PME4_ARATH
ID PME4_ARATH Reviewed; 588 AA.
AC O80722; Q5MFV7; Q8H194; Q9T0P8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Pectinesterase 4;
DE Short=PE 4;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 18;
DE Short=AtPME18;
DE AltName: Full=Pectin methylesterase 4;
DE Short=AtPME4;
DE AltName: Full=VANGUARD1-like protein 1;
DE Short=VGD1-like protein 1;
DE Flags: Precursor;
GN Name=PME4; Synonyms=ARATH18, VGDH1; OrderedLocusNames=At2g47030;
GN ORFNames=F14M4.14;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15659637; DOI=10.1105/tpc.104.027631;
RA Jiang L., Yang S.-L., Xie L.-F., Puah C.S., Zhang X.-Q., Yang W.-C.,
RA Sundaresan V., Ye D.;
RT "VANGUARD1 encodes a pectin methylesterase that enhances pollen tube growth
RT in the Arabidopsis style and transmitting tract.";
RL Plant Cell 17:584-596(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Wassilewskija; TISSUE=Flower;
RA Richard L., Micheli F., Goldberg R.;
RT "Molecular characterization of AtPME4: a flower-specific gene encoding
RT pectin methylesterase in Arabidopsis thaliana.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [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 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. Plays an important role in
CC growth of pollen tubes in female floral tissues, possibly via enhancing
CC the interaction between the pollen tube and female floral tissues by
CC modification of the cell walls. {ECO:0000269|PubMed:15659637}.
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:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen grains and pollen tubes.
CC {ECO:0000269|PubMed:15659637}.
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=AAN15509.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact leading to a large internal deletion.; 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; AY830949; AAV91509.1; -; mRNA.
DR EMBL; AF077855; AAC27719.1; -; Genomic_DNA.
DR EMBL; AC004411; AAC34241.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10790.1; -; Genomic_DNA.
DR EMBL; AY054462; AAK96654.1; -; mRNA.
DR EMBL; BT000190; AAN15509.1; ALT_SEQ; mRNA.
DR PIR; T02184; T02184.
DR PIR; T52330; T52330.
DR RefSeq; NP_182226.1; NM_130271.3.
DR AlphaFoldDB; O80722; -.
DR SMR; O80722; -.
DR BioGRID; 4652; 1.
DR IntAct; O80722; 1.
DR STRING; 3702.AT2G47030.1; -.
DR PaxDb; O80722; -.
DR PRIDE; O80722; -.
DR ProteomicsDB; 234689; -.
DR EnsemblPlants; AT2G47030.1; AT2G47030.1; AT2G47030.
DR GeneID; 819317; -.
DR Gramene; AT2G47030.1; AT2G47030.1; AT2G47030.
DR KEGG; ath:AT2G47030; -.
DR Araport; AT2G47030; -.
DR TAIR; locus:2041384; AT2G47030.
DR eggNOG; ENOG502QUTX; Eukaryota.
DR HOGENOM; CLU_012243_9_0_1; -.
DR InParanoid; O80722; -.
DR OMA; WAKMARS; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; O80722; -.
DR BioCyc; ARA:AT2G47030-MON; -.
DR BRENDA; 3.1.1.11; 399.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:O80722; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80722; baseline and differential.
DR Genevisible; O80722; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
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 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 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; PS00503; PECTINESTERASE_2; 1.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..588
FT /note="Pectinesterase 4"
FT /id="PRO_0000023476"
FT ACT_SITE 406
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 427
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 496
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 498
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 405
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 46
FT /note="Q -> R (in Ref. 1; AAV91509)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="T -> A (in Ref. 1; AAV91509)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="K -> N (in Ref. 1; AAV91509)"
FT /evidence="ECO:0000305"
FT CONFLICT 359..360
FT /note="Missing (in Ref. 2; AAC27719)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="V -> A (in Ref. 1; AAV91509)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="N -> S (in Ref. 1; AAV91509)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 588 AA; 64138 MW; 70E9A966040D67F2 CRC64;
MIGKVVVSVA SILLIVGVAI GVVAFINKNG DANLSPQMKA VQGICQSTSD KASCVKTLEP
VKSEDPNKLI KAFMLATKDE LTKSSNFTGQ TEVNMGSSIS PNNKAVLDYC KRVFMYALED
LATIIEEMGE DLSQIGSKID QLKQWLIGVY NYQTDCLDDI EEDDLRKAIG EGIANSKILT
TNAIDIFHTV VSAMAKINNK VDDLKNMTGG IPTPGAPPVV DESPVADPDG PARRLLEDID
ETGIPTWVSG ADRKLMAKAG RGRRGGRGGG ARVRTNFVVA KDGSGQFKTV QQAVDACPEN
NRGRCIIYIK AGLYREQVII PKKKNNIFMF GDGARKTVIS YNRSVALSRG TTTSLSATVQ
VESEGFMAKW MGFKNTAGPM GHQAAAIRVN GDRAVIFNCR FDGYQDTLYV NNGRQFYRNC
VVSGTVDFIF GKSATVIQNT LIVVRKGSKG QYNTVTADGN ELGLGMKIGI VLQNCRIVPD
RKLTPERLTV ATYLGRPWKK FSTTVIMSTE MGDLIRPEGW KIWDGESFHK SCRYVEYNNR
GPGAFANRRV NWAKVARSAA EVNGFTAANW LGPINWIQEA NVPVTIGL
