PMEI2_ARATH
ID PMEI2_ARATH Reviewed; 173 AA.
AC Q9LUV1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Pectinesterase inhibitor 2 {ECO:0000305};
DE AltName: Full=Pectin methylesterase inhibitor 2 {ECO:0000303|PubMed:14675772};
DE Short=AtPMEI2 {ECO:0000303|PubMed:14675772};
DE Flags: Precursor;
GN Name=PMEI2 {ECO:0000303|PubMed:14675772}; OrderedLocusNames=At3g17220;
GN ORFNames=MGD8.3;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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, AND TISSUE SPECIFICITY.
RX PubMed=14675772; DOI=10.1016/s0014-5793(03)01344-9;
RA Wolf S., Grsic-Rausch S., Rausch T., Greiner S.;
RT "Identification of pollen-expressed pectin methylesterase inhibitors in
RT Arabidopsis.";
RL FEBS Lett. 555:551-555(2003).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=14741367; DOI=10.1016/s0014-5793(03)01491-1;
RA Raiola A., Camardella L., Giovane A., Mattei B., De Lorenzo G., Cervone F.,
RA Bellincampi D.;
RT "Two Arabidopsis thaliana genes encode functional pectin methylesterase
RT inhibitors.";
RL FEBS Lett. 557:199-203(2004).
RN [5]
RP INTERACTION WITH PPME1, AND TISSUE SPECIFICITY.
RX PubMed=17971035; DOI=10.1111/j.1365-313x.2007.03325.x;
RA Roeckel N., Wolf S., Kost B., Rausch T., Greiner S.;
RT "Elaborate spatial patterning of cell-wall PME and PMEI at the pollen tube
RT tip involves PMEI endocytosis, and reflects the distribution of esterified
RT and de-esterified pectins.";
RL Plant J. 53:133-143(2008).
CC -!- FUNCTION: Inhibits pectin methylesterase (PME) from flowers, siliques
CC and pollen tube. {ECO:0000269|PubMed:14675772}.
CC -!- SUBUNIT: Interacts with PPME1. {ECO:0000269|PubMed:17971035}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250|UniProtKB:Q9LNF2}.
CC -!- TISSUE SPECIFICITY: Highest expression in flowers (PubMed:14675772,
CC PubMed:14741367, PubMed:17971035). Expressed exclusively at the pollen
CC tube tip (PubMed:14675772, PubMed:17971035).
CC {ECO:0000269|PubMed:14675772, ECO:0000269|PubMed:14741367,
CC ECO:0000269|PubMed:17971035}.
CC -!- MISCELLANEOUS: The polarized accumulation at the pollen tube apex
CC depends at least in part on local endocytosis at the flanks of the tip.
CC -!- SIMILARITY: Belongs to the PMEI family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB022216; BAB02724.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75922.1; -; Genomic_DNA.
DR RefSeq; NP_188348.1; NM_112599.2.
DR AlphaFoldDB; Q9LUV1; -.
DR SMR; Q9LUV1; -.
DR BioGRID; 6314; 1.
DR STRING; 3702.AT3G17220.1; -.
DR PaxDb; Q9LUV1; -.
DR PRIDE; Q9LUV1; -.
DR ProteomicsDB; 234934; -.
DR EnsemblPlants; AT3G17220.1; AT3G17220.1; AT3G17220.
DR GeneID; 820981; -.
DR Gramene; AT3G17220.1; AT3G17220.1; AT3G17220.
DR KEGG; ath:AT3G17220; -.
DR Araport; AT3G17220; -.
DR TAIR; locus:2089010; AT3G17220.
DR eggNOG; ENOG502S9C3; Eukaryota.
DR HOGENOM; CLU_123543_1_0_1; -.
DR InParanoid; Q9LUV1; -.
DR OMA; CSKTQKP; -.
DR OrthoDB; 1198655at2759; -.
DR PhylomeDB; Q9LUV1; -.
DR PRO; PR:Q9LUV1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUV1; baseline and differential.
DR Genevisible; Q9LUV1; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR GO; GO:0090404; C:pollen tube tip; IDA:TAIR.
DR GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IDA:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IDA:TAIR.
DR CDD; cd15797; PMEI; 1.
DR Gene3D; 1.20.140.40; -; 1.
DR InterPro; IPR035513; Invertase/methylesterase_inhib.
DR InterPro; IPR006501; Pectinesterase_inhib_dom.
DR InterPro; IPR034086; PMEI_plant.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF101148; SSF101148; 1.
DR TIGRFAMs; TIGR01614; PME_inhib; 1.
PE 1: Evidence at protein level;
KW Apoplast; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..173
FT /note="Pectinesterase inhibitor 2"
FT /id="PRO_0000024707"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 34..43
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
FT DISULFID 99..139
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
SQ SEQUENCE 173 AA; 18367 MW; A84348F21048BFF0 CRC64;
MAAYLTNRVL MSSLMFFVMT GSLNAQVADI KAICGKAKNQ SFCTSYMKSN PKTSGADLQT
LANITFGSAQ TSASEGFRKI QSLVKTATNP TMKKAYTSCV QHYKSAISSL NDAKQSLASG
DGKGLNIKVS AAMEGPSTCE QDMADFKVDP SAVKNSGDFQ NICGIVLVIS NMM
