ALG3_PICST
ID ALG3_PICST Reviewed; 477 AA.
AC A3LTB7;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 74.
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; ORFNames=PICST_58095;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a
CC dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[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 + 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}.
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DR EMBL; CP000498; ABN66377.2; -; Genomic_DNA.
DR RefSeq; XP_001384406.2; XM_001384369.1.
DR AlphaFoldDB; A3LTB7; -.
DR STRING; 4924.XP_001384406.2; -.
DR CAZy; GT58; Glycosyltransferase Family 58.
DR EnsemblFungi; ABN66377; ABN66377; PICST_58095.
DR GeneID; 4838968; -.
DR KEGG; pic:PICST_58095; -.
DR eggNOG; KOG2762; Eukaryota.
DR HOGENOM; CLU_035382_3_0_1; -.
DR InParanoid; A3LTB7; -.
DR OMA; PERYGIH; -.
DR OrthoDB; 774318at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002258; Chromosome 4.
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: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;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..477
FT /note="Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-
FT mannosyltransferase"
FT /id="PRO_0000350931"
FT TOPO_DOM 1..48
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..172
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..316
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..406
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..477
FT /note="Lumenal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 477 AA; 53790 MW; 54DA89F304148739 CRC64;
MSEPESSVAN NDGESTQAPQ LAELTLKNVL GDIVNGVHFI IFDPLGNRFV VPVIILLTSI
ITKVIITKVP YTEIDFVTYM QQIQLVNQGE IDYAEISGDT GPIVYPAGFV QIYQWLYSQT
NGGADIATGQ SIFGYLMTAT VVFVCVAYTM SPTTKPWVLF LLLGSKRLYS IYVLRLFNDC
FTTAAMVGVT VFLQQGSYWY STSSFISFLF AIVGADLFSI AISIKMNALL YLPAVVIIAY
FLVGENILLF AIVLAIVPLV QILVGWKFLL PLFDDEAASQ IRWNYINNAF NFGRKFLFKW
TVNWRFIGEE TFLSDKFSIL LMGGHIVVLL FFIFTRFLNS KVTGKSIWQL IKDAFKPSST
ISSNNKLIDY NVGPKLILLI LATTNVIGVL FSRSLHYQFL SWYCWQLPFL LHSTGWNFIV
CLVLWGAHEW TWNVYPSTVA SSLVLVGILS SVLVGTWRNE AVWFEENNVV DDEKKNE
