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ALG11_DEBHA
ID   ALG11_DEBHA             Reviewed;         616 AA.
AC   Q6BVB2;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase;
DE            EC=2.4.1.131;
DE   AltName: Full=Alpha-1,2-mannosyltransferase ALG11;
DE   AltName: Full=Asparagine-linked glycosylation protein 11;
DE   AltName: Full=Glycolipid 2-alpha-mannosyltransferase;
GN   Name=ALG11; OrderedLocusNames=DEHA2C03982g;
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: Required for N-linked oligosaccharide assembly. Has a role in
CC       the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core
CC       oligosaccharide on the cytoplasmic face of the endoplasmic reticulum
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC         beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-
CC         D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC         [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC         GlcNAc-diphosphodolichol + 2 GDP + 2 H(+); Xref=Rhea:RHEA:29523,
CC         Rhea:RHEA-COMP:12626, Rhea:RHEA-COMP:12627, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132511,
CC         ChEBI:CHEBI:132515; EC=2.4.1.131;
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000305}.
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DR   EMBL; CR382135; CAG85902.2; -; Genomic_DNA.
DR   RefSeq; XP_457857.2; XM_457857.1.
DR   AlphaFoldDB; Q6BVB2; -.
DR   STRING; 4959.XP_457857.2; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   EnsemblFungi; CAG85902; CAG85902; DEHA2C03982g.
DR   GeneID; 2900656; -.
DR   KEGG; dha:DEHA2C03982g; -.
DR   VEuPathDB; FungiDB:DEHA2C03982g; -.
DR   eggNOG; KOG1387; Eukaryota.
DR   HOGENOM; CLU_017896_1_1_1; -.
DR   InParanoid; Q6BVB2; -.
DR   OMA; WKHFTLI; -.
DR   OrthoDB; 1051021at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000599; Chromosome C.
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:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd03806; GT4_ALG11-like; 1.
DR   InterPro; IPR038013; ALG11.
DR   InterPro; IPR031814; ALG11_N.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   PANTHER; PTHR45919; PTHR45919; 1.
DR   Pfam; PF15924; ALG11_N; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..616
FT                   /note="GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-
FT                   mannosyltransferase"
FT                   /id="PRO_0000080275"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        386
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        502
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   616 AA;  70746 MW;  69F8BBC8881DF1DB CRC64;
     MGYLVVIGVI ACVAYGILQV VSTVLPRLLL VPSQNWQDKI KKEIEQPMVR YLKVGNKRSS
     YRRRLVLASK QPSFYTNFVN NKIKVASVDS QNDEGEFLAE MKKRDVRDPQ RKIIYGFFHP
     YANNGGGGER VLWQAVQATL ATSDRNIVAI YTTNYESDPT SILDKVEAKF QISRLDEDRI
     VFVYLRKYAR LIDGDYWKRF TLIGQLFGSM VLSWEAMFEL SPDVWIDTIG LPGSYLLVSL
     VLKIPIMSYV HYPIIQPEMF NKLKFQGLSQ IRVPKLSEIK TDVFSIGKLI YWSGVFYFYK
     YLGSLVNITL ANGSWTFNHI SNIWTINKDE AGYEMDILYP PCGTETLTKN VETLGSRENK
     LLFIAQFRPE KRHSLILRQY SKFLVNATSI GTPLKNIPTL VFLGSCRTPD DTKTLHDLKQ
     EVDDLELNGY VEFVVDCSYE DIMVWLSKVK FGLNAMWNEH FGIGVVEYMS RGVIPLCHAS
     AGPLLDIVTN WDNEPTSVSW YNNTGFFFKD KSDPDFDLSL QSDTASEFLQ FSSRDNKDST
     STYPTLARLL DELFITNPDL ISETRLQSMR ENGVKSVLEK FSNGVFTLKW MQYSNQLGDL
     EKSYREERRS GIEKVY
 
 
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