PME17_ARATH
ID PME17_ARATH Reviewed; 511 AA.
AC O22149; Q570I2; Q9ASU4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 17;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 17;
DE AltName: Full=Pectin methylesterase inhibitor 17;
DE Includes:
DE RecName: Full=Pectinesterase 17;
DE Short=PE 17;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 17;
DE Short=AtPME17;
DE Flags: Precursor;
GN Name=PME17; Synonyms=ARATH17; OrderedLocusNames=At2g45220;
GN ORFNames=F4L23.27;
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 394-511.
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 TISSUE SPECIFICITY.
RX PubMed=9767082; DOI=10.1016/s0378-1119(98)00431-4;
RA Micheli F., Holliger C., Goldberg R., Richard L.;
RT "Characterization of the pectin methylesterase-like gene AtPME3: a new
RT member of a gene family comprising at least 12 genes in Arabidopsis
RT thaliana.";
RL Gene 220:13-20(1998).
RN [6]
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 [7]
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, ECO:0000269|PubMed:9767082}.
CC -!- DEVELOPMENTAL STAGE: Expressed during late developmental phases of
CC siliques. {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=BAD93862.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC002387; AAB82640.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10527.1; -; Genomic_DNA.
DR EMBL; AF361829; AAK32841.1; -; mRNA.
DR EMBL; AK220726; BAD93862.1; ALT_INIT; mRNA.
DR PIR; H84887; H84887.
DR RefSeq; NP_566038.1; NM_130085.4.
DR AlphaFoldDB; O22149; -.
DR SMR; O22149; -.
DR BioGRID; 4466; 2.
DR IntAct; O22149; 2.
DR STRING; 3702.AT2G45220.1; -.
DR PaxDb; O22149; -.
DR PRIDE; O22149; -.
DR ProteomicsDB; 236643; -.
DR EnsemblPlants; AT2G45220.1; AT2G45220.1; AT2G45220.
DR GeneID; 819130; -.
DR Gramene; AT2G45220.1; AT2G45220.1; AT2G45220.
DR KEGG; ath:AT2G45220; -.
DR Araport; AT2G45220; -.
DR TAIR; locus:2050941; AT2G45220.
DR eggNOG; ENOG502QSQ4; Eukaryota.
DR HOGENOM; CLU_012243_9_1_1; -.
DR InParanoid; O22149; -.
DR OMA; FLTHNSN; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; O22149; -.
DR BioCyc; ARA:AT2G45220-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:O22149; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22149; baseline and differential.
DR Genevisible; O22149; 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:0050829; P:defense response to Gram-negative bacterium; IMP:TAIR.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR GO; GO:0009620; P:response to fungus; IEP:TAIR.
DR Gene3D; 1.20.140.40; -; 1.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
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 Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00722; CASH; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF101148; SSF101148; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01614; PME_inhib; 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..511
FT /note="Probable pectinesterase/pectinesterase inhibitor 17"
FT /id="PRO_0000371674"
FT REGION 24..171
FT /note="Pectinesterase inhibitor 17"
FT REGION 237..414
FT /note="Pectinesterase 17"
FT ACT_SITE 330
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 351
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 277
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 329
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 344..364
FT /evidence="ECO:0000250"
SQ SEQUENCE 511 AA; 55977 MW; 96487096A87F9375 CRC64;
MMAFRAYIIN FVILCILVAS TVSGYNQKDV KAWCSQTPNP KPCEYFLTHN SNNEPIKSES
EFLKISMKLV LDRAILAKTH AFTLGPKCRD TREKAAWEDC IKLYDLTVSK INETMDPNVK
CSKLDAQTWL STALTNLDTC RAGFLELGVT DIVLPLMSNN VSNLLCNTLA INKVPFNYTP
PEKDGFPSWV KPGDRKLLQS STPKDNAVVA KDGSGNFKTI KEAIDAASGS GRFVIYVKQG
VYSENLEIRK KNVMLRGDGI GKTIITGSKS VGGGTTTFNS ATVAAVGDGF IARGITFRNT
AGASNEQAVA LRSGSDLSVF YQCSFEAYQD TLYVHSNRQF YRDCDVYGTV DFIFGNAAAV
LQNCNIFARR PRSKTNTITA QGRSDPNQNT GIIIHNSRVT AASDLRPVLG STKTYLGRPW
RQYSRTVFMK TSLDSLIDPR GWLEWDGNFA LKTLFYAEFQ NTGPGASTSG RVTWPGFRVL
GSASEASKFT VGTFLAGGSW IPSSVPFTSG L
