PMEI9_ARATH
ID PMEI9_ARATH Reviewed; 204 AA.
AC Q9SI72; Q0WU20;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Pectinesterase inhibitor 9 {ECO:0000305};
DE AltName: Full=Pectin methylesterase inhibitor 9 {ECO:0000303|PubMed:28034952};
DE Short=AtPMEI9 {ECO:0000303|PubMed:28034952};
DE Flags: Precursor;
GN Name=PMEI9 {ECO:0000303|PubMed:28034952};
GN OrderedLocusNames=At1g62770 {ECO:0000312|Araport:AT1G62770};
GN ORFNames=F23N19.14 {ECO:0000312|EMBL:AAF19545.1};
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 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 [4]
RP FUNCTION, AND 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 probably targets
CC root-expressed PME, regulates de-methylesterification of pectins in
CC roots and affects root growth. {ECO:0000269|PubMed:28034952}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250|UniProtKB:Q9STY5}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and etiolated hypocotyls.
CC Expressed in seedlings, leaves, stems, siliques, floral buds and mature
CC seeds. {ECO:0000269|PubMed:28034952}.
CC -!- SIMILARITY: Belongs to the PMEI family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE99378.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC007190; AAF19545.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34002.1; -; Genomic_DNA.
DR EMBL; AK227371; BAE99378.1; ALT_FRAME; mRNA.
DR RefSeq; NP_564802.1; NM_104955.3.
DR AlphaFoldDB; Q9SI72; -.
DR SMR; Q9SI72; -.
DR STRING; 3702.AT1G62770.1; -.
DR PaxDb; Q9SI72; -.
DR PRIDE; Q9SI72; -.
DR ProteomicsDB; 234782; -.
DR EnsemblPlants; AT1G62770.1; AT1G62770.1; AT1G62770.
DR GeneID; 842576; -.
DR Gramene; AT1G62770.1; AT1G62770.1; AT1G62770.
DR KEGG; ath:AT1G62770; -.
DR Araport; AT1G62770; -.
DR TAIR; locus:2026237; AT1G62770.
DR eggNOG; ENOG502QXIN; Eukaryota.
DR HOGENOM; CLU_033761_0_2_1; -.
DR InParanoid; Q9SI72; -.
DR OMA; RAVKDCI; -.
DR OrthoDB; 1528760at2759; -.
DR PhylomeDB; Q9SI72; -.
DR PRO; PR:Q9SI72; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SI72; 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:TAIR.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IBA:GO_Central.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..204
FT /note="Pectinesterase inhibitor 9"
FT /id="PRO_5008430306"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 38..47
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
FT DISULFID 106..157
FT /evidence="ECO:0000250|UniProtKB:Q9LNF2"
SQ SEQUENCE 204 AA; 22684 MW; 04666120F8E11925 CRC64;
MELKNTIFLV ILLSITILQS SSATPNRSES DQFIVSSCQT TQYPSLCVHT LSAYATKIRH
NNDQDLAQTA LIISLARAKS VTIFVAKLTK ETPKFKRREY LAIKDCIEVL GNSVDRLAQS
VKELARAGHA VASEDFMWKM SNVQTWVSAA LTDETTCLDG FSERAMGGKV KRLIRYKVVH
VAQVTSNALA LVNQFAEKRS VKFP
