NANA_ARATH
ID NANA_ARATH Reviewed; 461 AA.
AC Q9LTW4; F4J9V9; Q8VYM5;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Aspartic proteinase NANA, chloroplast {ECO:0000303|PubMed:22987884};
DE EC=3.4.23.- {ECO:0000269|PubMed:22987884};
DE Flags: Precursor;
GN Name=NANA {ECO:0000303|PubMed:22987884};
GN OrderedLocusNames=At3g12700 {ECO:0000312|Araport:AT3G12700};
GN ORFNames=MBK21.8 {ECO:0000312|EMBL:BAB02414.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-461 (ISOFORM 1).
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 GENE FAMILY.
RX PubMed=14697270; DOI=10.1016/j.phytochem.2003.09.005;
RA Beers E.P., Jones A.M., Dickerman A.W.;
RT "The S8 serine, C1A cysteine and A1 aspartic protease families in
RT Arabidopsis.";
RL Phytochemistry 65:43-58(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY SUCROSE, SUBCELLULAR LOCATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=22987884; DOI=10.1104/pp.112.204016;
RA Paparelli E., Gonzali S., Parlanti S., Novi G., Giorgi F.M., Licausi F.,
RA Kosmacz M., Feil R., Lunn J.E., Brust H., van Dongen J.T., Steup M.,
RA Perata P.;
RT "Misexpression of a chloroplast aspartyl protease leads to severe growth
RT defects and alters carbohydrate metabolism in Arabidopsis.";
RL Plant Physiol. 160:1237-1250(2012).
CC -!- FUNCTION: Aspartic proteinase that can use azocasein as substrate and
CC regulates endogenous sugar levels (e.g. sucrose, glucose and fructose)
CC by modulating starch accumulation and remobilization (PubMed:22987884).
CC Influences general morphology and development (PubMed:22987884).
CC {ECO:0000269|PubMed:22987884}.
CC -!- ACTIVITY REGULATION: Repressed by pepstatin A.
CC {ECO:0000269|PubMed:22987884}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:22987884};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:22987884}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LTW4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LTW4-2; Sequence=VSP_059153, VSP_059154;
CC -!- INDUCTION: Expressed with a pronounced diurnal rhythm characterized by
CC a peak at the end of the day and early night (at protein level).
CC Slightly induced by sucrose (Suc). {ECO:0000269|PubMed:22987884}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL49921.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB024033; BAB02414.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75236.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75237.1; -; Genomic_DNA.
DR EMBL; AY070426; AAL49921.1; ALT_INIT; mRNA.
DR RefSeq; NP_001154610.1; NM_001161138.1. [Q9LTW4-2]
DR RefSeq; NP_187876.2; NM_112106.4. [Q9LTW4-1]
DR AlphaFoldDB; Q9LTW4; -.
DR SMR; Q9LTW4; -.
DR STRING; 3702.AT3G12700.1; -.
DR MEROPS; A01.A30; -.
DR PaxDb; Q9LTW4; -.
DR PRIDE; Q9LTW4; -.
DR ProteomicsDB; 251200; -. [Q9LTW4-1]
DR EnsemblPlants; AT3G12700.1; AT3G12700.1; AT3G12700. [Q9LTW4-1]
DR EnsemblPlants; AT3G12700.2; AT3G12700.2; AT3G12700. [Q9LTW4-2]
DR GeneID; 820452; -.
DR Gramene; AT3G12700.1; AT3G12700.1; AT3G12700. [Q9LTW4-1]
DR Gramene; AT3G12700.2; AT3G12700.2; AT3G12700. [Q9LTW4-2]
DR KEGG; ath:AT3G12700; -.
DR Araport; AT3G12700; -.
DR TAIR; locus:2087790; AT3G12700.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_8_0_1; -.
DR InParanoid; Q9LTW4; -.
DR OMA; GSEFTWF; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; Q9LTW4; -.
DR PRO; PR:Q9LTW4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LTW4; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IMP:TAIR.
DR GO; GO:0010019; P:chloroplast-nucleus signaling pathway; IMP:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR CDD; cd05476; pepsin_A_like_plant; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034161; Pepsin-like_plant.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Aspartyl protease; Chloroplast; Glycoprotein;
KW Hydrolase; Plastid; Protease; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN ?..461
FT /note="Aspartic proteinase NANA, chloroplast"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441984"
FT DOMAIN 106..456
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 191..263
FT /note="YADGSAAQGVFAKETITVGLTNGRMARLPGHLIGCSSSFTGQSFQGADGVLG
FT LAFSDFSFTSTATSLYGAKFS -> EFFGVAWIRCKCIAREGEIKYMQMGQQHKAYSQR
FT RLSQLVSLMVVWLDSLVTSLVVVVPLQDRASKEPMGFLV (in isoform 2)"
FT /id="VSP_059153"
FT VAR_SEQ 264..461
FT /note="Missing (in isoform 2)"
FT /id="VSP_059154"
SQ SEQUENCE 461 AA; 50568 MW; 208A4CF0CBCA8EAA CRC64;
MYINTLFWKQ NPTGDKKNQE EKMQKTLLSC LITTLLLITV ADSMKDTSVR LKLAHRDTLL
PKPLSRIEDV IGADQKRHSL ISRKRNSTVG VKMDLGSGID YGTAQYFTEI RVGTPAKKFR
VVVDTGSELT WVNCRYRARG KDNRRVFRAD ESKSFKTVGC LTQTCKVDLM NLFSLTTCPT
PSTPCSYDYR YADGSAAQGV FAKETITVGL TNGRMARLPG HLIGCSSSFT GQSFQGADGV
LGLAFSDFSF TSTATSLYGA KFSYCLVDHL SNKNVSNYLI FGSSRSTKTA FRRTTPLDLT
RIPPFYAINV IGISLGYDML DIPSQVWDAT SGGGTILDSG TSLTLLADAA YKQVVTGLAR
YLVELKRVKP EGVPIEYCFS FTSGFNVSKL PQLTFHLKGG ARFEPHRKSY LVDAAPGVKC
LGFVSAGTPA TNVIGNIMQQ NYLWEFDLMA STLSFAPSAC T
