PAE12_ARATH
ID PAE12_ARATH Reviewed; 415 AA.
AC Q9SFF6; Q9M9K8;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Pectin acetylesterase 12 {ECO:0000303|PubMed:25115560};
DE EC=3.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=PAE12 {ECO:0000303|PubMed:25115560};
GN OrderedLocusNames=At3g05910 {ECO:0000312|Araport:AT3G05910};
GN ORFNames=F10A16.21 {ECO:0000312|EMBL:AAF26093.1},
GN F2O10.13 {ECO:0000312|EMBL:AAF23225.1};
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 INDUCTION.
RX PubMed=12026180; DOI=10.1094/mpmi.2002.15.4.404;
RA Vercauteren I., de Almeida Engler J., De Groodt R., Gheysen G.;
RT "An Arabidopsis thaliana pectin acetylesterase gene is upregulated in
RT nematode feeding sites induced by root-knot and cyst nematodes.";
RL Mol. Plant Microbe Interact. 15:404-407(2002).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q9SFF6-1; Sequence=Displayed;
CC -!- INDUCTION: In roots by the parasitic nematodes Heterodera schachtii and
CC Meloidogyne incognita. {ECO:0000269|PubMed:12026180}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:25115560}.
CC -!- SIMILARITY: Belongs to the pectinacetylesterase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26093.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC012393; AAF26093.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC013454; AAF23225.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74314.1; -; Genomic_DNA.
DR EMBL; AF428303; AAL16135.1; -; mRNA.
DR EMBL; AY050847; AAK92782.1; -; mRNA.
DR EMBL; AY096751; AAM20385.1; -; mRNA.
DR RefSeq; NP_566263.1; NM_111465.5. [Q9SFF6-1]
DR AlphaFoldDB; Q9SFF6; -.
DR SMR; Q9SFF6; -.
DR STRING; 3702.AT3G05910.1; -.
DR ESTHER; arath-Q9SFF6; Pectinacetylesterase-Notum.
DR iPTMnet; Q9SFF6; -.
DR PaxDb; Q9SFF6; -.
DR PRIDE; Q9SFF6; -.
DR ProteomicsDB; 248886; -. [Q9SFF6-1]
DR EnsemblPlants; AT3G05910.1; AT3G05910.1; AT3G05910. [Q9SFF6-1]
DR GeneID; 819760; -.
DR Gramene; AT3G05910.1; AT3G05910.1; AT3G05910. [Q9SFF6-1]
DR KEGG; ath:AT3G05910; -.
DR Araport; AT3G05910; -.
DR TAIR; locus:2074459; AT3G05910.
DR eggNOG; KOG4287; Eukaryota.
DR HOGENOM; CLU_031008_0_0_1; -.
DR InParanoid; Q9SFF6; -.
DR OMA; FFYNKTE; -.
DR OrthoDB; 610784at2759; -.
DR PhylomeDB; Q9SFF6; -.
DR PRO; PR:Q9SFF6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SFF6; baseline and differential.
DR Genevisible; Q9SFF6; 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; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..415
FT /note="Pectin acetylesterase 12"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431777"
FT ACT_SITE 197
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 293
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 360
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 415 AA; 46327 MW; 4131CC9C66D35269 CRC64;
MVKLLLVGFV VAGIILGTQA NEYLDFNVTE IDRIEELEFG FSKYSSNLNP LMVGLTLIRG
ADSGAVCLDG TLPGYHLHRG HGSGANSWLI QLEGGGWCNN IRTCVYRKTT RRGSSNYMEK
QLQFTGILSD KAQENPDFFN WNRVKLRYCD GASFSGDGQN QAAQLQFRGE RIWRAAIDDL
KANGMRYANQ ALLSGCSAGG LAAILRCDEF RNLFPGSTKV KCLSDAGLFL DTADVSGGRT
IRNLYNGVVE LQSVKNNLPR ICTNHLDPTS CFFPQNLISQ MKTPLFIVNA AYDTWQIQSS
IAPTSADPSG FWHDCRLNHG KCTPAQLRFL QGFREQMLRV VKGFSMSRQN GLFINSCFAH
CQTERQDTWF ADDSPVIRKK AVAIAVGDWY FDRAEVKLVD CPYPCDKSCH NLVFR
