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Pectinesterase inhibitor 1 (Pectin methylesterase inhibitor 1) (AtPMEI1)

 PMEI1_ARATH             Reviewed;         176 AA.
Q9LNF2;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 101.
RecName: Full=Pectinesterase inhibitor 1 {ECO:0000305};
AltName: Full=Pectin methylesterase inhibitor 1 {ECO:0000303|PubMed:14675772};
Short=AtPMEI1 {ECO:0000303|PubMed:14675772};
Flags: Precursor;
Name=PMEI1 {ECO:0000303|PubMed:14675772}; OrderedLocusNames=At1g48020;
ORFNames=F21D18.29, F21D18_23, T2J15.7;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14675772; DOI=10.1016/S0014-5793(03)01344-9;
Wolf S., Grsic-Rausch S., Rausch T., Greiner S.;
"Identification of pollen-expressed pectin methylesterase inhibitors
in Arabidopsis.";
FEBS Lett. 555:551-555(2003).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14741367; DOI=10.1016/S0014-5793(03)01491-1;
Raiola A., Camardella L., Giovane A., Mattei B., De Lorenzo G.,
Cervone F., Bellincampi D.;
"Two Arabidopsis thaliana genes encode functional pectin
methylesterase inhibitors.";
FEBS Lett. 557:199-203(2004).
[7]
INTERACTION WITH PPME1, AND TISSUE SPECIFICITY.
PubMed=17971035; DOI=10.1111/j.1365-313X.2007.03325.x;
Roeckel N., Wolf S., Kost B., Rausch T., Greiner S.;
"Elaborate spatial patterning of cell-wall PME and PMEI at the pollen
tube tip involves PMEI endocytosis, and reflects the distribution of
esterified and de-esterified pectins.";
Plant J. 53:133-143(2008).
[8]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 28-176, DISULFIDE BONDS,
SUBUNIT, AND MUTAGENESIS OF PRO-55.
PubMed=15528298; DOI=10.1105/tpc.104.025684;
Hothorn M., Wolf S., Aloy P., Greiner S., Scheffzek K.;
"Structural insights into the target specificity of plant invertase
and pectin methylesterase inhibitory proteins.";
Plant Cell 16:3437-3447(2004).
[9]
SUBCELLULAR LOCATION.
PubMed=21223393; DOI=10.1111/j.1365-313X.2010.04421.x;
De Caroli M., Lenucci M.S., Di Sansebastiano G.P., Dalessandro G.,
De Lorenzo G., Piro G.;
"Protein trafficking to the cell wall occurs through mechanisms
distinguishable from default sorting in tobacco.";
Plant J. 65:295-308(2011).
-!- FUNCTION: Inhibits pectin methylesterase (PME) from flowers and
siliques (PubMed:14675772). Inhibits PME from leaves
(PubMed:14741367). {ECO:0000269|PubMed:14675772,
ECO:0000269|PubMed:14741367}.
-!- SUBUNIT: Monomer and homodimer. Interacts in vitro with PPME1.
{ECO:0000269|PubMed:15528298, ECO:0000269|PubMed:17971035}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
{ECO:0000269|PubMed:21223393}.
-!- TISSUE SPECIFICITY: Highest expression in flowers
(PubMed:14675772, PubMed:14741367, PubMed:17971035). Expressed
exclusively at the pollen tube tip (PubMed:14675772,
PubMed:17971035). {ECO:0000269|PubMed:14675772,
ECO:0000269|PubMed:14741367, ECO:0000269|PubMed:17971035}.
-!- DOMAIN: The N-terminal alpha-hairpin extension is required for
pectinmethylesterase inhibitor activity.
-!- SIMILARITY: Belongs to the PMEI family. {ECO:0000305}.
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EMBL; AC023673; AAF79530.1; -; Genomic_DNA.
EMBL; AC051631; AAG51524.1; -; Genomic_DNA.
EMBL; CP002684; AEE32238.1; -; Genomic_DNA.
EMBL; AK118003; BAC42636.1; -; mRNA.
EMBL; BT003715; AAO39943.1; -; mRNA.
RefSeq; NP_175236.1; NM_103698.3.
UniGene; At.45220; -.
PDB; 1X8Z; X-ray; 2.86 A; A/B/C=28-176.
PDB; 1X90; X-ray; 2.68 A; A/B=28-176.
PDB; 1X91; X-ray; 1.50 A; A=28-176.
PDBsum; 1X8Z; -.
PDBsum; 1X90; -.
PDBsum; 1X91; -.
ProteinModelPortal; Q9LNF2; -.
SMR; Q9LNF2; -.
BioGrid; 26445; 1.
MINT; MINT-8063644; -.
STRING; 3702.AT1G48020.1; -.
PaxDb; Q9LNF2; -.
EnsemblPlants; AT1G48020.1; AT1G48020.1; AT1G48020.
GeneID; 841220; -.
Gramene; AT1G48020.1; AT1G48020.1; AT1G48020.
KEGG; ath:AT1G48020; -.
Araport; AT1G48020; -.
TAIR; locus:2023797; AT1G48020.
eggNOG; ENOG410JJP1; Eukaryota.
eggNOG; ENOG4111AIM; LUCA.
HOGENOM; HOG000115585; -.
InParanoid; Q9LNF2; -.
OMA; RANATNT; -.
OrthoDB; EOG09360OXV; -.
PhylomeDB; Q9LNF2; -.
EvolutionaryTrace; Q9LNF2; -.
PRO; PR:Q9LNF2; -.
Proteomes; UP000006548; Chromosome 1.
GO; GO:0048046; C:apoplast; IDA:UniProtKB.
GO; GO:0071944; C:cell periphery; IBA:GO_Central.
GO; GO:0090404; C:pollen tube tip; NAS:TAIR.
GO; GO:0046910; F:pectinesterase inhibitor activity; IDA:TAIR.
GO; GO:0009860; P:pollen tube growth; IDA:TAIR.
CDD; cd15797; PMEI; 1.
Gene3D; 1.20.140.40; -; 1.
InterPro; IPR035513; Invertase/methylesterase_inhib.
InterPro; IPR006501; Pectinesterase_inhib_dom.
InterPro; IPR034086; PMEI_plant.
Pfam; PF04043; PMEI; 1.
SMART; SM00856; PMEI; 1.
SUPFAM; SSF101148; SSF101148; 1.
TIGRFAMs; TIGR01614; PME_inhib; 1.
1: Evidence at protein level;
3D-structure; Apoplast; Complete proteome; Disulfide bond;
Glycoprotein; Reference proteome; Secreted; Signal.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 176 Pectinesterase inhibitor 1.
/FTId=PRO_0000024706.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 35 44 {ECO:0000269|PubMed:15528298}.
DISULFID 98 138 {ECO:0000269|PubMed:15528298}.
MUTAGEN 55 55 P->A: Inhibits dimer formation and
reduces inhibitory activity.
{ECO:0000269|PubMed:15528298}.
TURN 31 33 {ECO:0000244|PDB:1X91}.
HELIX 34 37 {ECO:0000244|PDB:1X91}.
HELIX 41 50 {ECO:0000244|PDB:1X91}.
HELIX 57 85 {ECO:0000244|PDB:1X91}.
HELIX 89 117 {ECO:0000244|PDB:1X91}.
HELIX 121 142 {ECO:0000244|PDB:1X91}.
STRAND 145 147 {ECO:0000244|PDB:1X8Z}.
HELIX 150 172 {ECO:0000244|PDB:1X91}.
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


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