PAE9_ARATH
ID PAE9_ARATH Reviewed; 451 AA.
AC B9DFR3; Q8W4A4; Q9FF93;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Pectin acetylesterase 9 {ECO:0000303|PubMed:25115560};
DE EC=3.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=PAE9 {ECO:0000303|PubMed:25115560};
GN OrderedLocusNames=At5g23870 {ECO:0000312|Araport:AT5G23870};
GN ORFNames=MRO11.9 {ECO:0000312|EMBL:BAB10060.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-415 (ISOFORM 2).
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 GENE FAMILY, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=25115560; DOI=10.1007/s00425-014-2139-6;
RA de Souza A., Hull P.A., Gille S., Pauly M.;
RT "Identification and functional characterization of the distinct plant
RT pectin esterases PAE8 and PAE9 and their deletion mutants.";
RL Planta 240:1123-1138(2014).
CC -!- FUNCTION: Hydrolyzes acetyl esters in homogalacturonan regions of
CC pectin. In type I primary cell wall, galacturonic acid residues of
CC pectin can be acetylated at the O-2 and O-3 positions. Decreasing the
CC degree of acetylation of pectin gels in vitro alters their physical
CC properties. {ECO:0000269|PubMed:25115560}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B9DFR3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B9DFR3-2; Sequence=VSP_057377, VSP_057378;
CC -!- DISRUPTION PHENOTYPE: Reduced inflorescence stem growth and increased
CC levels of acetate in rosette leaves. {ECO:0000269|PubMed:25115560}.
CC -!- SIMILARITY: Belongs to the pectinacetylesterase family. {ECO:0000305}.
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DR EMBL; AB005244; BAB10060.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93226.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93227.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68835.1; -; Genomic_DNA.
DR EMBL; AK316872; BAH19580.1; -; mRNA.
DR EMBL; AY062706; AAL32784.1; -; mRNA.
DR EMBL; AY093369; AAM13368.1; -; mRNA.
DR RefSeq; NP_001318631.1; NM_001343830.1. [B9DFR3-2]
DR RefSeq; NP_197775.3; NM_122292.4. [B9DFR3-2]
DR RefSeq; NP_974827.1; NM_203098.2. [B9DFR3-1]
DR AlphaFoldDB; B9DFR3; -.
DR SMR; B9DFR3; -.
DR STRING; 3702.AT5G23870.3; -.
DR ESTHER; arath-B9DFR3; Pectinacetylesterase-Notum.
DR PaxDb; B9DFR3; -.
DR PRIDE; B9DFR3; -.
DR ProteomicsDB; 248650; -. [B9DFR3-1]
DR EnsemblPlants; AT5G23870.1; AT5G23870.1; AT5G23870. [B9DFR3-2]
DR EnsemblPlants; AT5G23870.3; AT5G23870.3; AT5G23870. [B9DFR3-1]
DR EnsemblPlants; AT5G23870.4; AT5G23870.4; AT5G23870. [B9DFR3-2]
DR GeneID; 832452; -.
DR Gramene; AT5G23870.1; AT5G23870.1; AT5G23870. [B9DFR3-2]
DR Gramene; AT5G23870.3; AT5G23870.3; AT5G23870. [B9DFR3-1]
DR Gramene; AT5G23870.4; AT5G23870.4; AT5G23870. [B9DFR3-2]
DR KEGG; ath:AT5G23870; -.
DR Araport; AT5G23870; -.
DR TAIR; locus:2172833; AT5G23870.
DR eggNOG; KOG4287; Eukaryota.
DR InParanoid; B9DFR3; -.
DR OMA; IEIDCAY; -.
DR OrthoDB; 610784at2759; -.
DR PhylomeDB; B9DFR3; -.
DR PRO; PR:B9DFR3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B9DFR3; baseline and differential.
DR Genevisible; B9DFR3; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0052793; F:pectin acetylesterase activity; IDA:TAIR.
DR GO; GO:0071555; P:cell wall organization; IMP:TAIR.
DR InterPro; IPR004963; PAE/NOTUM.
DR PANTHER; PTHR21562; PTHR21562; 1.
DR Pfam; PF03283; PAE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell wall; Cell wall biogenesis/degradation;
KW Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..451
FT /note="Pectin acetylesterase 9"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431774"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 280
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 348
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 411..415
FT /note="ASNAS -> VNLDI (in isoform 2)"
FT /id="VSP_057377"
FT VAR_SEQ 416..451
FT /note="Missing (in isoform 2)"
FT /id="VSP_057378"
SQ SEQUENCE 451 AA; 50038 MW; 24DFDBC158BBC04B CRC64;
MKTTTRLLDL TAAMVLVVYV SFSPPLVSGE PGRRVSMTLV RDAAALGAFC LDGSLPAYHL
DRGFGAGSNN WILQFEGGGW CNDIASCVER AKTRRGSTRY MSKTVVFTGV LSNNASQNPD
FYNWNKVRLR YCDGASFAGD SQFGNGTSLL YFRGQRIWNA IILDLLPKGL AKAHKALLTG
CSAGGLSTFL HCDNFTSYLP KNASVKCMSD AGFFLDAIDV AANRTMRSFY SQLVSLQGIQ
KNLDPSCTHA FFPEPSLCFF PQYVLRFIKT PFFILNSAYD VFQFHHGLVP PSADQTGRWN
RCKLNVTACN PHQLDALQGF RKDMLGALMN FFRNSTRGGM FINSCFDHCQ SALEETWLSP
TSPRINNKTI AETVGDWYFG RGEEAKEIGC PYPCDKTCHN LIPASTSDFL ASNASGSGHN
SRGTHLTFLF LLLNFFFFFV ISKFSKKDYV T
