ALG10_ARATH
ID ALG10_ARATH Reviewed; 509 AA.
AC Q8L638; Q9LZ85;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase {ECO:0000305};
DE EC=2.4.1.256 {ECO:0000269|PubMed:21707802};
DE AltName: Full=Alpha-1,2-glucosyltransferase ALG10 homolog {ECO:0000305};
DE AltName: Full=Protein HOMOLOG OF YEAST ALG10 {ECO:0000303|PubMed:21707802};
GN Name=ALG10 {ECO:0000303|PubMed:21707802};
GN OrderedLocusNames=At5g02410 {ECO:0000312|Araport:AT5G02410};
GN ORFNames=T1E22_170 {ECO:0000312|EMBL:CAB85546.1};
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 MRNA].
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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].
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21707802; DOI=10.1111/j.1365-313x.2011.04688.x;
RA Farid A., Pabst M., Schoberer J., Altmann F., Gloessl J., Strasser R.;
RT "Arabidopsis thaliana alpha1,2-glucosyltransferase (ALG10) is required for
RT efficient N-glycosylation and leaf growth.";
RL Plant J. 68:314-325(2011).
CC -!- FUNCTION: Adds the third 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(2)Man(9)GlcNAc(2)-PP-Dol. Can complement an ALG10-
CC deficient yeast mutant. {ECO:0000269|PubMed:21707802}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-
CC alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate
CC + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + H(+); Xref=Rhea:RHEA:29543, Rhea:RHEA-COMP:9517,
CC Rhea:RHEA-COMP:9528, Rhea:RHEA-COMP:12633, Rhea:RHEA-COMP:12634,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:132522, ChEBI:CHEBI:132523; EC=2.4.1.256;
CC Evidence={ECO:0000269|PubMed:21707802};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21707802}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Small plants with reduced leaf size.
CC Hypoglycosylation of glycoproteins leading to ER stress and activation
CC of the unfolded protein response (UPR). Increased sensitivity to salt
CC stress. {ECO:0000269|PubMed:21707802}.
CC -!- SIMILARITY: Belongs to the ALG10 glucosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB85546.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KJ138711; AHL38651.1; -; mRNA.
DR EMBL; AL162874; CAB85546.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90469.1; -; Genomic_DNA.
DR EMBL; AY099540; AAM20392.1; -; mRNA.
DR EMBL; BT002117; AAN72128.1; -; mRNA.
DR PIR; T48262; T48262.
DR RefSeq; NP_195861.2; NM_120319.4.
DR AlphaFoldDB; Q8L638; -.
DR STRING; 3702.AT5G02410.1; -.
DR CAZy; GT59; Glycosyltransferase Family 59.
DR TCDB; 9.B.231.1.5; the die2/alg10 glycosyl transferase (die2/alg10) family.
DR PaxDb; Q8L638; -.
DR PRIDE; Q8L638; -.
DR ProteomicsDB; 244984; -.
DR EnsemblPlants; AT5G02410.1; AT5G02410.1; AT5G02410.
DR GeneID; 831764; -.
DR Gramene; AT5G02410.1; AT5G02410.1; AT5G02410.
DR KEGG; ath:AT5G02410; -.
DR Araport; AT5G02410; -.
DR TAIR; locus:2180162; AT5G02410.
DR eggNOG; KOG2642; Eukaryota.
DR HOGENOM; CLU_017053_1_0_1; -.
DR InParanoid; Q8L638; -.
DR OMA; INKTFQW; -.
DR OrthoDB; 476469at2759; -.
DR PhylomeDB; Q8L638; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q8L638; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L638; baseline and differential.
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:0106073; F:dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046527; F:glucosyltransferase activity; IMP:TAIR.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR InterPro; IPR016900; Alg10.
DR PANTHER; PTHR12989; PTHR12989; 1.
DR Pfam; PF04922; DIE2_ALG10; 1.
DR PIRSF; PIRSF028810; Alpha1_2_glucosyltferase_Alg10; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-
FT glucosyltransferase"
FT /id="PRO_5005703628"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..57
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..124
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..285
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..355
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..428
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..509
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 210..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 509 AA; 58439 MW; CAEBD9F82E2548E7 CRC64;
MGKLAVAAIT SLWVIPMSII VNHIVPEPYM DEIFHVPQAQ QYCNGNFRSW DPMITTPPGL
YYLSLAHVAS LFPGMLLMEN TSQSFSEACS TSVLRSTNAV SAVLCGVLVY EIIRFLGPNL
SDRKATFMAL VMSLYPLHWF FTFLYYTDVA SLTAVLAMYL TCLKRRYVLS ALFGTLAVFI
RQTNVVWMLF VACSGILDFT LDSSKQKGKQ EVNQELHQSS NKKGATLRSN LRKRKSDISS
DTSDPFNHGQ TVPSTEDTSD LVYDIYTVIS TSWNLKWRIL IKFSPFIFVV VAFGIFILWN
GGIVLGAKEA HVVSLHFAQI MYFSLVSALF TAPLHFSVNQ LRHQFHQLHR NWSLSLILTL
VALVAGFVSV HFFSLAHPYL LADNRHYPFY LWRKIINAHW LMKYILVPVY VYSWFSILTL
LAKTRRQTWI LVYFLATCGV LVPTPLIEFR YYTIPFYLFM LHSCVRSSSF ATWLLIGTIF
VSINVFTMAM FLFRPFKWSH EDGVQRFIW
