PAE6_ARATH
ID PAE6_ARATH Reviewed; 419 AA.
AC Q84JS1; Q9M1R8;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Pectin acetylesterase 6 {ECO:0000303|PubMed:25115560};
DE EC=3.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=PAE6 {ECO:0000303|PubMed:25115560};
GN OrderedLocusNames=At3g62060 {ECO:0000312|Araport:AT3G62060};
GN ORFNames=T17J13.20 {ECO:0000312|EMBL:CAB71866.1};
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].
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB71866.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL138651; CAB71866.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80302.1; -; Genomic_DNA.
DR EMBL; BT003870; AAO41919.1; -; mRNA.
DR EMBL; BT005088; AAO50621.1; -; mRNA.
DR PIR; T47998; T47998.
DR RefSeq; NP_191765.2; NM_116071.5.
DR AlphaFoldDB; Q84JS1; -.
DR SMR; Q84JS1; -.
DR STRING; 3702.AT3G62060.1; -.
DR ESTHER; arath-Q84JS1; Pectinacetylesterase-Notum.
DR PaxDb; Q84JS1; -.
DR PRIDE; Q84JS1; -.
DR ProteomicsDB; 236318; -.
DR EnsemblPlants; AT3G62060.1; AT3G62060.1; AT3G62060.
DR GeneID; 825379; -.
DR Gramene; AT3G62060.1; AT3G62060.1; AT3G62060.
DR KEGG; ath:AT3G62060; -.
DR Araport; AT3G62060; -.
DR TAIR; locus:2097973; AT3G62060.
DR eggNOG; KOG4287; Eukaryota.
DR HOGENOM; CLU_031008_0_0_1; -.
DR InParanoid; Q84JS1; -.
DR OMA; THRVAQT; -.
DR PhylomeDB; Q84JS1; -.
DR PRO; PR:Q84JS1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84JS1; baseline and differential.
DR Genevisible; Q84JS1; 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 Cell wall; Cell wall biogenesis/degradation; Glycoprotein; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..419
FT /note="Pectin acetylesterase 6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431771"
FT ACT_SITE 200
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 296
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 363
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 419 AA; 46479 MW; 74F77CF19B4C159B CRC64;
MRSLLLWIAV VVCLLCSVAA VVQSGSSDGF GKPRDTETAI SFLEYKLMAP SVPMIPLTLI
HGADSKGAVC LDGTLPGYHL DRGFGSGANS WLIQLEGGGW CNNHRSCVYR KTSRRGSSKF
MEKALAFTGI LSNRSEENPD FFNWNRIKLR YCDGASFSGD SQDESSQLFY RGQRIWQVAM
EEFLSLGMKQ ANQALLSGCS AGGLASILHC DEFRELLPSS TKVKCLSDAG MFLDSVDVSG
GHSLRNMFQG VVTVQNLQKD LSSTCTNHLD PTSCFFPQNL VSDIKTPMFL LNTAYDSWQI
QESLAPPTAD PGGIWKACKS DHSRCNSSQI QFFQEFRNQM LFAVNSFSNS DQNGLYINSC
FAHCQTERQD TWFAQDSPQL NGKRVAESVG DWYFDRAKNV KAIDCPYPCD TTCHNLIFE
