PAE4_ARATH
ID PAE4_ARATH Reviewed; 409 AA.
AC Q9SR23;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Pectin acetylesterase 4 {ECO:0000303|PubMed:25115560};
DE EC=3.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=PAE4 {ECO:0000303|PubMed:25115560};
GN OrderedLocusNames=At3g09405 {ECO:0000312|Araport:AT3G09405};
GN ORFNames=F3L24.30 {ECO:0000312|EMBL:AAF14046.1};
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 GENE FAMILY.
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 -!- SIMILARITY: Belongs to the pectinacetylesterase family. {ECO:0000305}.
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DR EMBL; AC011436; AAF14046.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74763.1; -; Genomic_DNA.
DR RefSeq; NP_001154601.1; NM_001161129.2.
DR AlphaFoldDB; Q9SR23; -.
DR SMR; Q9SR23; -.
DR STRING; 3702.AT3G09405.1; -.
DR ESTHER; arath-q9sr23; Pectinacetylesterase-Notum.
DR PaxDb; Q9SR23; -.
DR PRIDE; Q9SR23; -.
DR ProteomicsDB; 226047; -.
DR EnsemblPlants; AT3G09405.1; AT3G09405.1; AT3G09405.
DR GeneID; 7922320; -.
DR Gramene; AT3G09405.1; AT3G09405.1; AT3G09405.
DR KEGG; ath:AT3G09405; -.
DR Araport; AT3G09405; -.
DR TAIR; locus:5019474748; AT3G09405.
DR eggNOG; KOG4287; Eukaryota.
DR HOGENOM; CLU_031008_0_0_1; -.
DR InParanoid; Q9SR23; -.
DR OrthoDB; 610784at2759; -.
DR PhylomeDB; Q9SR23; -.
DR PRO; PR:Q9SR23; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SR23; baseline and differential.
DR Genevisible; Q9SR23; 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 3: Inferred from homology;
KW Cell wall; Cell wall biogenesis/degradation; Glycoprotein; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..409
FT /note="Pectin acetylesterase 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431769"
FT ACT_SITE 199
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 295
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 362
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 409 AA; 45749 MW; 16C190689D1B0DDC CRC64;
MVIRSLLQCR TWSKSDWLLA SIGIVLIVYS FSLSFNSTSD SIPSVDRSDL VKLKLSSKAK
ERGAFCLDGS LPGYHFHKGS GSGSNSWLLY LEGGGGCRTI ESCSARAMTR LGSSNFFEHE
VPFFGVLSSD PSQNPDFFNW NRVMIRYCDG ACFSGHPEAE FKNETRLFFR GQLIWEAIMD
ELLSMGMSHA KRAMLTGCSA GGLSTLIHCD YFRDHLPKDA TVKCVSDGGY ILNVLDVLGN
PTMGSFFHDV VTLQSVDKSL DQNCVAKMEP SKCMFPQESL KNIRTPVFLV NTAYDYWQIQ
NGLVPDSPDL DERWKICRLN IQECDAAQMK VLHGFRSSLI DAIGEFHVNK EGGMFINSCN
SHCQIRESWH SATSTRIENK TIAESVGDWY FNRKPVKLID CPYPCNASC
