PMI12_ARATH
ID PMI12_ARATH Reviewed; 174 AA.
AC Q9FJR5;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Pectinesterase inhibitor 12 {ECO:0000305};
DE AltName: Full=Pectin methylesterase inhibitor 12 {ECO:0000303|PubMed:28082716};
DE Short=AtPMEI12 {ECO:0000303|PubMed:28082716};
DE Flags: Precursor;
GN Name=PMEI12 {ECO:0000303|PubMed:28082716};
GN OrderedLocusNames=At5g46960 {ECO:0000312|Araport:AT5G46960};
GN ORFNames=MQD22.10 {ECO:0000312|EMBL:BAB10235.1};
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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; AB013394; BAB10235.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95452.1; -; Genomic_DNA.
DR RefSeq; NP_568673.1; NM_124067.2.
DR AlphaFoldDB; Q9FJR5; -.
DR SMR; Q9FJR5; -.
DR STRING; 3702.AT5G46960.1; -.
DR iPTMnet; Q9FJR5; -.
DR PaxDb; Q9FJR5; -.
DR PRIDE; Q9FJR5; -.
DR ProteomicsDB; 226156; -.
DR EnsemblPlants; AT5G46960.1; AT5G46960.1; AT5G46960.
DR GeneID; 834742; -.
DR Gramene; AT5G46960.1; AT5G46960.1; AT5G46960.
DR KEGG; ath:AT5G46960; -.
DR Araport; AT5G46960; -.
DR TAIR; locus:2171032; AT5G46960.
DR HOGENOM; CLU_033761_7_2_1; -.
DR InParanoid; Q9FJR5; -.
DR OMA; PNTCEDG; -.
DR OrthoDB; 1302136at2759; -.
DR PhylomeDB; Q9FJR5; -.
DR PRO; PR:Q9FJR5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJR5; baseline and differential.
DR GO; GO:0048046; C:apoplast; IDA:UniProtKB.
DR GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0071669; P:plant-type cell wall organization or biogenesis; IMP:UniProtKB.
DR CDD; cd15795; PMEI-Pla_a_1_like; 1.
DR Gene3D; 1.20.140.40; -; 1.
DR InterPro; IPR035513; Invertase/methylesterase_inhib.
DR InterPro; IPR006501; Pectinesterase_inhib_dom.
DR InterPro; IPR034088; Pla_a_1-like.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..174
FT /note="Pectinesterase inhibitor 12"
FT /id="PRO_5008429892"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 28..43
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
FT DISULFID 100..140
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
SQ SEQUENCE 174 AA; 19070 MW; B24E087F73C1DF3D CRC64;
MKFLVSLVIF SLFLNGFATA QTLIQDSCKK AFAKDPQLSY DFCVNSLTQD PQSKAATTLE
SLVLASTKTA AAKITNLKGI VAQDLKDQRY QDIVEDLKLC LGFYNDANDD LTTALANIKS
RDYQGANINL SAALDVPGNC EDDFKEAKKT SPITNENSIL FKTILIPLAF TNML
