PMI11_ARATH
ID PMI11_ARATH Reviewed; 202 AA.
AC Q9STY5;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Pectinesterase inhibitor 11 {ECO:0000305};
DE AltName: Full=Pectin methylesterase inhibitor 11 {ECO:0000303|PubMed:28082716};
DE Short=AtPMEI11 {ECO:0000303|PubMed:28082716};
DE Flags: Precursor;
GN Name=PMEI11 {ECO:0000303|PubMed:28082716};
GN OrderedLocusNames=At3g47380 {ECO:0000312|Araport:AT3G47380};
GN ORFNames=T21L8.130 {ECO:0000312|EMBL:CAB51210.1};
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 FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
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 involved in the
CC maintenance of cell wall integrity in response to necrotrophic
CC pathogens. Modulates PME activity and pectin methylesterification
CC during infection by Botrytis cinerea and contributes to resistance
CC against the pathogen. {ECO:0000269|PubMed:28082716}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:28082716}.
CC -!- INDUCTION: Induced in leaves during infection by Botrytis cinerea.
CC {ECO:0000269|PubMed:28082716}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have enhanced susceptibility to infection
CC by the necrotrophic pathogen Botrytis cinerea.
CC {ECO:0000269|PubMed:28082716}.
CC -!- SIMILARITY: Belongs to the PMEI family. {ECO:0000305}.
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DR EMBL; AL096860; CAB51210.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78274.1; -; Genomic_DNA.
DR PIR; T12993; T12993.
DR RefSeq; NP_190322.1; NM_114606.3.
DR AlphaFoldDB; Q9STY5; -.
DR SMR; Q9STY5; -.
DR STRING; 3702.AT3G47380.1; -.
DR PaxDb; Q9STY5; -.
DR PRIDE; Q9STY5; -.
DR ProteomicsDB; 234749; -.
DR EnsemblPlants; AT3G47380.1; AT3G47380.1; AT3G47380.
DR GeneID; 823892; -.
DR Gramene; AT3G47380.1; AT3G47380.1; AT3G47380.
DR KEGG; ath:AT3G47380; -.
DR Araport; AT3G47380; -.
DR TAIR; locus:2099545; AT3G47380.
DR eggNOG; ENOG502QXIN; Eukaryota.
DR HOGENOM; CLU_033761_0_2_1; -.
DR InParanoid; Q9STY5; -.
DR OMA; KMCGSAK; -.
DR OrthoDB; 1528760at2759; -.
DR PhylomeDB; Q9STY5; -.
DR PRO; PR:Q9STY5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9STY5; baseline and differential.
DR GO; GO:0048046; C:apoplast; IDA:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IBA:GO_Central.
DR GO; GO:0071669; P:plant-type cell wall organization or biogenesis; 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 Apoplast; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..202
FT /note="Pectinesterase inhibitor 11"
FT /id="PRO_5008430396"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 43..52
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
FT DISULFID 109..160
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
SQ SEQUENCE 202 AA; 22226 MW; 04FA1D5B69BF21E6 CRC64;
MAKQIFYTLF LFLLSTAILT ASSSAPRAAI TSKRAINFIQ ASCKATTYPT VCVNSLTGYA
NSIQTSPRRL AETALNVTVT QAQSTKVFVW RLGRFTSLKK REIQAVKDCI EEIHDAVDRL
TMSIHEVKMC GSAKGRDQFW FHMSNAQTWT SAALTNANTC SDGFAGRVMD GRVKNSVRAR
ILNLGRGTSN ALALINAFAK KY
