NTAQ1_ARATH
ID NTAQ1_ARATH Reviewed; 221 AA.
AC O22944; Q0WL89;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein N-terminal glutamine amidohydrolase {ECO:0000305};
DE EC=3.5.1.122 {ECO:0000269|PubMed:30117535};
DE AltName: Full=Protein NH2-terminal glutamine deamidase {ECO:0000305};
DE Short=N-terminal Gln amidase {ECO:0000305};
DE Short=Nt(Q)-amidase {ECO:0000305};
GN Name=NTAQ1 {ECO:0000303|PubMed:30117535}; OrderedLocusNames=At2g41760;
GN ORFNames=T11A7.14;
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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30117535; DOI=10.1111/nph.15387;
RA Vicente J., Mendiondo G.M., Pauwels J., Pastor V., Izquierdo Y.,
RA Naumann C., Movahedi M., Rooney D., Gibbs D.J., Smart K., Bachmair A.,
RA Gray J.E., Dissmeyer N., Castresana C., Ray R.V., Gevaert K.,
RA Holdsworth M.J.;
RT "Distinct branches of the N-end rule pathway modulate the plant immune
RT response.";
RL New Phytol. 221:988-1000(2019).
CC -!- FUNCTION: Mediates the side-chain deamidation of N-terminal glutamine
CC residues to glutamate, an important step in N-end rule pathway of
CC protein degradation (PubMed:30117535). Conversion of the resulting N-
CC terminal glutamine to glutamate renders the protein susceptible to
CC arginylation, polyubiquitination and degradation as specified by the N-
CC end rule (PubMed:30117535). Does not act on substrates with internal or
CC C-terminal glutamine and does not act on non-glutamine residues in any
CC position (PubMed:30117535). Involved in immune response
CC (PubMed:30117535). Controls the expression of specific defense-response
CC genes, activates the synthesis pathway for the phytoalexin camalexin,
CC and influences basal resistance to the hemibiotroph pathogen
CC Pseudomonas syringae pv tomato (Pst) (PubMed:30117535).
CC {ECO:0000269|PubMed:30117535}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-terminal L-glutaminyl-[protein] = N-terminal L-
CC glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:50680, Rhea:RHEA-
CC COMP:12668, Rhea:RHEA-COMP:12777, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:64721, ChEBI:CHEBI:64722;
CC EC=3.5.1.122; Evidence={ECO:0000269|PubMed:30117535};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q96HA8}.
CC -!- SIMILARITY: Belongs to the NTAQ1 family. {ECO:0000305}.
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DR EMBL; AC002339; AAC02771.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10029.1; -; Genomic_DNA.
DR EMBL; AY037225; AAK59825.1; -; mRNA.
DR EMBL; AY060532; AAL31163.1; -; mRNA.
DR EMBL; AK230318; BAF02118.1; -; mRNA.
DR PIR; G84845; G84845.
DR RefSeq; NP_565959.1; NM_129740.4.
DR AlphaFoldDB; O22944; -.
DR SMR; O22944; -.
DR BioGRID; 4112; 2.
DR IntAct; O22944; 2.
DR STRING; 3702.AT2G41760.1; -.
DR iPTMnet; O22944; -.
DR PaxDb; O22944; -.
DR PRIDE; O22944; -.
DR ProteomicsDB; 249161; -.
DR EnsemblPlants; AT2G41760.1; AT2G41760.1; AT2G41760.
DR GeneID; 818775; -.
DR Gramene; AT2G41760.1; AT2G41760.1; AT2G41760.
DR KEGG; ath:AT2G41760; -.
DR Araport; AT2G41760; -.
DR TAIR; locus:2054381; AT2G41760.
DR eggNOG; KOG3261; Eukaryota.
DR HOGENOM; CLU_091083_2_0_1; -.
DR InParanoid; O22944; -.
DR OMA; GWGTVYS; -.
DR PhylomeDB; O22944; -.
DR BRENDA; 3.5.1.122; 399.
DR PRO; PR:O22944; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22944; baseline and differential.
DR Genevisible; O22944; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008418; F:protein-N-terminal asparagine amidohydrolase activity; IEA:InterPro.
DR GO; GO:0070773; F:protein-N-terminal glutamine amidohydrolase activity; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:1901183; P:positive regulation of camalexin biosynthetic process; IMP:TAIR.
DR GO; GO:0036211; P:protein modification process; IBA:GO_Central.
DR Gene3D; 3.10.620.10; -; 1.
DR InterPro; IPR037132; N_Gln_amidohydro_ab_roll_sf.
DR InterPro; IPR039733; NTAQ1.
DR InterPro; IPR023128; Prot_N_Gln_amidohydro_ab_roll.
DR PANTHER; PTHR13035; PTHR13035; 1.
DR Pfam; PF09764; Nt_Gln_amidase; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydrolase; Plant defense; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..221
FT /note="Protein N-terminal glutamine amidohydrolase"
FT /id="PRO_0000381834"
FT ACT_SITE 23
FT /evidence="ECO:0000250"
FT ACT_SITE 79
FT /evidence="ECO:0000250"
FT ACT_SITE 97
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 114
FT /note="E -> G (in Ref. 4; BAF02118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 24972 MW; 03D59A9843427D60 CRC64;
MSGVTSEPIA MDATRFQHTP YYCEENVYLL CKTLCENGVA EATCSDLFVV FISNEKKQVP
LWHQKASTRA DGVVLWDYHV ICVQRKKESD SEPLVWDLDS TLPFPSPLAS YVTETIQPSF
QLFAEYQRFF RIVHAPLFFK HFASDRRHMK EPDGSWTAQP PPYEPIVAQD GILHNLSEYI
AMSGADTLSS LDPETVTAAI SQKLGVVVSH TQLQDLFTKL P
