PAE11_ARATH
ID PAE11_ARATH Reviewed; 391 AA.
AC Q9FH82; Q8LAE9; Q93ZX9;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Pectin acetylesterase 11 {ECO:0000303|PubMed:25115560};
DE EC=3.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=PAE11 {ECO:0000303|PubMed:25115560};
GN OrderedLocusNames=At5g45280 {ECO:0000312|Araport:AT5G45280};
GN ORFNames=K9E15.6 {ECO:0000312|EMBL:BAB10249.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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] (ISOFORMS 1 AND 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FH82-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FH82-2; Sequence=VSP_057380, VSP_057381;
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; AB020744; BAB10249.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95225.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95226.1; -; Genomic_DNA.
DR EMBL; AY057665; AAL15296.1; -; mRNA.
DR EMBL; AY056198; AAL07047.1; -; mRNA.
DR EMBL; AY150453; AAN12894.1; -; mRNA.
DR EMBL; AY087860; AAM65412.1; -; mRNA.
DR RefSeq; NP_199341.1; NM_123896.4. [Q9FH82-1]
DR RefSeq; NP_851135.1; NM_180804.1. [Q9FH82-2]
DR AlphaFoldDB; Q9FH82; -.
DR SMR; Q9FH82; -.
DR STRING; 3702.AT5G45280.2; -.
DR ESTHER; arath-q8lae9; Pectinacetylesterase-Notum.
DR SwissPalm; Q9FH82; -.
DR PaxDb; Q9FH82; -.
DR PRIDE; Q9FH82; -.
DR ProteomicsDB; 236315; -. [Q9FH82-1]
DR EnsemblPlants; AT5G45280.1; AT5G45280.1; AT5G45280. [Q9FH82-2]
DR EnsemblPlants; AT5G45280.2; AT5G45280.2; AT5G45280. [Q9FH82-1]
DR GeneID; 834564; -.
DR Gramene; AT5G45280.1; AT5G45280.1; AT5G45280. [Q9FH82-2]
DR Gramene; AT5G45280.2; AT5G45280.2; AT5G45280. [Q9FH82-1]
DR KEGG; ath:AT5G45280; -.
DR Araport; AT5G45280; -.
DR TAIR; locus:2158495; AT5G45280.
DR eggNOG; KOG4287; Eukaryota.
DR HOGENOM; CLU_031008_0_3_1; -.
DR InParanoid; Q9FH82; -.
DR OMA; WFFERST; -.
DR OrthoDB; 610784at2759; -.
DR PhylomeDB; Q9FH82; -.
DR PRO; PR:Q9FH82; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FH82; baseline and differential.
DR Genevisible; Q9FH82; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0052793; F:pectin acetylesterase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
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 Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..391
FT /note="Pectin acetylesterase 11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431776"
FT ACT_SITE 171
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 267
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 334
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT VAR_SEQ 306..370
FT /note="GYRDQVLAALAPVRSATTNGLFLDSCHAHCQGGSAATWSGDKGPTVANTKMA
FT KAVGDWFFERSTF -> ETKCWLRWRLFDPRRRTDCSWTRAMLIAKVEALPLGPATKVP
FT QSRIRKWLRRLEIGSLRGVRFRT (in isoform 2)"
FT /id="VSP_057380"
FT VAR_SEQ 371..391
FT /note="Missing (in isoform 2)"
FT /id="VSP_057381"
FT CONFLICT 3
FT /note="W -> R (in Ref. 4; AAM65412)"
FT /evidence="ECO:0000305"
FT CONFLICT 136..137
FT /note="TH -> AN (in Ref. 4; AAM65412)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="D -> E (in Ref. 4; AAM65412)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="R -> Q (in Ref. 4; AAM65412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 42009 MW; 4541E211DA6432A5 CRC64;
MTWLKQMWSS ILVLAVVVIG ARAVPITYLE SAVAKGAVCL DGSAPAYHFD KGSGSGVNNW
IVHMEGGGWC TDIATCVQRK STMKGSSKLM NKDFGFSGIL GGKQSTNPDF YNWNRIKVRY
CDGSSFTGDI EAVDPTHKLF FRGARVWRAV IDDLMAKGMS NAQNAILSGC SAGALAAILH
CDQFKSTLPK TAKVKCVSDA GYFIHGKDIT GGSYIQSYYA KVVATHGSAK SLPASCTSSM
KPDLCFFPQY VAKTLQTPLF VINAAFDSWQ IKNVLAPTSV DKSKAWKTCK LDLKKCTAAQ
LQTVQGYRDQ VLAALAPVRS ATTNGLFLDS CHAHCQGGSA ATWSGDKGPT VANTKMAKAV
GDWFFERSTF QNVDCSSLNC NPTCPAVSTE D
