ALG6_ARATH
ID ALG6_ARATH Reviewed; 533 AA.
AC Q9FF17;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase;
DE EC=2.4.1.267;
DE AltName: Full=Asparagine-linked glycosylation protein 6 homolog;
DE AltName: Full=Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase;
DE AltName: Full=Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase;
GN OrderedLocusNames=At5g38460; ORFNames=MXI10.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Adds the first glucose residue to the lipid-linked
CC oligosaccharide precursor for N-linked glycosylation. Transfers glucose
CC from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked
CC oligosaccharide Man(9)GlcNAc(2)-PP-Dol (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->3)-alpha-
CC D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-
CC alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + H(+); Xref=Rhea:RHEA:30635, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9528, Rhea:RHEA-COMP:12631, Rhea:RHEA-
CC COMP:12632, ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:132520, ChEBI:CHEBI:132521; EC=2.4.1.267;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB005248; BAB09358.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94319.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94320.1; -; Genomic_DNA.
DR EMBL; AY035066; AAK59571.1; -; mRNA.
DR EMBL; AY056364; AAL07250.1; -; mRNA.
DR RefSeq; NP_001190434.1; NM_001203505.1.
DR RefSeq; NP_198662.1; NM_123207.2.
DR AlphaFoldDB; Q9FF17; -.
DR SMR; Q9FF17; -.
DR STRING; 3702.AT5G38460.2; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR PaxDb; Q9FF17; -.
DR PRIDE; Q9FF17; -.
DR ProteomicsDB; 244967; -.
DR EnsemblPlants; AT5G38460.1; AT5G38460.1; AT5G38460.
DR EnsemblPlants; AT5G38460.2; AT5G38460.2; AT5G38460.
DR GeneID; 833834; -.
DR Gramene; AT5G38460.1; AT5G38460.1; AT5G38460.
DR Gramene; AT5G38460.2; AT5G38460.2; AT5G38460.
DR KEGG; ath:AT5G38460; -.
DR Araport; AT5G38460; -.
DR TAIR; locus:2177431; AT5G38460.
DR eggNOG; KOG2575; Eukaryota.
DR HOGENOM; CLU_008110_3_0_1; -.
DR InParanoid; Q9FF17; -.
DR OMA; RQWYFNT; -.
DR OrthoDB; 595382at2759; -.
DR PhylomeDB; Q9FF17; -.
DR BioCyc; ARA:AT5G38460-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9FF17; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FF17; baseline and differential.
DR Genevisible; Q9FF17; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042281; F:dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR039488; ALG6.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR PANTHER; PTHR12413; PTHR12413; 1.
DR PANTHER; PTHR12413:SF1; PTHR12413:SF1; 1.
DR Pfam; PF03155; Alg6_Alg8; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..533
FT /note="Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-
FT 1,3-glucosyltransferase"
FT /id="PRO_0000174159"
FT TRANSMEM 42..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 61113 MW; 79DEC123A6387F26 CRC64;
MPKKKPAKHS GEDDITIPVS PQTGSSIDTW WWLTHKGTTT SFLCISLFAL LIRSAVTMYP
YSGAGIPPKF GDFEAQRHWM EITTNLPVID WYRNGTYNDL TYWGLDYPPL TAYQSYIHGI
FLRFFNPESV ALLSSRGHES YLGKLLMRWT VLSSDAFIFF PAALFFVLVY HRNRTRGGKS
EVAWHIAMIL LNPCLILIDH GHFQYNCISL GLTVGAIAAV LCESEVLTCV LFSLALSHKQ
MSAYFAPAFF SHLLGKCLRR KSPILSVIKL GIAVIVTFVI FWWPYVHSLD DFLMVLSRLA
PFERGIYEDY VANFWCTTSI LIKWKNLFTT QSLKSISLAA TILASLPSMV QQILSPSNEG
FLYGLLNSSM AFYLFSFQVH EKSILMPFLS ATLLALKLPD HFSHLTYYAL FSMFPLLCRD
KLLIPYLTLS FLFTVIYHSP GNHHAIQKTD VSFFSFKNFP GYVFLLRTHF FISVVLHVLY
LTIKPPQKYP FLFEALIMIL CFSYFIMFAF YTNYTQWTLS SHFGSSDKEK KQI
