PMEI4_ARATH
ID PMEI4_ARATH Reviewed; 199 AA.
AC Q9SB38; Q8LEH1;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Pectinesterase inhibitor 4 {ECO:0000305};
DE AltName: Full=Pectin methylesterase inhibitor 4 {ECO:0000303|PubMed:20819179};
DE Short=AtPMEI4 {ECO:0000305};
DE Flags: Precursor;
GN Name=PMEI4 {ECO:0000303|PubMed:20819179};
GN OrderedLocusNames=At4g25250 {ECO:0000312|Araport:AT4G25250};
GN ORFNames=F24A6.90 {ECO:0000312|EMBL:CAA23066.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=20819179; DOI=10.1111/j.1469-8137.2010.03409.x;
RA Pelletier S., Van Orden J., Wolf S., Vissenberg K., Delacourt J.,
RA Ndong Y.A., Pelloux J., Bischoff V., Urbain A., Mouille G., Lemonnier G.,
RA Renou J.P., Hoefte H.;
RT "A role for pectin de-methylesterification in a developmentally regulated
RT growth acceleration in dark-grown Arabidopsis hypocotyls.";
RL New Phytol. 188:726-739(2010).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25826258; DOI=10.4161/15592324.2014.983351;
RA Senechal F., Mareck A., Marcelo P., Lerouge P., Pelloux J.;
RT "Arabidopsis PME17 activity can be controlled by pectin methylesterase
RT inhibitor4.";
RL Plant Signal. Behav. 10:E983351-E983351(2015).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=28034952; DOI=10.1104/pp.16.01790;
RA Hocq L., Senechal F., Lefebvre V., Lehner A., Domon J.M., Mollet J.C.,
RA Dehors J., Pageau K., Marcelo P., Guerineau F., Kolsek K., Mercadante D.,
RA Pelloux J.;
RT "Combined experimental and computational approaches reveal distinct pH-
RT dependence of pectin methyl esterase inhibitors.";
RL Plant Physiol. 173:1075-1093(2017).
CC -!- FUNCTION: Pectin methylesterase (PME) inhibitor that can target the
CC root-expressed PME17, regulate de-methylesterification of pectins in
CC roots and affects root growth. {ECO:0000269|PubMed:25826258}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250|UniProtKB:Q9STY5}.
CC -!- TISSUE SPECIFICITY: Expressed in outer cell layer of roots,
CC particularly in the root-hair zone (PubMed:25826258). Expressed in
CC roots and siliques (PubMed:28034952). {ECO:0000269|PubMed:25826258,
CC ECO:0000269|PubMed:28034952}.
CC -!- DEVELOPMENTAL STAGE: developmentally up-regulated in roots during
CC growth acceleration of dark-grown hypocotyls.
CC {ECO:0000269|PubMed:20819179}.
CC -!- SIMILARITY: Belongs to the PMEI family. {ECO:0000305}.
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DR EMBL; AL035396; CAA23066.1; -; Genomic_DNA.
DR EMBL; AL161563; CAB81336.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85031.1; -; Genomic_DNA.
DR EMBL; BT004588; AAO42834.1; -; mRNA.
DR EMBL; AK227550; BAE99546.1; -; mRNA.
DR EMBL; AY085416; AAM62643.1; -; mRNA.
DR PIR; T05546; T05546.
DR RefSeq; NP_194255.1; NM_118657.3.
DR AlphaFoldDB; Q9SB38; -.
DR SMR; Q9SB38; -.
DR STRING; 3702.AT4G25250.1; -.
DR PaxDb; Q9SB38; -.
DR PRIDE; Q9SB38; -.
DR ProteomicsDB; 226209; -.
DR DNASU; 828628; -.
DR EnsemblPlants; AT4G25250.1; AT4G25250.1; AT4G25250.
DR GeneID; 828628; -.
DR Gramene; AT4G25250.1; AT4G25250.1; AT4G25250.
DR KEGG; ath:AT4G25250; -.
DR Araport; AT4G25250; -.
DR TAIR; locus:2122699; AT4G25250.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_033761_0_2_1; -.
DR InParanoid; Q9SB38; -.
DR OMA; QNYKTFV; -.
DR OrthoDB; 1403601at2759; -.
DR PhylomeDB; Q9SB38; -.
DR PRO; PR:Q9SB38; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SB38; baseline and differential.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
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:2000280; P:regulation of root development; 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..199
FT /note="Pectinesterase inhibitor 4"
FT /id="PRO_5008430272"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 42..51
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
FT DISULFID 109..158
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
FT CONFLICT 6
FT /note="V -> I (in Ref. 5; AAM62643)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="L -> I (in Ref. 5; AAM62643)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="K -> N (in Ref. 5; AAM62643)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="A -> T (in Ref. 5; AAM62643)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="M -> I (in Ref. 5; AAM62643)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="I -> V (in Ref. 5; AAM62643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 21897 MW; 483659A1318E8330 CRC64;
MLRFVVLSLT LMVFINSSNF PKTAATPPGT YQNHTTYVKT ACNSTTYPTM CYNCLSSYSS
TIKSDPIKLC TTSLNLNVKS AKNATLVVSN LLQKAKAAKS HEVSILKDCV DEMKDTIDEL
KQAVAEMKYV RGGGKTTEEH LKNVKTWVSS ALTDEGTCTD GFEEGRVNVE TKKKVKKAIS
ELSKTTSNTL ALLTHYLSY
