ALG3_ARATH
ID ALG3_ARATH Reviewed; 438 AA.
AC O82244; F4IM37; F4IM39; Q944H6;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=Alpha-1,3-mannosyltransferase ALG3;
DE AltName: Full=Asparagine-linked glycosylation protein 3;
DE Short=AtALG3;
DE AltName: Full=Not56-like protein;
GN Name=ALG3; OrderedLocusNames=At2g47760; ORFNames=F17A22.15;
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] (ISOFORM 1).
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).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=18567790; DOI=10.1105/tpc.108.060731;
RA Henquet M., Lehle L., Schreuder M., Rouwendal G., Molthoff J., Helsper J.,
RA van der Krol S., Bosch D.;
RT "Identification of the gene encoding the alpha1,3-mannosyltransferase
RT (ALG3) in Arabidopsis and characterization of downstream n-glycan
RT processing.";
RL Plant Cell 20:1652-1664(2008).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20356820; DOI=10.1093/glycob/cwq028;
RA Kajiura H., Seki T., Fujiyama K.;
RT "Arabidopsis thaliana ALG3 mutant synthesizes immature oligosaccharides in
RT the ER and accumulates unique N-glycans.";
RL Glycobiology 20:736-751(2010).
CC -!- FUNCTION: Required for N-linked oligosaccharide assembly. Adds the
CC sixth mannose residue in an alpha-1,3 linkage onto the dolichol-PP-
CC oligosaccharide precursor dolichol-PP-Man(5)GlcNAc(2).
CC {ECO:0000269|PubMed:18567790, ECO:0000269|PubMed:20356820}.
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 Evidence={ECO:0000269|PubMed:18567790};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18567790, ECO:0000269|PubMed:20356820}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:18567790,
CC ECO:0000269|PubMed:20356820}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O82244-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O82244-2; Sequence=VSP_041719;
CC Name=3;
CC IsoId=O82244-3; Sequence=VSP_041720;
CC -!- DISRUPTION PHENOTYPE: No obvious phenotype under normal and high
CC temperature or salt/osmotic stress conditions.
CC {ECO:0000269|PubMed:20356820}.
CC -!- MISCELLANEOUS: In the absence of ALG3 activity, the N-glycans
CC transferred to proteins are aberrant, indicating that the
CC oligosaccharyltransferase (OST) complex is substrate-tolerant.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 58 family.
CC {ECO:0000305}.
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DR EMBL; AC005309; AAC63631.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10884.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10885.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62178.1; -; Genomic_DNA.
DR EMBL; AF428424; AAL16193.1; -; mRNA.
DR EMBL; BT008303; AAP37662.1; -; mRNA.
DR PIR; B84919; B84919.
DR RefSeq; NP_001031556.1; NM_001036479.1. [O82244-2]
DR RefSeq; NP_001031557.1; NM_001036480.1. [O82244-3]
DR RefSeq; NP_182297.1; NM_130343.4. [O82244-1]
DR AlphaFoldDB; O82244; -.
DR STRING; 3702.AT2G47760.1; -.
DR CAZy; GT58; Glycosyltransferase Family 58.
DR PaxDb; O82244; -.
DR PRIDE; O82244; -.
DR ProteomicsDB; 244839; -. [O82244-1]
DR EnsemblPlants; AT2G47760.2; AT2G47760.2; AT2G47760. [O82244-2]
DR EnsemblPlants; AT2G47760.3; AT2G47760.3; AT2G47760. [O82244-3]
DR EnsemblPlants; AT2G47760.5; AT2G47760.5; AT2G47760. [O82244-1]
DR GeneID; 819388; -.
DR Gramene; AT2G47760.2; AT2G47760.2; AT2G47760. [O82244-2]
DR Gramene; AT2G47760.3; AT2G47760.3; AT2G47760. [O82244-3]
DR Gramene; AT2G47760.5; AT2G47760.5; AT2G47760. [O82244-1]
DR KEGG; ath:AT2G47760; -.
DR Araport; AT2G47760; -.
DR TAIR; locus:2043343; AT2G47760.
DR eggNOG; KOG2762; Eukaryota.
DR InParanoid; O82244; -.
DR OMA; PERYGIH; -.
DR PhylomeDB; O82244; -.
DR BRENDA; 2.4.1.258; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:O82244; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82244; baseline and differential.
DR Genevisible; O82244; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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:0000033; F:alpha-1,3-mannosyltransferase activity; IDA:TAIR.
DR GO; GO:0052925; F:dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IMP:TAIR.
DR InterPro; IPR007873; Glycosyltransferase_ALG3.
DR PANTHER; PTHR12646; PTHR12646; 1.
DR Pfam; PF05208; ALG3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..438
FT /note="Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-
FT mannosyltransferase"
FT /id="PRO_0000412588"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041719"
FT VAR_SEQ 381..438
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_041720"
FT CONFLICT 228
FT /note="V -> A (in Ref. 3; AAL16193/AAP37662)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 49243 MW; FBF2921BC5D9AC75 CRC64;
MAGASSPASL RASRSRRLGK ETNRSDLFKK PAVPFAFALI LADAILVALI IAYVPYTKID
WDAYMSQVSG FLGGERDYGN LKGDTGPLVY PAGFLYVYSA VQNLTGGEVY PAQILFGVLY
IVNLGIVLII YVKTDVVPWW ALSLLCLSKR IHSIFVLRLF NDCFAMTLLH ASMALFLYRK
WHLGMLVFSG AVSVKMNVLL YAPTLLLLLL KAMNIIGVVS ALAGAALVQI LVGLPFLITY
PVSYIANAFD LGRVFIHFWS VNFKFVPERV FVSKEFAVCL LIAHLFLLVA FANYKWCKHE
GGIIGFMRSR HFFLTLPSSL SFSDVSASRI ITKEHVVTAM FVGNFIGIVF ARSLHYQFYS
WYFYSLPYLL WRTPFPTWLR LIMFLGIELC WNVYPSTPSS SGLLLCLHLI ILVGLWLAPS
VDPYQLKEHP KSQIHKKA
