PME12_ARATH
ID PME12_ARATH Reviewed; 547 AA.
AC O48711; Q570D4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 12;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 12;
DE AltName: Full=Pectin methylesterase inhibitor 12;
DE Includes:
DE RecName: Full=Pectinesterase 12;
DE Short=PE 12;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 12;
DE Short=AtPME12;
DE Flags: Precursor;
GN Name=PME12; Synonyms=ARATH12; OrderedLocusNames=At2g26440;
GN ORFNames=T9J22.11;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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] OF 447-547.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15337457; DOI=10.1016/j.carres.2004.06.023;
RA Markovic O., Janecek S.;
RT "Pectin methylesterases: sequence-structural features and phylogenetic
RT relationships.";
RL Carbohydr. Res. 339:2281-2295(2004).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16622707; DOI=10.1007/s00425-006-0261-9;
RA Louvet R., Cavel E., Gutierrez L., Guenin S., Roger D., Gillet F.,
RA Guerineau F., Pelloux J.;
RT "Comprehensive expression profiling of the pectin methylesterase gene
RT family during silique development in Arabidopsis thaliana.";
RL Planta 224:782-791(2006).
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol;
CC Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques.
CC {ECO:0000269|PubMed:16622707}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout silique development.
CC {ECO:0000269|PubMed:16622707}.
CC -!- MISCELLANEOUS: The PMEI region may act as an autoinhibitory domain and
CC prevent untimely PME activity during transport.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the pectinesterase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93990.1; Type=Erroneous initiation; 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; AC002505; AAC14493.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07839.1; -; Genomic_DNA.
DR EMBL; AY072224; AAL60045.1; -; mRNA.
DR EMBL; AY122952; AAM67485.1; -; mRNA.
DR EMBL; AK220775; BAD93990.1; ALT_INIT; mRNA.
DR PIR; T00977; T00977.
DR RefSeq; NP_180212.1; NM_128201.5.
DR AlphaFoldDB; O48711; -.
DR SMR; O48711; -.
DR STRING; 3702.AT2G26440.1; -.
DR PaxDb; O48711; -.
DR PRIDE; O48711; -.
DR ProteomicsDB; 236571; -.
DR EnsemblPlants; AT2G26440.1; AT2G26440.1; AT2G26440.
DR GeneID; 817184; -.
DR Gramene; AT2G26440.1; AT2G26440.1; AT2G26440.
DR KEGG; ath:AT2G26440; -.
DR Araport; AT2G26440; -.
DR TAIR; locus:2066195; AT2G26440.
DR eggNOG; ENOG502R64Q; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; O48711; -.
DR OMA; YPDVCFD; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; O48711; -.
DR BioCyc; ARA:AT2G26440-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:O48711; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48711; baseline and differential.
DR Genevisible; O48711; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR Gene3D; 1.20.140.40; -; 1.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR035513; Invertase/methylesterase_inhib.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR033131; Pectinesterase_Asp_AS.
DR InterPro; IPR000070; Pectinesterase_cat.
DR InterPro; IPR006501; Pectinesterase_inhib_dom.
DR InterPro; IPR018040; Pectinesterase_Tyr_AS.
DR Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF101148; SSF101148; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01614; PME_inhib; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..547
FT /note="Probable pectinesterase/pectinesterase inhibitor 12"
FT /id="PRO_0000371669"
FT REGION 31..185
FT /note="Pectinesterase inhibitor 12"
FT REGION 237..533
FT /note="Pectinesterase 12"
FT ACT_SITE 365
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 386
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 312
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 364
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 379..399
FT /evidence="ECO:0000250"
SQ SEQUENCE 547 AA; 60417 MW; 9CEB99E60E6378C7 CRC64;
MALSSFNLSS LLFLLFFTPS VFSYSYQPSL NPHETSATSF CKNTPYPDAC FTSLKLSISI
NISPNILSFL LQTLQTALSE AGKLTDLLSG AGVSNNLVEG QRGSLQDCKD LHHITSSFLK
RSISKIQDGV NDSRKLADAR AYLSAALTNK ITCLEGLESA SGPLKPKLVT SFTTTYKHIS
NSLSALPKQR RTTNPKTGGN TKNRRLLGLF PDWVYKKDHR FLEDSSDGYD EYDPSESLVV
AADGTGNFST INEAISFAPN MSNDRVLIYV KEGVYDENID IPIYKTNIVL IGDGSDVTFI
TGNRSVGDGW TTFRSATLAV SGEGFLARDI MITNTAGPEK HQAVALRVNA DFVALYRCVI
DGYQDTLYTH SFRQFYRECD IYGTIDYIFG NAAVVFQGCN IVSKLPMPGQ FTVITAQSRD
TQDEDTGISM QNCSILASED LFNSSNKVKS YLGRPWREFS RTVVMESYID EFIDGSGWSK
WNGGEALDTL YYGEYNNNGP GSETVKRVNW PGFHIMGYED AFNFTATEFI TGDGWLGSTS
FPYDNGI
