NTAN1_ARATH
ID NTAN1_ARATH Reviewed; 347 AA.
AC O64876; Q8LDD1;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein N-terminal asparagine amidohydrolase {ECO:0000303|PubMed:30117535};
DE EC=3.5.1.121 {ECO:0000305};
DE AltName: Full=Protein NH2-terminal asparagine amidohydrolase {ECO:0000305};
DE AltName: Full=Protein NH2-terminal asparagine deamidase {ECO:0000305};
GN Name=NTAN1 {ECO:0000303|PubMed:30117535};
GN OrderedLocusNames=At2g44420 {ECO:0000312|Araport:AT2G44420};
GN ORFNames=F4I1.23 {ECO:0000312|EMBL:AEC10418.1};
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=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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
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: N-terminal asparagine deamidase that mediates deamidation of
CC N-terminal asparagine residues to aspartate. Required for the
CC ubiquitin-dependent turnover of intracellular proteins that initiate
CC with Met-Asn. These proteins are acetylated on the retained initiator
CC methionine and can subsequently be modified by the removal of N-acetyl
CC methionine by acylaminoacid hydrolase (AAH). Conversion of the
CC resulting N-terminal asparagine to aspartate by NTAN1 renders the
CC protein susceptible to arginylation, polyubiquitination and degradation
CC as specified by the N-end rule. This enzyme does not act on substrates
CC with internal or C-terminal asparagines and does not act on glutamine
CC residues in any position (By similarity). Does not seems to be involved
CC in immune response, unlike the N-terminal glutamine amidohydrolase
CC NTAQ1 (PubMed:30117535). {ECO:0000250|UniProtKB:Q64311,
CC ECO:0000269|PubMed:30117535}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + N-terminal L-asparaginyl-[protein] = N-terminal
CC L-aspartyl-[protein] + NH4(+); Xref=Rhea:RHEA:50676, Rhea:RHEA-
CC COMP:12669, Rhea:RHEA-COMP:12776, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:50348,
CC ChEBI:CHEBI:64720; EC=3.5.1.121; Evidence={ECO:0000305};
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DR EMBL; AC004521; AAC16088.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10418.1; -; Genomic_DNA.
DR EMBL; AK117511; BAC42174.1; -; mRNA.
DR EMBL; BT005103; AAO50636.1; -; mRNA.
DR EMBL; AY086075; AAM63281.1; -; mRNA.
DR PIR; T02397; T02397.
DR RefSeq; NP_566017.1; NM_130005.3.
DR AlphaFoldDB; O64876; -.
DR SMR; O64876; -.
DR STRING; 3702.AT2G44420.1; -.
DR PaxDb; O64876; -.
DR PRIDE; O64876; -.
DR EnsemblPlants; AT2G44420.1; AT2G44420.1; AT2G44420.
DR GeneID; 819049; -.
DR Gramene; AT2G44420.1; AT2G44420.1; AT2G44420.
DR KEGG; ath:AT2G44420; -.
DR Araport; AT2G44420; -.
DR TAIR; locus:2050549; AT2G44420.
DR eggNOG; ENOG502QSQW; Eukaryota.
DR HOGENOM; CLU_066533_0_0_1; -.
DR InParanoid; O64876; -.
DR PhylomeDB; O64876; -.
DR PRO; PR:O64876; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64876; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008418; F:protein-N-terminal asparagine amidohydrolase activity; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR026750; NTAN1.
DR PANTHER; PTHR12498; PTHR12498; 1.
DR Pfam; PF14736; N_Asn_amidohyd; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..347
FT /note="Protein N-terminal asparagine amidohydrolase"
FT /id="PRO_0000445545"
FT CONFLICT 286
FT /note="Q -> R (in Ref. 5; AAM63281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 39174 MW; DC58D6AB8A739222 CRC64;
MIYVGGVQFL DESSSFSLSS SSQGSSLLVD VMSHPVITLA SDSFKNLEEK NVSFDESDSE
SSTKDRYVYI FQREFAVVNP ALVDFVGTDE ATTCVGLVIR NRKSGMTSVA HMDSPEIVDL
GISQMLLLVL QDDVDAELDV HMVGGYEDVD IKNADGVGDY AKPEGYSFPL CCKLVETLQK
RRENFHIQTL FILGHNTKLD SQANTCPIFN GCLVNTSTGA ILPASFNRTS RCPDEIVRRI
RVSSSFEDSS WKGKLLDTYD TKTDRFIIAP CRWTMRLIEY VWELNQLTDE EILTNCSTSP
SAEGPDFVNS LRRNWGYLLK YPEWSKTFPR RQPRVFERTV DGHWKKC
