ALG11_ARATH
ID ALG11_ARATH Reviewed; 463 AA.
AC Q9XEE9; F4IH01; Q0WT32; Q7DNH4;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase;
DE EC=2.4.1.131;
DE AltName: Full=Alpha-1,2-mannosyltransferase ALG11;
DE AltName: Full=Asparagine-linked glycosylation protein 11;
DE AltName: Full=Protein LEAF WILTING 3;
GN Name=ALG11; Synonyms=LEW3; OrderedLocusNames=At2g40190; ORFNames=T07M07.7;
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].
RX PubMed=10207155;
RA Wang M.L., Belmonte S., Kim U., Dolan M., Morris J.W., Goodman H.M.;
RT "A cluster of ABA-regulated genes on Arabidopsis thaliana BAC T07M07.";
RL Genome Res. 9:325-333(1999).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Morosawa T.,
RA Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K.,
RA Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K.,
RA Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA Hayashizaki Y., Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-463.
RA Cheuk R., Chen H., Kim C.J., Shinn P., Bowser L., Carninci P., Dale J.M.,
RA Hayashizaki Y., Ishida J., Jones T., Kamiya A., Karlin-Neumann G.,
RA Kawai J., Lam B., Lin J., Miranda M., Narusaka M., Nguyen M., Onodera C.S.,
RA Palm C.J., Quach H.L., Sakurai T., Satou M., Seki M., Southwick A.,
RA Toriumi M., Wong C., Wu H.C., Yamada K., Yu G., Shinozaki K., Davis R.W.,
RA Theologis A., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-148,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19732381; DOI=10.1111/j.1365-313x.2009.04013.x;
RA Zhang M., Henquet M., Chen Z., Zhang H., Zhang Y., Ren X., van der Krol S.,
RA Gonneau M., Bosch D., Gong Z.;
RT "LEW3, encoding a putative alpha-1,2-mannosyltransferase (ALG11) in N-
RT linked glycoprotein, plays vital roles in cell-wall biosynthesis and the
RT abiotic stress response in Arabidopsis thaliana.";
RL Plant J. 60:983-999(2009).
CC -!- FUNCTION: Required for N-linked oligosaccharide assembly. Has a role in
CC the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core
CC oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.
CC {ECO:0000269|PubMed:19732381}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=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 + 2 GDP-alpha-
CC D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + 2 GDP + 2 H(+); Xref=Rhea:RHEA:29523,
CC Rhea:RHEA-COMP:12626, Rhea:RHEA-COMP:12627, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132511,
CC ChEBI:CHEBI:132515; EC=2.4.1.131;
CC Evidence={ECO:0000269|PubMed:19732381};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19732381}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19732381}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9XEE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9XEE9-2; Sequence=VSP_041714;
CC -!- TISSUE SPECIFICITY: Expressed in shoots, leaves, sepals, filaments,
CC siliques, stems, roots and guard cells. {ECO:0000269|PubMed:19732381}.
CC -!- DISRUPTION PHENOTYPE: Lethality. {ECO:0000269|PubMed:19732381}.
CC -!- MISCELLANEOUS: In the absence of ALG11 activity, no N-glycans are
CC produced and transferred to proteins.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25934.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF085279; AAD25934.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09794.1; -; Genomic_DNA.
DR EMBL; AK227731; BAE99716.1; -; mRNA.
DR EMBL; BT009712; AAP88346.1; -; mRNA.
DR PIR; D84826; D84826.
DR RefSeq; NP_181548.2; NM_129577.5. [Q9XEE9-1]
DR AlphaFoldDB; Q9XEE9; -.
DR SMR; Q9XEE9; -.
DR STRING; 3702.AT2G40190.1; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR PaxDb; Q9XEE9; -.
DR PRIDE; Q9XEE9; -.
DR ProteomicsDB; 245070; -. [Q9XEE9-1]
DR EnsemblPlants; AT2G40190.1; AT2G40190.1; AT2G40190. [Q9XEE9-1]
DR GeneID; 818610; -.
DR Gramene; AT2G40190.1; AT2G40190.1; AT2G40190. [Q9XEE9-1]
DR KEGG; ath:AT2G40190; -.
DR Araport; AT2G40190; -.
DR TAIR; locus:2065080; AT2G40190.
DR eggNOG; KOG1387; Eukaryota.
DR HOGENOM; CLU_017896_2_0_1; -.
DR InParanoid; Q9XEE9; -.
DR OMA; RFNIHLH; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9XEE9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9XEE9; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; IMP:TAIR.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR CDD; cd03806; GT4_ALG11-like; 1.
DR InterPro; IPR038013; ALG11.
DR InterPro; IPR031814; ALG11_N.
DR InterPro; IPR001296; Glyco_trans_1.
DR PANTHER; PTHR45919; PTHR45919; 1.
DR Pfam; PF15924; ALG11_N; 1.
DR Pfam; PF00534; Glycos_transf_1; 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..463
FT /note="GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-
FT mannosyltransferase"
FT /id="PRO_0000412585"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_041714"
FT MUTAGEN 148
FT /note="G->E: In lew3; deficiency in N-glycosylation leading
FT to dwarf phenotype, reduced fertility and impaired
FT cellulose synthesis."
FT /evidence="ECO:0000269|PubMed:19732381"
SQ SEQUENCE 463 AA; 52573 MW; 7092C34149CD4AE1 CRC64;
MAIYFILYTL LTIIFAVSLS LFLSVINARK SRKRAVGFFH PYTNDGGGGE RVLWCAVKAI
QEENPDLDCV IFTGDHDSSS DSLARRAVDR FGVHLQSPPK VIHLNKRKWI EESTYPHFTM
IGQSLGSVYL AWEALRMFTP LYFLDTSGYA FTYPLARIFG CKVVCYTHYP TISLDMISRV
RQRNSMYNND ASIAKSNWLS TCKLVYYRAF SWMYGMVGSC THLAMVNSSW TKSHIEVLWR
IPERITRVYP PCDTSGLQAF PLERSSDPPK IISVAQFRPE KAHMLQLEAF SLALEKLDAD
VPRPKLQFVG SCRNNSDEER LQKLKDRAVE LKVDGDVQFY KNAMYRELVE LLGNAVAGLH
GMIDEHFGIS VVEYMAAGAI PIAHNSAGPK MDIVLEEDGQ KTGFLAETVE EYAEAILEIV
KMNETERLKM AESARKRAAR FSEQRFCEDF KTAIRPIFTG PLK
