PMI10_ARATH
ID PMI10_ARATH Reviewed; 312 AA.
AC Q9SI74;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Pectinesterase inhibitor 10 {ECO:0000305};
DE AltName: Full=Pectin methylesterase inhibitor 10 {ECO:0000303|PubMed:28082716};
DE Short=AtPMEI10 {ECO:0000303|PubMed:28082716};
DE Flags: Precursor;
GN Name=PMEI10 {ECO:0000303|PubMed:28082716};
GN OrderedLocusNames=At1g62760 {ECO:0000312|Araport:AT1G62760};
GN ORFNames=F23N19.12 {ECO:0000312|EMBL:AAF19547.1};
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 FUNCTION, 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:0000250|UniProtKB:Q9STY5}.
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; AC007190; AAF19547.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34001.1; -; Genomic_DNA.
DR RefSeq; NP_176463.2; NM_104953.3.
DR AlphaFoldDB; Q9SI74; -.
DR SMR; Q9SI74; -.
DR STRING; 3702.AT1G62760.1; -.
DR PaxDb; Q9SI74; -.
DR PRIDE; Q9SI74; -.
DR ProteomicsDB; 234748; -.
DR EnsemblPlants; AT1G62760.1; AT1G62760.1; AT1G62760.
DR GeneID; 842574; -.
DR Gramene; AT1G62760.1; AT1G62760.1; AT1G62760.
DR KEGG; ath:AT1G62760; -.
DR Araport; AT1G62760; -.
DR TAIR; locus:2026227; AT1G62760.
DR eggNOG; ENOG502S0CF; Eukaryota.
DR HOGENOM; CLU_892393_0_0_1; -.
DR InParanoid; Q9SI74; -.
DR OMA; ASHAMNE; -.
DR OrthoDB; 1204976at2759; -.
DR PhylomeDB; Q9SI74; -.
DR PRO; PR:Q9SI74; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SI74; 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: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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..312
FT /note="Pectinesterase inhibitor 10"
FT /id="PRO_5008430293"
FT REGION 24..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 152..161
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
FT DISULFID 218..268
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
SQ SEQUENCE 312 AA; 32354 MW; F526A966D49928D3 CRC64;
MNILSQTQIL HLSIAILLFI TTSSSSLSPS SSSPSLSPSP PSSSPSSAPP SSLSPSSPPP
LSLSPSSPPP PPPSSSPLSS LSPSLSPSPP SSSPSSAPPS SLSPSSPPPL SLSPSSPPPP
PPSSSPLSSL SPSSSSSTYS NQTNLDYIKT SCNITLYKTI CYNSLSPYAS TIRSNPQKLA
VIALNLTLSS AKSASKFVKN ISHGGGLTRL EVVAVADCVE EIGDSVTSLQ DSIRELDSIN
YKDSAKFEMV MSDVETWVSA ALTNDDTCMD GFSLVKTAVK DLVRRHVVEV ARLTSNALAL
INMYASTQEN FS
