NAGLU_ARATH
ID NAGLU_ARATH Reviewed; 806 AA.
AC Q9FNA3;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Alpha-N-acetylglucosaminidase {ECO:0000305};
DE EC=3.2.1.50 {ECO:0000305};
DE AltName: Full=N-acetyl-glucosaminidase {ECO:0000303|PubMed:18782908};
DE Short=AtNAGLU {ECO:0000303|PubMed:18782908};
DE AltName: Full=Protein CYCLOPS 1 {ECO:0000303|PubMed:18782908};
DE Flags: Precursor;
GN Name=NAGLU {ECO:0000303|PubMed:18782908};
GN Synonyms=CYL1 {ECO:0000303|PubMed:18782908};
GN OrderedLocusNames=At5g13690 {ECO:0000312|Araport:AT5G13690};
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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].
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 DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18782908; DOI=10.1093/jxb/ern215;
RA Ronceret A., Gadea-Vacas J., Guilleminot J., Devic M.;
RT "The alpha-N-acetyl-glucosaminidase gene is transcriptionally activated in
RT male and female gametes prior to fertilization and is essential for seed
RT development in Arabidopsis.";
RL J. Exp. Bot. 59:3649-3659(2008).
CC -!- FUNCTION: Involved in the remodeling of the N-acetyl-glucosamine
CC residues of proteoglycan complexes during reproductive development. Is
CC essential to promote the first divisions of the zygote.
CC {ECO:0000305|PubMed:18782908}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine
CC residues in N-acetyl-alpha-D-glucosaminides.; EC=3.2.1.50;
CC Evidence={ECO:0000305};
CC -!- DEVELOPMENTAL STAGE: Expressed during early and late male
CC gametogenesis, and in cells of the embryo sac at the time of
CC fertilization. After fertilization, expressed in the embryo, suspensor,
CC and endosperm until the cotyledon stage embryo.
CC {ECO:0000269|PubMed:18782908}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous, due to
CC embryo development arrested at one-cell stage.
CC {ECO:0000269|PubMed:18782908}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 89 family. {ECO:0000305}.
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DR EMBL; AB006704; BAB08696.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91928.1; -; Genomic_DNA.
DR EMBL; AY080811; AAL87291.1; -; mRNA.
DR EMBL; AY117179; AAM51254.1; -; mRNA.
DR RefSeq; NP_196873.1; NM_121372.3.
DR AlphaFoldDB; Q9FNA3; -.
DR SMR; Q9FNA3; -.
DR STRING; 3702.AT5G13690.1; -.
DR CAZy; GH89; Glycoside Hydrolase Family 89.
DR MetOSite; Q9FNA3; -.
DR PaxDb; Q9FNA3; -.
DR PRIDE; Q9FNA3; -.
DR ProteomicsDB; 251082; -.
DR EnsemblPlants; AT5G13690.1; AT5G13690.1; AT5G13690.
DR GeneID; 831214; -.
DR Gramene; AT5G13690.1; AT5G13690.1; AT5G13690.
DR KEGG; ath:AT5G13690; -.
DR Araport; AT5G13690; -.
DR TAIR; locus:2173209; AT5G13690.
DR eggNOG; KOG2233; Eukaryota.
DR HOGENOM; CLU_011988_2_1_1; -.
DR InParanoid; Q9FNA3; -.
DR OMA; SNHIFFC; -.
DR OrthoDB; 584128at2759; -.
DR PhylomeDB; Q9FNA3; -.
DR BioCyc; ARA:AT5G13690-MON; -.
DR PRO; PR:Q9FNA3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNA3; baseline and differential.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0004561; F:alpha-N-acetylglucosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:UniProtKB.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR007781; NAGLU.
DR InterPro; IPR024732; NAGLU_C.
DR InterPro; IPR024240; NAGLU_N.
DR InterPro; IPR024733; NAGLU_tim-barrel.
DR PANTHER; PTHR12872; PTHR12872; 1.
DR Pfam; PF05089; NAGLU; 1.
DR Pfam; PF12972; NAGLU_C; 1.
DR Pfam; PF12971; NAGLU_N; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..806
FT /note="Alpha-N-acetylglucosaminidase"
FT /evidence="ECO:0000255"
FT /id="PRO_5006751773"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 806 AA; 92689 MW; 8F8500032F3BCFA2 CRC64;
MHSIKLVLLV LLIISFHSQT VSKHHPTIDG LLDRLDSLLP TSSVQESAAK GLLQRLLPTH
SQSFELRIIS KDACGGTSCF VIENYDGPGR IGPEILIKGT TGVEIASGLH WYLKYKCNAH
VSWDKTGGIQ VASVPQPGHL PRIDSKRIFI RRPVPWNYYQ NVVTSSYSYV WWGWERWERE
IDWMALQGIN LPLAFTGQEA IWQKVFKRFN ISKEDLDDYF GGPAFLAWAR MGNLHAWGGP
LSKNWLDDQL LLQKQILSRM LKFGMTPVLP SFSGNVPSAL RKIYPEANIT RLDNWNTVDG
DSRWCCTYLL NPSDPLFIEI GEAFIKQQTE EYGEITNIYN CDTFNENTPP TSEPEYISSL
GAAVYKAMSK GNKNAVWLMQ GWLFSSDSKF WKPPQLKALL HSVPFGKMIV LDLYAEVKPI
WNKSAQFYGT PYIWCMLHNF GGNIEMYGAL DSISSGPVDA RVSKNSTMVG VGMCMEGIEQ
NPVVYELTSE MAFRDEKVDV QKWLKSYARR RYMKENHQIE AAWEILYHTV YNCTDGIADH
NTDFIVKLPD WDPSSSVQDD LKQKDSYMIS TGPYETKRRV LFQDKTADLP KAHLWYSTKE
VIQALKLFLE AGDDLSRSLT YRYDMVDLTR QVLSKLANQV YTEAVTAFVK KDIGSLGQLS
EKFLELIKDM DVLLASDDNC LLGTWLESAK KLAKNGDERK QYEWNARTQV TMWYDSNDVN
QSKLHDYANK FWSGLLEDYY LPRARLYFNE MLKSLRDKKI FKVEKWRREW IMMSHKWQQS
SSEVYPVKAK GDALAISRHL LSKYFP
