PMEI3_ARATH
ID PMEI3_ARATH Reviewed; 205 AA.
AC Q84WE4; Q8LE11;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Pectinesterase inhibitor 3 {ECO:0000305};
DE AltName: Full=Pectin methylesterase inhibitor 3 {ECO:0000303|PubMed:19097903};
DE Short=AtPMEI3 {ECO:0000303|PubMed:28082716};
DE Flags: Precursor;
GN Name=PMEI3 {ECO:0000303|PubMed:19097903};
GN OrderedLocusNames=At5g20740 {ECO:0000312|Araport:AT5G20740};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19097903; DOI=10.1016/j.cub.2008.10.065;
RA Peaucelle A., Louvet R., Johansen J.N., Hoefte H., Laufs P., Pelloux J.,
RA Mouille G.;
RT "Arabidopsis phyllotaxis is controlled by the methyl-esterification status
RT of cell-wall pectins.";
RL Curr. Biol. 18:1943-1948(2008).
RN [7]
RP INDUCTION.
RX PubMed=28082716; DOI=10.1104/pp.16.01185;
RA Lionetti V., Fabri E., De Caroli M., Hansen A.R., Willats W.G., Piro G.,
RA Bellincampi D.;
RT "Three pectin methyl esterase inhibitors protect cell wall integrity for
RT immunity to Botrytis.";
RL Plant Physiol. 173:1844-1863(2017).
CC -!- FUNCTION: Pectin methylesterase (PME) inhibitor that regulates de-
CC methylesterification of pectins in the apical meristem and affects
CC primordia formation and phyllotactic patterning.
CC {ECO:0000269|PubMed:19097903}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250|UniProtKB:Q9STY5}.
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=Q84WE4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in apical meristem.
CC {ECO:0000269|PubMed:19097903}.
CC -!- INDUCTION: Down-regulated in leaves during infection with Botrytis
CC cinerea. {ECO:0000269|PubMed:28082716}.
CC -!- SIMILARITY: Belongs to the PMEI family. {ECO:0000305}.
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DR EMBL; AF296832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92888.1; -; Genomic_DNA.
DR EMBL; BT003915; AAO41962.1; -; mRNA.
DR EMBL; BT020562; AAW70408.1; -; mRNA.
DR EMBL; AY085686; AAM62905.1; -; mRNA.
DR RefSeq; NP_197574.1; NM_122081.3. [Q84WE4-1]
DR AlphaFoldDB; Q84WE4; -.
DR SMR; Q84WE4; -.
DR STRING; 3702.AT5G20740.1; -.
DR PaxDb; Q84WE4; -.
DR ProteomicsDB; 236646; -. [Q84WE4-1]
DR EnsemblPlants; AT5G20740.1; AT5G20740.1; AT5G20740. [Q84WE4-1]
DR GeneID; 832197; -.
DR Gramene; AT5G20740.1; AT5G20740.1; AT5G20740. [Q84WE4-1]
DR KEGG; ath:AT5G20740; -.
DR Araport; AT5G20740; -.
DR TAIR; locus:2180484; AT5G20740.
DR eggNOG; ENOG502RXR5; Eukaryota.
DR HOGENOM; CLU_033761_0_2_1; -.
DR InParanoid; Q84WE4; -.
DR OMA; WQMSNAE; -.
DR PhylomeDB; Q84WE4; -.
DR PRO; PR:Q84WE4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84WE4; baseline and differential.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004857; F:enzyme inhibitor activity; IBA:GO_Central.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IBA:GO_Central.
DR GO; GO:1902183; P:regulation of shoot apical meristem development; IMP:UniProtKB.
DR Gene3D; 1.20.140.40; -; 1.
DR InterPro; IPR035513; Invertase/methylesterase_inhib.
DR InterPro; IPR006501; Pectinesterase_inhib_dom.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF101148; SSF101148; 1.
DR TIGRFAMs; TIGR01614; PME_inhib; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Apoplast; Disulfide bond; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..205
FT /note="Pectinesterase inhibitor 3"
FT /id="PRO_5008428148"
FT DISULFID 38..47
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
FT DISULFID 104..156
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
FT CONFLICT 4
FT /note="T -> P (in Ref. 5; AAM62905)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="T -> I (in Ref. 5; AAM62905)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="E -> G (in Ref. 5; AAM62905)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="V -> I (in Ref. 5; AAM62905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 205 AA; 22329 MW; 0CA6D118B9CE904E CRC64;
MAPTQNLFLV AIAFAVIFTA STVHGRHNGA EDIVHSSCEH ASYPSLCVRT LSSYSGPTIT
NRRDLAQAAI KISLSHAQSA AKKLAVVRDS VGKKKQEKAA LVDCVEMIGD SVDELSRTLG
VLKHLRVSGG SAKEFRWQMS NAQTWASAAL TDDDTCLDGF QGMDDGEIKT EVKQWMTKVA
RVTSNALYMV NQLDETRGKP HDVHL