(data stored in ACNUC7421 zone)

SWISSPROT: ALG3_ASHGO

ID   ALG3_ASHGO              Reviewed;         432 AA.
AC   Q751K5;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   11-DEC-2019, entry version 89.
DE   RecName: Full=Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase;
DE            EC=2.4.1.258;
DE   AltName: Full=Asparagine-linked glycosylation protein 6;
DE   AltName: Full=Dol-P-Man-dependent alpha(1-3)-mannosyltransferase;
DE   AltName: Full=Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase;
GN   Name=ALG3; OrderedLocusNames=AGL299C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 179.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Adds the first Dol-P-Man derived mannose in an alpha-1,3
CC       linkage to Man(5)GlcNAc(2)-PP-Dol. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=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 + dolichyl beta-D-mannosyl phosphate =
CC         alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC         Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC         (1->4)-alpha-D-GlcNAc-diphosphodolichol + dolichyl phosphate + H(+);
CC         Xref=Rhea:RHEA:29527, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC         Rhea:RHEA-COMP:12627, Rhea:RHEA-COMP:12628, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132515,
CC         ChEBI:CHEBI:132516; EC=2.4.1.258;
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 ALG3 family. {ECO:0000305}.
DR   EMBL; AE016820; AAS54192.2; -; Genomic_DNA.
DR   RefSeq; NP_986368.2; NM_211430.2.
DR   STRING; 33169.AAS54192; -.
DR   CAZy; GT58; Glycosyltransferase Family 58.
DR   EnsemblFungi; AAS54192; AAS54192; AGOS_AGL299C.
DR   GeneID; 4622661; -.
DR   KEGG; ago:AGOS_AGL299C; -.
DR   HOGENOM; HOG000237555; -.
DR   InParanoid; Q751K5; -.
DR   KO; K03845; -.
DR   OMA; AAHVYIY; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:InterPro.
DR   GO; GO:0052925; F:dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR007873; Glycosyltransferase_ALG3.
DR   PANTHER; PTHR12646; PTHR12646; 1.
DR   Pfam; PF05208; ALG3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q751K5.
DR   SWISS-2DPAGE; Q751K5.
KW   Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..432
FT                   /note="Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-
FT                   mannosyltransferase"
FT                   /id="PRO_0000350919"
FT   TOPO_DOM        1..124
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        146..168
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..206
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        228..230
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..290
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        312..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        365..375
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        397..408
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        430..432
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   432 AA;  48634 MW;  146BB41AC4F9D865 CRC64;
     MSAAVPTTRA GTPPTLQCGW RSACGKLLDI ANYVIFSPEA SAVVMPVLVA WECVLLKLIV
     KHVPYTEIDY LAYMEQIWQI NNGERDYSKI EGGTGPLVYP AGHVLIHRLL ERATDGLQNV
     ARGQDIFTWL YLLTLVLQFG VYRMLRLPPW CIVLACLSKR LHSVYVLRLF NDGWTTLMMV
     VAVFLLLLAA RHPRLCLPAA LVYSAAVSIK MNALLYLPGV LVALFLLTRG HLLALALCGA
     VAVAWQVLVA ADFLSTHPAE YFATAFDFRR QFMYRWSVNW QLVGEQVFSH PTFHRCLLLS
     HIAILMLFFF TRYAAPRQPN WFRTAAAALR HPATAVLAAS PPRAHVAYVL LVSNFIGVLF
     ARSLHYQFLA WYHWTLPALL HWARMPCLLA LLWYVLHELC WDTYPPSSVA SATLYALNSA
     LLLLLYINGP PA
//

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