ALG2_DEBHA
ID ALG2_DEBHA Reviewed; 476 AA.
AC Q6BVA4;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 101.
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=DEHA2C04158g;
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: 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 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; CAG85910.2; -; Genomic_DNA.
DR RefSeq; XP_457865.2; XM_457865.1.
DR AlphaFoldDB; Q6BVA4; -.
DR SMR; Q6BVA4; -.
DR STRING; 4959.XP_457865.2; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblFungi; CAG85910; CAG85910; DEHA2C04158g.
DR GeneID; 2900691; -.
DR KEGG; dha:DEHA2C04158g; -.
DR VEuPathDB; FungiDB:DEHA2C04158g; -.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_030619_1_0_1; -.
DR InParanoid; Q6BVA4; -.
DR OMA; TIFTSHC; -.
DR OrthoDB; 1339573at2759; -.
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: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:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..476
FT /note="Alpha-1,3/1,6-mannosyltransferase ALG2"
FT /id="PRO_0000080265"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 476 AA; 54443 MW; 9872AE8A1F3E3189 CRC64;
MSKKLGNNSK KIAFVHPDLG IGGAERLVVD AAVGLQELEN EVTIYTSHCD KKHCFEEVSS
NLLDVEVYGD FFPTNVLKRF HILFAIIRQF YLVLALIFTG KIKQYDYFIV DQLSFCIPLL
CCFSRPECKI LFYCHFPDQL LALKGGFLKR FYRMPFDLIE EWTTGISDQI VVNSKFTKGI
FHKTFKGLKN IEPGVIYPCV DLNSATDTEE DKLMDEEVNE FFKGGKFFLS VNRFERKKNI
GLAIQSFAKF KAQLPKNVSE DNRIKPRLVV AGGFDPRVLE NVEYLQELNG LSESLNLKCF
TIRGKLLIIP PATDILFLPS IKSSLKKSLI KNAELLLYTP SFEHFGIVPV ESMLFKTPVL
SANNGGPLES IVHFTSDNIA TATGYSQEPN DELWSKTMHT FYTELDEATK LKLGENGLTR
VHELFSRHQM SEAFMQNLIQ SNSKDEEKGI LYGILKMWRI ELLFVLISYY LVRLYK
