ID   ALG2_RHIPU              Reviewed;         455 AA.
AC   O94738;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=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;
OS   Rhizomucor pusillus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Rhizomucor.
OX   NCBI_TaxID=4840;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND MUTAGENESIS OF GLY-368.
RX   PubMed=9795208; DOI=10.1016/s0378-1119(98)00456-9;
RA   Yamazaki H., Shiraishi N., Takeuchi K., Ohnishi Y., Horinouchi S.;
RT   "Characterization of alg2 encoding a mannosyltransferase in the zygomycete
RT   fungus Rhizomucor pusillus.";
RL   Gene 221:179-184(1998).
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.
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: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR   EMBL; AB015055; BAA34297.1; -; mRNA.
DR   EMBL; AB015054; BAA34296.1; -; Genomic_DNA.
DR   AlphaFoldDB; O94738; -.
DR   SMR; O94738; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   UniPathway; UPA00378; -.
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; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosyltransferase; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..455
FT                   /note="Alpha-1,3/1,6-mannosyltransferase ALG2"
FT                   /id="PRO_0000080268"
FT   TRANSMEM        73..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        434..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         368
FT                   /note="G->R: Temperature-sensitive phenotype."
FT                   /evidence="ECO:0000269|PubMed:9795208"
SQ   SEQUENCE   455 AA;  51222 MW;  8128C7C2365E46EF CRC64;
     MTSKSLNVAF IHPDLGIGGA ERLVVDAAVG IQKKGHQVIF YTSHHDPNHC FEETRDGTLK
     VQVRGDWLPR TIFGRFYILC AILRQFVLVA SLILWERHSY DIFFVDQLSA CVPLLKWFTT
     AKILFYCHFP DKLLTQRNST IKKLYRAPVD KMEELTTGMS DLIAVNSGFT AGMFKKSFPS
     VHQTPQILYP PINFDAYDRP VDRNDPTVKI LETDKRVLLS INRFERKKNV ELALRAFAAL
     KIKNMVPKDV FANYRLVLAG GYDKRVRENV EYLEELDQLA TEEFGLQTFT IHPSSAAADV
     PADAQVVFLC SFNDAQRTFL LDQAKLLLYT PSNEHFGITP VEGMYASVPV IAVNTGGPVE
     TVKNKETGLL LPSDPDVWAE GIRDFIIEKY NGKQMGQHGR QHVQSKFSLP AFADRLEAMM
     IELETSTPDQ SSSGAVYLLG AIGVLFACII YCIKQ