PAE1_ARATH
ID PAE1_ARATH Reviewed; 388 AA.
AC F4I107; O80537;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Pectin acetylesterase 1 {ECO:0000303|PubMed:25115560};
DE EC=3.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=PAE1 {ECO:0000303|PubMed:25115560};
GN OrderedLocusNames=At1g09550 {ECO:0000312|Araport:AT1G09550};
GN ORFNames=F14J9.21 {ECO:0000312|EMBL:AAC33215.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC33215.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC003970; AAC33215.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE28460.1; -; Genomic_DNA.
DR PIR; B86229; B86229.
DR RefSeq; NP_172426.2; NM_100826.3.
DR AlphaFoldDB; F4I107; -.
DR SMR; F4I107; -.
DR STRING; 3702.AT1G09550.1; -.
DR ESTHER; arath-pae1; Pectinacetylesterase-Notum.
DR PaxDb; F4I107; -.
DR PRIDE; F4I107; -.
DR ProteomicsDB; 236316; -.
DR EnsemblPlants; AT1G09550.1; AT1G09550.1; AT1G09550.
DR GeneID; 837481; -.
DR Gramene; AT1G09550.1; AT1G09550.1; AT1G09550.
DR KEGG; ath:AT1G09550; -.
DR Araport; AT1G09550; -.
DR TAIR; locus:2012245; AT1G09550.
DR eggNOG; KOG4287; Eukaryota.
DR HOGENOM; CLU_031008_0_0_1; -.
DR InParanoid; F4I107; -.
DR OMA; CTSHIKP; -.
DR OrthoDB; 610784at2759; -.
DR PRO; PR:F4I107; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I107; baseline and differential.
DR Genevisible; F4I107; 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 3: Inferred from homology;
KW Cell wall; Cell wall biogenesis/degradation; Glycoprotein; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..388
FT /note="Pectin acetylesterase 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431766"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 283
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 349
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 388 AA; 42345 MW; 6FA038326E24880D CRC64;
MKTLLYWGWS SLAGLILFSI LAHGEMKTFN ESNGTNANVL MVGLTLVQAA AAKGAVCLDG
SVPGYHLCRG YGSGANNWII QLQGGAWCDS IQNCQSRKGS GYGSSTLMEK ELAFLGLLSN
KAAENPDFYN WNKVKVRYCD GASFDGDSEN KAAQLQYRGK RIFLAVMEDL MEKGMRQAKQ
ALLSGCSSGG LSAILRCDDF NNLFPPTTTV KCMSDAGFFL DAVDVSGGHS LRRMYSGVVN
TQGLQNTLPP TCTSHIKPFL CFFPQYIINQ VKTPLFILNS GFDSWQIGNS LAPPSADKSG
SWHNCSFSFR CTASQMHFLE GFKMSMLDAL KTFSKFSKNG VLITSGWAHC QAERQDTWFP
GYSGAGKAKG IAVAVGDWYF ERTKQNSS
