ALG2_CANAL
ID ALG2_CANAL Reviewed; 443 AA.
AC Q59LF2; A0A1D8PQB6;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Alpha-1,3/1,6-mannosyltransferase ALG2;
DE EC=2.4.1.132;
DE EC=2.4.1.257;
DE AltName: Full=Asparagine-linked glycosylation protein 2;
DE AltName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase;
DE AltName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase;
DE AltName: Full=GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase;
GN Name=ALG2; OrderedLocusNames=CAALFM_C604030WA;
GN ORFNames=CaO19.1221, CaO19.8808;
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: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and
CC Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol
CC diphosphate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol +
CC GDP + H(+); Xref=Rhea:RHEA:29515, Rhea:RHEA-COMP:11044, Rhea:RHEA-
CC COMP:12624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:58472, ChEBI:CHEBI:132510; EC=2.4.1.132;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:29519,
CC Rhea:RHEA-COMP:12624, Rhea:RHEA-COMP:12626, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132510,
CC ChEBI:CHEBI:132511; EC=2.4.1.257;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017628; AOW30324.1; -; Genomic_DNA.
DR RefSeq; XP_710571.2; XM_705479.2.
DR AlphaFoldDB; Q59LF2; -.
DR SMR; Q59LF2; -.
DR STRING; 237561.Q59LF2; -.
DR PRIDE; Q59LF2; -.
DR GeneID; 3647832; -.
DR KEGG; cal:CAALFM_C604030WA; -.
DR CGD; CAL0000176395; ALG2.
DR VEuPathDB; FungiDB:C6_04030W_A; -.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_030619_1_0_1; -.
DR InParanoid; Q59LF2; -.
DR OrthoDB; 1339573at2759; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q59LF2; -.
DR Proteomes; UP000000559; Chromosome 6.
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:0000033; F:alpha-1,3-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004378; F:GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102704; F:GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0033164; F:glycolipid 1,6-alpha-mannosyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR InterPro; IPR027054; ALG2.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR PANTHER; PTHR45918; PTHR45918; 1.
DR Pfam; PF13439; Glyco_transf_4; 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..443
FT /note="Alpha-1,3/1,6-mannosyltransferase ALG2"
FT /id="PRO_0000080263"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 443 AA; 50457 MW; 5B23EDA7B0288791 CRC64;
MSKRQENKKI AFIHPDLGIG GAERLVVDAA VGLQDFGHDI IIYTSHCDLT HCFEEVSSGQ
LKVSVHGDSL PTNLFGKLHI FFAILRQFYL VCWLIFTGTI KNYDYFIVDQ LSFCIPLLKM
FCNSNCQVLF YCHFPDQLLV RRTSFLKKLY RVPFDAIEEY TTGSSDQIVV NSNFTKQIFH
DTFKKLNHID PQVVYPCVDT ETIVDTNASS NSEVSKFFKD SPFFLSINRF ERSKNIELAI
KSFARMNKLM VTKAIKSFAR MNKLMVTNKK PRLVIAGGYD SRVAENVEYL AELSTLCDEL
NLINFTIRGK LIMMPPSVDV LFLPSISTQL KNSLIQQTEL LLYTPPREHF GIVPLEAMLA
KTPVLAINFG GPLETVVNYN GNNLDEATGY TETGDFTKWS KIIMKHYNLD ESTKIKLGEN
GRNRVINKFS RKKLAQSLDN ILN
