GCS1_ARATH
ID GCS1_ARATH Reviewed; 852 AA.
AC F4HTM3; F4HTM2; O64796; Q8GWC8; Q940D4; Q9C5B4; Q9CAG7;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Mannosyl-oligosaccharide glucosidase GCS1;
DE EC=3.2.1.106;
DE AltName: Full=Alpha-glucosidase 1;
DE Short=Glucosidase 1;
DE AltName: Full=Protein KNOPF;
DE AltName: Full=Protein MUNCHKIN;
GN Name=GCS1; Synonyms=KNF, MUC, RSW; OrderedLocusNames=At1g67490;
GN ORFNames=F12B7.4, T1F15.4;
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 [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11230125; DOI=10.1093/emboj/20.5.1010;
RA Boisson M., Gomord V., Audran C., Berger N., Dubreucq B., Granier F.,
RA Lerouge P., Faye L., Caboche M., Lepiniec L.;
RT "Arabidopsis glucosidase I mutants reveal a critical role of N-glycan
RT trimming in seed development.";
RL EMBO J. 20:1010-1019(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11901167; DOI=10.1083/jcb.200111093;
RA Gillmor C.S., Poindexter P., Lorieau J., Palcic M.M., Somerville C.;
RT "Alpha-glucosidase I is required for cellulose biosynthesis and
RT morphogenesis in Arabidopsis.";
RL J. Cell Biol. 156:1003-1013(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=17138701; DOI=10.1105/tpc.105.036400;
RA Saint-Jore-Dupas C., Nebenfuehr A., Boulaflous A., Follet-Gueye M.-L.,
RA Plasson C., Hawes C., Driouich A., Faye L., Gomord V.;
RT "Plant N-glycan processing enzymes employ different targeting mechanisms
RT for their spatial arrangement along the secretory pathway.";
RL Plant Cell 18:3182-3200(2006).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF GLY-504.
RC STRAIN=cv. Columbia;
RX PubMed=18503769; DOI=10.1016/j.febslet.2008.05.019;
RA Furumizu C., Komeda Y.;
RT "A novel mutation in KNOPF uncovers the role of alpha-glucosidase I during
RT post-embryonic development in Arabidopsis thaliana.";
RL FEBS Lett. 582:2237-2241(2008).
RN [8]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF 1-MET--ILE-13 AND
RP 6-ARG--ARG-12.
RX PubMed=19995436; DOI=10.1186/1471-2229-9-144;
RA Boulaflous A., Saint-Jore-Dupas C., Herranz-Gordo M.-C.,
RA Pagny-Salehabadi S., Plasson C., Garidou F., Kiefer-Meyer M.-C.,
RA Ritzenthaler C., Faye L., Gomord V.;
RT "Cytosolic N-terminal arginine-based signals together with a luminal signal
RT target a type II membrane protein to the plant ER.";
RL BMC Plant Biol. 9:144-144(2009).
CC -!- FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from the
CC Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor. Required for the
CC accumulation of seed storage proteins, the formation of protein bodies,
CC cell differentiation, cellulose biosynthesis and organization (in cell
CC walls), cell shape determination and organization (e.g. epidermal
CC cells), and embryo development. Involved in root development.
CC {ECO:0000269|PubMed:11230125, ECO:0000269|PubMed:11901167,
CC ECO:0000269|PubMed:18503769}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-
CC (1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose +
CC N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-
CC D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-
CC beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-
CC [protein]; Xref=Rhea:RHEA:55988, Rhea:RHEA-COMP:12806, Rhea:RHEA-
CC COMP:14355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59082,
CC ChEBI:CHEBI:132537; EC=3.2.1.106;
CC -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17138701, ECO:0000269|PubMed:19995436}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:17138701,
CC ECO:0000269|PubMed:19995436}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4HTM3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4HTM3-2; Sequence=VSP_044957;
CC -!- TISSUE SPECIFICITY: Constitutively expressed in roots, stems, leaves,
CC flowers and siliques. {ECO:0000269|PubMed:11230125,
CC ECO:0000269|PubMed:11901167}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. Impaired glucosidase activity
CC leading to a strongly reduced cellulose content. Abnormal shrunken
CC seeds with embryos arrested at the heart stage. Low levels of storage
CC proteins in seeds accompanied by a loss of protein bodies, abnormal
CC cell enlargement and occasional cell wall disruptions.
CC {ECO:0000269|PubMed:11230125, ECO:0000269|PubMed:11901167}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18786.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG52297.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ278990; CAC34725.1; -; Genomic_DNA.
DR EMBL; AY055858; AAL17718.1; -; mRNA.
DR EMBL; AC004393; AAC18786.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011020; AAG52297.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34653.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34654.1; -; Genomic_DNA.
DR EMBL; AK118927; BAC43508.1; -; mRNA.
DR PIR; C96698; C96698.
DR PIR; T02156; T02156.
DR RefSeq; NP_001031247.1; NM_001036170.1. [F4HTM3-2]
DR RefSeq; NP_176916.2; NM_105416.5. [F4HTM3-1]
DR AlphaFoldDB; F4HTM3; -.
DR SMR; F4HTM3; -.
DR STRING; 3702.AT1G67490.1; -.
DR CAZy; GH63; Glycoside Hydrolase Family 63.
DR iPTMnet; F4HTM3; -.
DR PaxDb; F4HTM3; -.
DR PRIDE; F4HTM3; -.
DR ProteomicsDB; 222177; -. [F4HTM3-1]
DR EnsemblPlants; AT1G67490.1; AT1G67490.1; AT1G67490. [F4HTM3-1]
DR EnsemblPlants; AT1G67490.2; AT1G67490.2; AT1G67490. [F4HTM3-2]
DR GeneID; 843070; -.
DR Gramene; AT1G67490.1; AT1G67490.1; AT1G67490. [F4HTM3-1]
DR Gramene; AT1G67490.2; AT1G67490.2; AT1G67490. [F4HTM3-2]
DR KEGG; ath:AT1G67490; -.
DR Araport; AT1G67490; -.
DR TAIR; locus:2008778; AT1G67490.
DR eggNOG; KOG2161; Eukaryota.
DR HOGENOM; CLU_007380_1_0_1; -.
DR InParanoid; F4HTM3; -.
DR OMA; YWKAPLY; -.
DR OrthoDB; 278028at2759; -.
DR BRENDA; 3.2.1.106; 399.
DR UniPathway; UPA00280; -.
DR PRO; PR:F4HTM3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HTM3; baseline and differential.
DR Genevisible; F4HTM3; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IDA:TAIR.
DR GO; GO:0004573; F:Glc3Man9GlcNAc2 oligosaccharide glucosidase activity; IBA:GO_Central.
DR GO; GO:0009913; P:epidermal cell differentiation; IMP:TAIR.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0010053; P:root epidermal cell differentiation; IMP:TAIR.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.110; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR031335; Glyco_hydro_63_C.
DR InterPro; IPR031631; Glyco_hydro_63N.
DR InterPro; IPR038518; Glyco_hydro_63N_sf.
DR InterPro; IPR004888; Glycoside_hydrolase_63.
DR PANTHER; PTHR10412; PTHR10412; 1.
DR Pfam; PF03200; Glyco_hydro_63; 1.
DR Pfam; PF16923; Glyco_hydro_63N; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Glycosidase;
KW Hydrolase; Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..852
FT /note="Mannosyl-oligosaccharide glucosidase GCS1"
FT /id="PRO_0000420920"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..852
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..150
FT /note="Required for endoplasmic reticulum targeting"
FT REGION 574..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..12
FT /note="Endoplasmic reticulum targeting"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 126..209
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044957"
FT MUTAGEN 1..13
FT /note="Missing: Abnormal subcellular location in the Golgi
FT apparatus."
FT /evidence="ECO:0000269|PubMed:19995436"
FT MUTAGEN 6..12
FT /note="RRSARGR->AASAAGA,LLSALGL: Abnormal subcellular
FT location in the Golgi apparatus."
FT /evidence="ECO:0000269|PubMed:19995436"
FT MUTAGEN 504
FT /note="G->D: In knf-101/muc; semi-dwarf plants with
FT abnormal cells shapes and altered epidermal cells
FT arrangements, as well as short and hairy roots."
FT /evidence="ECO:0000269|PubMed:18503769"
FT CONFLICT 373
FT /note="K -> N (in Ref. 1; CAC34725)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="E -> Q (in Ref. 2; AAL17718)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="K -> R (in Ref. 5; BAC43508)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="L -> R (in Ref. 1; CAC34725)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="V -> A (in Ref. 1; CAC34725)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="D -> N (in Ref. 1; CAC34725)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="L -> Q (in Ref. 5; BAC43508)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 852 AA; 97634 MW; E08C0EF09196347C CRC64;
MTGASRRSAR GRIKSSSLSP GSDEGSAYPP SIRRGKGKEL VSIGAFKTNL KILVGLIILG
IIVIYFVINR LVRHGLLFDE SQKPRVITPF PAPKVMDLSM FQGEHKESLY WGTYRPHVYF
GVRARTPLSL VAGLMWLGVK DEMYVMRHFC ENSDDLSTFG WREHNGRDYG RQELVENDMV
IETSFVKSKG DGLGYGGDWA VRIDVKNKGL NDDVKRSAHL FFYLADEGGN VLNLGQDGLD
FQGSSLLVSG SREDVGDWQI HLKSQNQLET HYSGFKTPHI YNLSDLVQQN LALQARKFGR
LQLSDTSEDS SNIYIFQISG RLPFTIDIPF ISGIKGESSN VEKRLTSLTG LPLSDLLKKK
HQEFDAKFNE CFKLSEKHDS ETLGVGRTAI ANMLGGIGYF YGQSKIYVPK STQPGSRDNF
LLYWPAELYT AVPSRPFFPR GFLWDEGFHQ LLIWRWDIRI TLDIVGHWLD LLNIDGWIPR
EQILGAEALS KVPEEFVVQY PSNGNPPTLF LVIRDLIDAI RMEKFVASEK DEVLSFLERA
SVRLDAWFQW FNTSQKGKEI GSYFWHGRDN TTTQELNPKT LSSGLDDYPR ASHPSEDERH
VDLRCWMYLA ADCMHSITEL LGKEDKLSKE NYNSTVKLLS NFNLLNQMHY DSDYGAYFDF
GNHTEKVKLI WKEVIQENGQ LSRQLVRKTF GKPKLKLVPH LGYVSFFPFM SRIIPPDSPI
LEKQLDLISN RSILWSDYGL VSLAKTSSMY MKRNTEHDAP YWRGPIWMNM NYMILSSLYH
YSIVDGPYRE KSKAIYTELR SNLIRNVVRN YYETGYIWEQ YDQVKGTGKG TRLFTGWSAL
TLLIMSEDYP IF
