PMEI1_ARATH
ID PMEI1_ARATH Reviewed; 176 AA.
AC Q9LNF2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Pectinesterase inhibitor 1 {ECO:0000305};
DE AltName: Full=Pectin methylesterase inhibitor 1 {ECO:0000303|PubMed:14675772};
DE Short=AtPMEI1 {ECO:0000303|PubMed:14675772};
DE Flags: Precursor;
GN Name=PMEI1 {ECO:0000303|PubMed:14675772}; OrderedLocusNames=At1g48020;
GN ORFNames=F21D18.29, F21D18_23, T2J15.7;
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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND 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 [7]
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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 28-176, DISULFIDE BONDS, SUBUNIT,
RP AND MUTAGENESIS OF PRO-55.
RX PubMed=15528298; DOI=10.1105/tpc.104.025684;
RA Hothorn M., Wolf S., Aloy P., Greiner S., Scheffzek K.;
RT "Structural insights into the target specificity of plant invertase and
RT pectin methylesterase inhibitory proteins.";
RL Plant Cell 16:3437-3447(2004).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=21223393; DOI=10.1111/j.1365-313x.2010.04421.x;
RA De Caroli M., Lenucci M.S., Di Sansebastiano G.P., Dalessandro G.,
RA De Lorenzo G., Piro G.;
RT "Protein trafficking to the cell wall occurs through mechanisms
RT distinguishable from default sorting in tobacco.";
RL Plant J. 65:295-308(2011).
CC -!- FUNCTION: Inhibits pectin methylesterase (PME) from flowers and
CC siliques (PubMed:14675772). Inhibits PME from leaves (PubMed:14741367).
CC {ECO:0000269|PubMed:14675772, ECO:0000269|PubMed:14741367}.
CC -!- SUBUNIT: Monomer and homodimer. Interacts in vitro with PPME1.
CC {ECO:0000269|PubMed:15528298, ECO:0000269|PubMed:17971035}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:21223393}.
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 -!- DOMAIN: The N-terminal alpha-hairpin extension is required for
CC pectinmethylesterase inhibitor activity.
CC -!- SIMILARITY: Belongs to the PMEI family. {ECO:0000305}.
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DR EMBL; AC023673; AAF79530.1; -; Genomic_DNA.
DR EMBL; AC051631; AAG51524.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32238.1; -; Genomic_DNA.
DR EMBL; AK118003; BAC42636.1; -; mRNA.
DR EMBL; BT003715; AAO39943.1; -; mRNA.
DR RefSeq; NP_175236.1; NM_103698.3.
DR PDB; 1X8Z; X-ray; 2.86 A; A/B/C=28-176.
DR PDB; 1X90; X-ray; 2.68 A; A/B=28-176.
DR PDB; 1X91; X-ray; 1.50 A; A=28-176.
DR PDBsum; 1X8Z; -.
DR PDBsum; 1X90; -.
DR PDBsum; 1X91; -.
DR AlphaFoldDB; Q9LNF2; -.
DR SMR; Q9LNF2; -.
DR BioGRID; 26445; 1.
DR STRING; 3702.AT1G48020.1; -.
DR PaxDb; Q9LNF2; -.
DR PRIDE; Q9LNF2; -.
DR ProteomicsDB; 226185; -.
DR EnsemblPlants; AT1G48020.1; AT1G48020.1; AT1G48020.
DR GeneID; 841220; -.
DR Gramene; AT1G48020.1; AT1G48020.1; AT1G48020.
DR KEGG; ath:AT1G48020; -.
DR Araport; AT1G48020; -.
DR TAIR; locus:2023797; AT1G48020.
DR eggNOG; ENOG502S9C3; Eukaryota.
DR HOGENOM; CLU_123543_1_0_1; -.
DR InParanoid; Q9LNF2; -.
DR OMA; KSHYRIC; -.
DR OrthoDB; 1198655at2759; -.
DR PhylomeDB; Q9LNF2; -.
DR EvolutionaryTrace; Q9LNF2; -.
DR PRO; PR:Q9LNF2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNF2; baseline and differential.
DR GO; GO:0048046; C:apoplast; IDA:UniProtKB.
DR GO; GO:0090404; C:pollen tube tip; NAS: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 3D-structure; Apoplast; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..176
FT /note="Pectinesterase inhibitor 1"
FT /id="PRO_0000024706"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 35..44
FT /evidence="ECO:0000269|PubMed:15528298"
FT DISULFID 98..138
FT /evidence="ECO:0000269|PubMed:15528298"
FT MUTAGEN 55
FT /note="P->A: Inhibits dimer formation and reduces
FT inhibitory activity."
FT /evidence="ECO:0000269|PubMed:15528298"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1X91"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:1X91"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:1X91"
FT HELIX 57..85
FT /evidence="ECO:0007829|PDB:1X91"
FT HELIX 89..117
FT /evidence="ECO:0007829|PDB:1X91"
FT HELIX 121..142
FT /evidence="ECO:0007829|PDB:1X91"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1X8Z"
FT HELIX 150..172
FT /evidence="ECO:0007829|PDB:1X91"
SQ SEQUENCE 176 AA; 18967 MW; 5D600D658A100076 CRC64;
MAANLRNNAF LSSLMFLLLI GSSYAITSSE MSTICDKTLN PSFCLKFLNT KFASPNLQAL
AKTTLDSTQA RATQTLKKLQ SIIDGGVDPR SKLAYRSCVD EYESAIGNLE EAFEHLASGD
GMGMNMKVSA ALDGADTCLD DVKRLRSVDS SVVNNSKTIK NLCGIALVIS NMLPRN
