     MYKYNKLLDI ILLAIIVYHL LISPYSKVEE SFNIQAIHDI INYGVFPQEN ISYNYDHNNF
     PGSVPRTFVG SLAIAGIAKV IQSFTSLIGL DNVIFKDQSQ LNLQILVRCV LGFANGFAFM
     KIRDSINQLT LRDRISKRRG LIGFWFMILL ISQFHILYYS SRTLPNFIAL PLVSHAISKI
     IVGDMSGLTW LAFTGVVFRL EIGLFGVIIA LVSSFVFGQS NISLNLIMLC VGTVVGLITT
     LTIDSYFWGY WLVPELVSFK FNIISGKSAE WGTEPWAAYF NKYIWQLFRP PIVLILTLPG
     IMHDPADDKI STASINKTPN EKKIEVTHPA KNSLRILFVS SLLFVVAMSF QPHKEWRFII
     YIAPVLTLQA ANGFANISIR WSTSVFNKLL VLICLAFMLI GILLSVVMGY ISSFNYPGGD
     ALLFVNNYIS NNHDKEFLIH MDVASCMSGI NRFGEIHNNS AITYDKTEDE FDLLTIWNDI
     DILITEVNLN EIDALHASSK LTYNPNNWKI IHSSDKYKGI SVIPIIQLIK EQRINSYTIP
     ALLTQIADEF IHIKFSTIRN LIQSMVIRSN YLYVYERVSP DEGLDELIEE LKDQVSYKSK
     ESDNPDLKEV DLHDLREDVN DEINILEEEF TS
//