ALG3_KOMPG
ID ALG3_KOMPG Reviewed; 465 AA.
AC Q6DNA2; C4R8P8;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 78.
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=PAS_chr4_0712;
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=15033937; DOI=10.1093/glycob/cwh023;
RA Davidson R.C., Nett J.H., Renfer E., Li H., Stadheim T.A., Miller B.J.,
RA Miele R.G., Hamilton S.R., Choi B.-K., Mitchell T.I., Wildt S.;
RT "Functional analysis of the ALG3 gene encoding the Dol-P-Man: Man5GlcNAc2-
RT PP-Dol mannosyltransferase enzyme of P. pastoris.";
RL Glycobiology 14:399-407(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864;
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
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 ECO:0000269|PubMed:15033937}.
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; AY653304; AAT72073.1; -; Genomic_DNA.
DR EMBL; FN392322; CAY71973.1; -; Genomic_DNA.
DR RefSeq; XP_002494152.1; XM_002494107.1.
DR AlphaFoldDB; Q6DNA2; -.
DR STRING; 644223.Q6DNA2; -.
DR CAZy; GT58; Glycosyltransferase Family 58.
DR EnsemblFungi; CAY71973; CAY71973; PAS_chr4_0712.
DR GeneID; 8200607; -.
DR KEGG; ppa:PAS_chr4_0712; -.
DR eggNOG; KOG2762; Eukaryota.
DR HOGENOM; CLU_035382_3_0_1; -.
DR InParanoid; Q6DNA2; -.
DR OMA; DWETYMI; -.
DR BRENDA; 2.4.1.258; 4827.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000314; 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..465
FT /note="Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-
FT mannosyltransferase"
FT /id="PRO_0000350933"
FT TOPO_DOM 1..33
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..120
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..211
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..306
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..407
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..465
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CONFLICT 188
FT /note="Y -> S (in Ref. 1; AAT72073)"
FT /evidence="ECO:0000305"
FT CONFLICT 198..203
FT /note="FILSLI -> LSVPD (in Ref. 1; AAT72073)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 53029 MW; 588C159AC7827F1C CRC64;
MPPIEPAERP KLTLKNVIGD LVALIQNVLF NPDFSVFVAP LLWLADSIVI KVIIGTVSYT
DIDFSSYMQQ IFKIRQGELD YSNIFGDTGP LVYPAGHVHA YSVLSWYSDG GEDVSFVQQA
FGWLYLGCLL LSISSYFFSG LGKIPPVYFV LLVASKRLHS IFVLRLFNDC LTTFLMLATI
IILQQASYWR KDGTTIPFIL SLIAADTYSL AISVKMNALL YLPAFLLLIY LICDENLIKA
LAPVLVLILV QVGVGYSFIL PLHYDDQANE IRSAYFRQAF DFSRQFLYKW TVNWRFLSQE
TFNNVHFHQL LFALHIITLV LFILKFLSPK NIGKPLGRFV LDIFKFWKPT LSPTNIINDP
ERSPDFVYTV MATTNLIGVL FARSLHYQFL SWYAFSLPYL LYKARLNFIA SIIVYAAHEY
CWLVFPATEQ SSALLVSILL LILILIFTNE QLFPSQSVPA EKKNT
