PAE5_ARATH
ID PAE5_ARATH Reviewed; 427 AA.
AC Q9SR22; F4IZY1; Q0WTI5;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Pectin acetylesterase 5 {ECO:0000303|PubMed:25115560};
DE EC=3.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=PAE5 {ECO:0000303|PubMed:25115560};
GN OrderedLocusNames=At3g09410 {ECO:0000312|Araport:AT3G09410};
GN ORFNames=F3L24.31 {ECO:0000312|EMBL:AAF14036.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-396 (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) 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=Q9SR22-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SR22-2; Sequence=VSP_057375, VSP_057376;
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; AC011436; AAF14036.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74764.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74765.1; -; Genomic_DNA.
DR EMBL; AK227569; BAE99563.1; -; mRNA.
DR EMBL; BT029739; ABM06009.1; -; mRNA.
DR RefSeq; NP_187552.3; NM_111775.4. [Q9SR22-1]
DR RefSeq; NP_974267.2; NM_202538.3. [Q9SR22-2]
DR AlphaFoldDB; Q9SR22; -.
DR SMR; Q9SR22; -.
DR STRING; 3702.AT3G09410.1; -.
DR ESTHER; arath-q9sr22; Pectinacetylesterase-Notum.
DR SwissPalm; Q9SR22; -.
DR PaxDb; Q9SR22; -.
DR PRIDE; Q9SR22; -.
DR ProteomicsDB; 248629; -. [Q9SR22-1]
DR EnsemblPlants; AT3G09410.1; AT3G09410.1; AT3G09410. [Q9SR22-1]
DR EnsemblPlants; AT3G09410.3; AT3G09410.3; AT3G09410. [Q9SR22-2]
DR GeneID; 820100; -.
DR Gramene; AT3G09410.1; AT3G09410.1; AT3G09410. [Q9SR22-1]
DR Gramene; AT3G09410.3; AT3G09410.3; AT3G09410. [Q9SR22-2]
DR KEGG; ath:AT3G09410; -.
DR Araport; AT3G09410; -.
DR TAIR; locus:2083569; AT3G09410.
DR eggNOG; KOG4287; Eukaryota.
DR HOGENOM; CLU_031008_0_0_1; -.
DR InParanoid; Q9SR22; -.
DR OMA; KECDVAQ; -.
DR OrthoDB; 610784at2759; -.
DR PhylomeDB; Q9SR22; -.
DR PRO; PR:Q9SR22; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SR22; baseline and differential.
DR Genevisible; Q9SR22; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0052793; F:pectin acetylesterase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR004963; PAE/NOTUM.
DR PANTHER; PTHR21562; PTHR21562; 1.
DR Pfam; PF03283; PAE; 1.
DR SUPFAM; SSF53474; SSF53474; 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..35
FT /evidence="ECO:0000305"
FT CHAIN 36..427
FT /note="Pectin acetylesterase 5"
FT /evidence="ECO:0000305"
FT /id="PRO_0000431770"
FT ACT_SITE 209
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 305
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 393..396
FT /note="TIAE -> VKDI (in isoform 2)"
FT /id="VSP_057375"
FT VAR_SEQ 397..427
FT /note="Missing (in isoform 2)"
FT /id="VSP_057376"
SQ SEQUENCE 427 AA; 47637 MW; 3E24993C9167822E CRC64;
MAIPRFSSLL RCRKWAKSDW LVASIGCVLI VFFLSFFFDP TSDSVPSVDR SRPIISPSDL
VKLKLSSVAK ERGAFCLDGS LPGYHFHEGS GSGSQSWLVH LEGGGWCNTV ASCSARALTK
LGSSNYFEQE VAFQGVLSSD PSQNPEFFNW NKVAIRYCDG ASFSGRPEAE FKNGTRLFFR
GQLIWEAIID ELLSMGMSDA KQAILTGCSA GGLASLIHCD YFRDHLPKDA AVKCVSDGGY
FLNVPDVLGN PTMRSFYHDV VNLQGVEKSL DQKCVAKTEP SKCMFPQEFL KNIRTPVFLV
NPAYDFWQIQ HVLVPTSADP DKSWAKCRLN IKECDAEQIK VLHGFRSSMM TAIGEFHQNK
DGGMFIDSCY AHCQTVMSVT WHSLTSPRIE NKTIAESVGD WYFNRKPVKL IDCPYPCNPS
CYNMNFT
