ALG11_KLULA
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 25-MAY-2022, entry version 97.
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 / 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; 28985.XP_455253.1; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblFungi; CAG97961; CAG97961; KLLA0_F03817g.
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: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:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IEA:EnsemblFungi.
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..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
