PAE3_ARATH
ID PAE3_ARATH Reviewed; 416 AA.
AC O80731;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Pectin acetylesterase 3 {ECO:0000303|PubMed:25115560};
DE EC=3.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=PAE3 {ECO:0000303|PubMed:25115560};
GN OrderedLocusNames=At2g46930 {ECO:0000312|Araport:AT2G46930};
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 GENE FAMILY, AND DISRUPTION PHENOTYPE.
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:0000250|UniProtKB:B9DFR3}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:25115560}.
CC -!- SIMILARITY: Belongs to the pectinacetylesterase family. {ECO:0000305}.
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DR EMBL; AC004411; AAC34238.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10774.1; -; Genomic_DNA.
DR EMBL; AY052671; AAK96575.1; -; mRNA.
DR PIR; T02194; T02194.
DR RefSeq; NP_182216.1; NM_130261.3.
DR AlphaFoldDB; O80731; -.
DR SMR; O80731; -.
DR STRING; 3702.AT2G46930.1; -.
DR ESTHER; arath-o80731; Pectinacetylesterase-Notum.
DR PaxDb; O80731; -.
DR PRIDE; O80731; -.
DR ProteomicsDB; 236317; -.
DR EnsemblPlants; AT2G46930.1; AT2G46930.1; AT2G46930.
DR GeneID; 819307; -.
DR Gramene; AT2G46930.1; AT2G46930.1; AT2G46930.
DR KEGG; ath:AT2G46930; -.
DR Araport; AT2G46930; -.
DR TAIR; locus:2041429; AT2G46930.
DR eggNOG; KOG4287; Eukaryota.
DR HOGENOM; CLU_031008_0_0_1; -.
DR InParanoid; O80731; -.
DR OMA; FFQDFRT; -.
DR OrthoDB; 610784at2759; -.
DR PhylomeDB; O80731; -.
DR PRO; PR:O80731; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80731; baseline and differential.
DR Genevisible; O80731; 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 Cell wall; Cell wall biogenesis/degradation; Glycoprotein; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..416
FT /note="Pectin acetylesterase 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431768"
FT ACT_SITE 198
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 294
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 361
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 416 AA; 45944 MW; 20D4EE2B75EEB387 CRC64;
MKSVLRIAAA IFWLWLFIVL GVIGSGNVRD TDDEISLLES QLVVTSPSQL LMVPLTLIQA
AASKGAVCLD GTLPGYHLHP GSGSGANRWL IQLEGGGWCN TRRSCIFRKT TRRGSSNHME
KVLAFTGILS NKSNENPDFF NWNRVKLRYC DGASFTGDSQ DESSQLYYRG QRIWHSAMEE
LLSKGMQKAE QALLSGCSAG GLASILHCDQ FKELFPGTTT VKCLSDAGMF MDAVDVSGGH
SLRKMFQGVV TVQNLQKELS TACTKHLDPT SCFFPQNLVS GIKTPMFLLN AAYDAWQVQE
SLAPPSVDLS GSWKACKSDH SHCNSSQIQF FQDFRTHMVD AVKSFATSTH NGVFINSCFA
HCQSERQDTW YAPDSPTLHG KTVAESVGDW YFDRTTVKAI DCPYPCDKTC HNLIFK
