PMI28_ORYSJ
ID PMI28_ORYSJ Reviewed; 227 AA.
AC Q0J8J8; Q6ZD64;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Pectinesterase inhibitor 28 {ECO:0000305};
DE AltName: Full=Pectin methylesterase inhibitor 28 {ECO:0000303|PubMed:26874295};
DE Short=OsPMEI28 {ECO:0000303|PubMed:26874295};
DE Flags: Precursor;
GN Name=PMEI28 {ECO:0000303|PubMed:26874295};
GN OrderedLocusNames=Os08g0108100 {ECO:0000312|EMBL:BAF22717.1},
GN LOC_Os08g01670 {ECO:0000305};
GN ORFNames=P0450B04.30 {ECO:0000312|EMBL:BAD09396.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [5]
RP INDUCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=26874295; DOI=10.1016/j.plaphy.2016.01.021;
RA Nguyen H.P., Jeong H.Y., Kim H., Kim Y.C., Lee C.;
RT "Molecular and biochemical characterization of rice pectin methylesterase
RT inhibitors (OsPMEIs).";
RL Plant Physiol. Biochem. 101:105-112(2016).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=27889517; DOI=10.1016/j.jplph.2016.11.006;
RA Nguyen H.P., Jeong H.Y., Jeon S.H., Kim D., Lee C.;
RT "Rice pectin methylesterase inhibitor28 (OsPMEI28) encodes a functional
RT PMEI and its overexpression results in a dwarf phenotype through increased
RT pectin methylesterification levels.";
RL J. Plant Physiol. 208:17-25(2017).
CC -!- FUNCTION: Pectin methylesterase (PME) inhibitor that inhibits PME in
CC vitro. Functions as a critical structural modulator by regulating the
CC degree of pectin methylesterification and the physiochemical properties
CC of the cell wall components. {ECO:0000269|PubMed:27889517}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250|UniProtKB:Q6ETW4}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, culms and flag leaves.
CC {ECO:0000269|PubMed:27889517}.
CC -!- INDUCTION: Induced by cold stress. Down-regulated by drought stress.
CC {ECO:0000269|PubMed:26874295}.
CC -!- MISCELLANEOUS: Plants over-expressing PMEI28 are dwarf and have
CC shortened culm length, due to increased level of pectin
CC methylesterification. {ECO:0000269|PubMed:27889517}.
CC -!- SIMILARITY: Belongs to the PMEI family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD09396.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AP004462; BAD09396.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008214; BAF22717.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT03473.1; -; Genomic_DNA.
DR EMBL; AK070037; BAG91735.1; -; mRNA.
DR RefSeq; XP_015650603.1; XM_015795117.1.
DR AlphaFoldDB; Q0J8J8; -.
DR SMR; Q0J8J8; -.
DR STRING; 4530.OS08T0108100-01; -.
DR PaxDb; Q0J8J8; -.
DR PRIDE; Q0J8J8; -.
DR EnsemblPlants; Os08t0108100-01; Os08t0108100-01; Os08g0108100.
DR GeneID; 4344463; -.
DR Gramene; Os08t0108100-01; Os08t0108100-01; Os08g0108100.
DR KEGG; osa:4344463; -.
DR eggNOG; ENOG502RXIR; Eukaryota.
DR HOGENOM; CLU_033761_5_1_1; -.
DR InParanoid; Q0J8J8; -.
DR OMA; ATIMVKI; -.
DR OrthoDB; 1439149at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
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:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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; Growth regulation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..227
FT /note="Pectinesterase inhibitor 28"
FT /evidence="ECO:0000255"
FT /id="PRO_5009341578"
FT REGION 28..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 66..75
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
FT DISULFID 139..179
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
SQ SEQUENCE 227 AA; 22476 MW; 39A97878C714069A CRC64;
MASSMAPAAA MAILLLALLM PATLCSRSGP PSSKHGHGGH AKRAPPPASP VVPVAPQAAA
LVRATCNSTA YYDVCVSALA ADPSSTTADV RGLSAIAVSV AAANASGAAQ AAAALANGTA
PLAAAAAGDG TVQALLRACA GKYGDARDAL AAAKESMGQQ DYDLATVHVS AGAEYPQVCK
ALFRRQRPGA YPAELAAREE ALNKLCSVAL DIIALLTSSP ASNNNNS
