ID   ALG11_CANAL             Reviewed;         609 AA.
AC   Q59S72; A0A1D8PPV0;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-MAY-2023, entry version 92.
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=CAALFM_C602270CA;
GN   ORFNames=CaO19.10972, CaO19.3468;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017628; AOW30162.1; -; Genomic_DNA.
DR   RefSeq; XP_712508.2; XM_707415.2.
DR   AlphaFoldDB; Q59S72; -.
DR   STRING; 237561.Q59S72; -.
DR   GlyCosmos; Q59S72; 2 sites, No reported glycans.
DR   EnsemblFungi; C6_02270C_A-T; C6_02270C_A-T-p1; C6_02270C_A.
DR   GeneID; 3645871; -.
DR   KEGG; cal:CAALFM_C602270CA; -.
DR   CGD; CAL0000201912; ALG11.
DR   VEuPathDB; FungiDB:C6_02270C_A; -.
DR   eggNOG; KOG1387; Eukaryota.
DR   HOGENOM; CLU_017896_1_1_1; -.
DR   InParanoid; Q59S72; -.
DR   OrthoDB; 197751at2759; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q59S72; -.
DR   Proteomes; UP000000559; Chromosome 6.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
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..609
FT                   /note="GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-
FT                   mannosyltransferase"
FT                   /id="PRO_0000080273"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        384
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   609 AA;  70929 MW;  D640F41FEFE276ED CRC64;
     MYLILLVVLA VYVTYKLITT VLPHHLLIPS QNWREKISYV VKYPKPIYLK VGTKRSSYRR
     RLILASENPA FYTNFINNKL KISPNDCENG DGFLNEMSRR DIDDPKRRII YGFFHPYANN
     GGGGERVLWQ AVKATLLADD KNICVIYTTN IEAQPLDILN KANKKFQIDG LDHSRVVFIY
     LRKFNNLIDG NYWKHFTLIG QLFGGILLSL EAMYELSPDV WIDTMGLPSS YLLVSLSLKI
     PILAYTHFPI LQEDMFGKLK FQKLKDLWKF NIIKFNDYFA LGKFIYWSIL YYFYVYLGSK
     VNIALANGSW TFNHLSKIWV FNTALGNVLD VLYPPCGTEF LIKQANLNQP RSNKLLYLAQ
     FRPEKRHALL LKEYSNFLSN NFPNVTQITN KFPTLVFAGS CRTADDTATL KFLQEQVAKL
     DLSRFVEFRI DISYDEVVEL LSSCKFGLNA MWNEHFGIGV VEYMARGCTP IVHASAGPLL
     DMIGRNDQQE NCLNNWKTDG GFFFKSYDDP DLDPNLQKNT ETGYIKFELF DQFIDYPTFE
     TLLKELYVND PTIIEDSKLL KMRQIDQNRV AEKFSNKAFN KKWIEYINDL NTLEKQYREE
     KRTKVEQVY
//