ALG8_ARATH
ID ALG8_ARATH Reviewed; 506 AA.
AC O80505;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase;
DE EC=2.4.1.265;
DE AltName: Full=Asparagine-linked glycosylation protein 8 homolog;
DE AltName: Full=Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase;
DE AltName: Full=Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase;
GN OrderedLocusNames=At2g44660; ORFNames=F16B22.15;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] OF 415-506.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
CC -!- FUNCTION: Adds the second 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 Glc(1)Man(9)GlcNAc(2)-PP-Dol (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-
CC Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->6)]-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:31307, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9528,
CC Rhea:RHEA-COMP:12632, Rhea:RHEA-COMP:12633, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57525, ChEBI:CHEBI:57683, ChEBI:CHEBI:132521,
CC ChEBI:CHEBI:132522; EC=2.4.1.265;
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 ALG6/ALG8 glucosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC27468.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003672; AAC27468.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10452.1; -; Genomic_DNA.
DR EMBL; BX842470; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T01593; T01593.
DR RefSeq; NP_181994.5; NM_130030.5.
DR AlphaFoldDB; O80505; -.
DR SMR; O80505; -.
DR STRING; 3702.AT2G44660.1; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR PaxDb; O80505; -.
DR PRIDE; O80505; -.
DR ProteomicsDB; 245067; -.
DR EnsemblPlants; AT2G44660.1; AT2G44660.1; AT2G44660.
DR GeneID; 819074; -.
DR Gramene; AT2G44660.1; AT2G44660.1; AT2G44660.
DR KEGG; ath:AT2G44660; -.
DR Araport; AT2G44660; -.
DR TAIR; locus:2042411; AT2G44660.
DR eggNOG; KOG2576; Eukaryota.
DR HOGENOM; CLU_022045_1_1_1; -.
DR InParanoid; O80505; -.
DR OMA; WDTFVGA; -.
DR OrthoDB; 595382at2759; -.
DR PhylomeDB; O80505; -.
DR BioCyc; ARA:AT2G44660-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:O80505; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80505; baseline and differential.
DR Genevisible; O80505; 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:0042283; F:dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IBA:GO_Central.
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; IPR039487; ALG8.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR PANTHER; PTHR12413; PTHR12413; 1.
DR PANTHER; PTHR12413:SF2; PTHR12413:SF2; 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..506
FT /note="Probable dolichyl pyrophosphate Glc1Man9GlcNAc2
FT alpha-1,3-glucosyltransferase"
FT /id="PRO_0000174166"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 501
FT /note="L -> P (in Ref. 3; BX842470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 58222 MW; C23639FAE29F1413 CRC64;
MDHREKSDRR LLLWFFAVAT AVKLLLIPSS RSTDFEVHRN WLAITNSLPL TKWYFDETSQ
WTLDYPPFFA YFERFLSIFA RLVDPRIVDL QSGLDYNAES VIYFQRISVI VSDLCLLYGV
YRLTRKLEPL KRNLICALVI WSPGLLIVDH IHFQYNGFLL GWLLLSISFL QEGRDLLGGF
LFAVLLCFKH LFAVTAPVYF VYLLRHYCWS GLVTGFRRLV TIGAVVVAVF AAAYGPFIYH
GQIQQVISRM FPFGRGLCHA YWAPNFWVFY IILDKGLAVL LRKLGYEIQI PSASFTGGLV
GDSSPFAVLP QITPLTTFAM VLLAISPCLI KAWKKPHSGL VARWVAYAYT CGFLFGWHVH
EKASLHFTIP LAIVAVQSLE DAKHYFLVSI VSCYSLYPLL YEPQEYPIKV LLLLLHSVVM
WLGFAAQYTD YKAQKKETSE IKSKFRIGCF EKSYLMGLII VEIVSQFLHP YFLGDKLPFL
PLMLISTYCT VGIMYSWIWQ LRKILT
