ENAS2_ARATH
ID ENAS2_ARATH Reviewed; 701 AA.
AC Q9SRL4;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cytosolic endo-beta-N-acetylglucosaminidase 2 {ECO:0000305};
DE Short=ENGase 2 {ECO:0000305};
DE EC=3.2.1.96 {ECO:0000269|PubMed:21597164, ECO:0000269|PubMed:21796445};
DE AltName: Full=Endo-beta-N-acetyglucosaminidase 85B {ECO:0000303|PubMed:21796445};
DE Short=AtENGase85B {ECO:0000303|PubMed:21796445};
GN Name=ENGASE2 {ECO:0000305};
GN Synonyms=ENGASE85B {ECO:0000303|PubMed:21796445};
GN OrderedLocusNames=At3g11040 {ECO:0000312|Araport:AT3G11040};
GN ORFNames=F9F8.14 {ECO:0000312|EMBL:AAF01517.1};
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 GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21597164; DOI=10.1271/bbb.110148;
RA Kimura Y., Takeoka Y., Inoue M., Maeda M., Fujiyama K.;
RT "Double-knockout of putative endo-beta-N-acetylglucosaminidase (ENGase)
RT genes in Arabidopsis thaliana: loss of ENGase activity induced accumulation
RT of high-mannose type free N-glycans bearing N,N'-acetylchitobiosyl unit.";
RL Biosci. Biotechnol. Biochem. 75:1019-1021(2011).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21796445; DOI=10.1007/s11103-011-9808-7;
RA Fischl R.M., Stadlmann J., Grass J., Altmann F., Leonard R.;
RT "The two endo-beta-N-acetylglucosaminidase genes from Arabidopsis thaliana
RT encode cytoplasmic enzymes controlling free N-glycan levels.";
RL Plant Mol. Biol. 77:275-284(2011).
CC -!- FUNCTION: Endoglycosidase that releases N-glycans from glycoproteins by
CC cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose
CC core. Involved in the production of high-mannose type N-glycans during
CC plant development and fruit maturation. {ECO:0000269|PubMed:21597164,
CC ECO:0000269|PubMed:21796445}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-
CC mannose glycopeptides and glycoproteins containing the
CC -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue
CC remains attached to the protein, the rest of the oligosaccharide is
CC released intact.; EC=3.2.1.96; Evidence={ECO:0000269|PubMed:21597164,
CC ECO:0000269|PubMed:21796445};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for dabsyl-Asn-Man5 {ECO:0000269|PubMed:21796445};
CC pH dependence:
CC Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:21796445};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21796445}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutants engase85A and engase85B accumulate
CC very high level of free N-glycans carrying two GlcNAc at the reducing
CC end, but their counterparts with a single GlcNAc are completely absent.
CC {ECO:0000269|PubMed:21597164, ECO:0000269|PubMed:21796445}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 85 family. {ECO:0000305}.
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DR EMBL; AC009991; AAF01517.1; -; Genomic_DNA.
DR EMBL; CP002686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q9SRL4; -.
DR SMR; Q9SRL4; -.
DR STRING; 3702.AT3G11040.1; -.
DR CAZy; GH85; Glycoside Hydrolase Family 85.
DR PaxDb; Q9SRL4; -.
DR EnsemblPlants; AT3G11040.3; AT3G11040.3; AT3G11040.
DR Gramene; AT3G11040.3; AT3G11040.3; AT3G11040.
DR Araport; AT3G11040; -.
DR TAIR; locus:2074598; AT3G11040.
DR eggNOG; KOG2331; Eukaryota.
DR HOGENOM; CLU_015297_1_0_1; -.
DR InParanoid; Q9SRL4; -.
DR PhylomeDB; Q9SRL4; -.
DR PRO; PR:Q9SRL4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRL4; baseline and differential.
DR Genevisible; Q9SRL4; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0033925; F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity; IDA:TAIR.
DR GO; GO:0006491; P:N-glycan processing; IDA:TAIR.
DR GO; GO:0006517; P:protein deglycosylation; IGI:TAIR.
DR InterPro; IPR032979; ENGase.
DR InterPro; IPR005201; Glyco_hydro_85.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR13246; PTHR13246; 1.
DR Pfam; PF03644; Glyco_hydro_85; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..701
FT /note="Cytosolic endo-beta-N-acetylglucosaminidase 2"
FT /id="PRO_0000432757"
SQ SEQUENCE 701 AA; 79325 MW; A9AFC5433BBBA12D CRC64;
MPKSNDDDVA QSEAVPLLDL VKPSLPISFP IKALQDLKSR SYFDSFHFQF NRSTVPFRRN
SDCLPNRPRV LVCHDMKGGY VDDKWVQGCE NEAGFAIWHW YLMDIFVYFS HSLVTIPPPC
WTNTAHRHGV KVLGTFITEW DEGKATCKEM LATKESAQMY AERLAELATA LGFDGWLINI
ENDIDEEQIP NMKEFVSHLK KVLHLSTPGA LVIWYDSVTV RGNLQWQDQL TELNKPFFDL
CDGIFMNYTW KESYPNLSAE VAGDRKFDVY MGIDVFGRGS FGGGQWTVNA ALDLLKRNNV
SAAIFAPGWV YETAQPPNFH TAQNKWWSLV EKSWGIVQTY PQVLPFYSDF NQGFGYHVSL
EGRQLSDSPW YNISCQSLQP LLEFNEDNKD IIQVTVDQEG KNVFDFSEQH LNNYYEYDSA
REASFNGGGN IVFRGKLKGD AYFTTRLFKP HLQLSSSPIT ISYSVKSDET SNLGILLSFS
SPSLETKSIL VAPEDPIRRF DDMSLQCLTT SVQTVSEWTV HEASLVMDGH TLTEISAFCY
RPENSTKSAE FVALLGHISV KDHVQNQQNP EILLPASSWV IEAHNVELVP GNSSSKILRV
KLEWRQKDLE DSAFTRYNVY AENVKSTDLR PRKVLEKPKS ETVLLGIAHV PAYYVAELVV
ESDVKAVRFM VQACGEDASL GKLDEALNLL VDLEGLSVNH D
