ID   ALG11_KLULA             Reviewed;         570 AA.
AC   Q6CLD6;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 103.
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=KLLA0F03817g;
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 /
RC   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: 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; CR382126; CAG97961.1; -; Genomic_DNA.
DR   RefSeq; XP_455253.1; XM_455253.1.
DR   AlphaFoldDB; Q6CLD6; -.
DR   STRING; 284590.Q6CLD6; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   GlyCosmos; Q6CLD6; 6 sites, No reported glycans.
DR   PaxDb; 284590-Q6CLD6; -.
DR   GeneID; 2895341; -.
DR   KEGG; kla:KLLA0_F03817g; -.
DR   eggNOG; KOG1387; Eukaryota.
DR   HOGENOM; CLU_017896_1_1_1; -.
DR   InParanoid; Q6CLD6; -.
DR   OMA; WKHFTLI; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   InterPro; IPR038013; ALG11.
DR   InterPro; IPR031814; ALG11_N.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   PANTHER; PTHR45919; GDP-MAN:MAN(3)GLCNAC(2)-PP-DOL ALPHA-1,2-MANNOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR45919:SF1; GDP-MAN:MAN(3)GLCNAC(2)-PP-DOL ALPHA-1,2-MANNOSYLTRANSFERASE; 1.
DR   Pfam; PF15924; ALG11_N; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..570
FT                   /note="GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-
FT                   mannosyltransferase"
FT                   /id="PRO_0000080276"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        490
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        562
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   570 AA;  65348 MW;  425A2A8D81205E1F CRC64;
     MKLADFVTYV FGSLLAGLVT LKVLSSFIPS LLVTLPAKVR LRVNNSLLKC SNNLNRIPVL
     DFGWKNSSVR RAFILASERP SDYTNKIYGD RVHIAYNDRI KRESFVNKLG FDSKRKLLGF
     FHPYCNAGGG GEKVLWKAVE TSLNQDKNNI CVIYTGDTDV NGSDILNSVR RRFEYDLDSD
     RIVFIFLQKR RLVESKSWPK FTLLGQAYGS IILSIEALTT LAPDYWIDTM GYPFAYPFVS
     LFARIPIVTY THYPVISTDM LQKLKTMPGF HTNFKLIGKY VYWKIFMLAY KFSGLFVEIA
     STNSTWTYNH IKSIWSSTKN IHIIYPPCST ESLIEGCDKS DPVKRLNQAV VIAQFRPEKR
     HELILSSFSS FIDATTKKDL IPKIIFIGST RNVEDREYVE TLKKYAFEAL KIPTHLVDFK
     TDCKYDDMKS ILYSSWFGIN AMWNEHFGIA VVEYMASGLI PLCHASAGPL YDIVVPWDSK
     KNEQSTDKAN ETGFFFIDET DPDFLAKDSS KYSSLRTLFA QVSKLNTVQR IDISNRAKMC
     SLSKFSDSEF ERSWNEVLEE LNLTHNRMFS
//