PME5_ARATH
ID PME5_ARATH Reviewed; 595 AA.
AC Q5MFV8; O80721; Q9SMV9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Pectinesterase 5;
DE Short=PE 5;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 5;
DE Short=AtPME5;
DE AltName: Full=Pectin methylesterase 67;
DE Short=AtPME67;
DE AltName: Full=Protein VANGUARD 1;
DE Flags: Precursor;
GN Name=PME5; Synonyms=ARATH67, VGD1; OrderedLocusNames=At2g47040;
GN ORFNames=F14M4.13;
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, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
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 [MRNA].
RC TISSUE=Flower bud;
RA Torki M., Mache R., Mandaron P., Falconet D.;
RT "Characterization of a flower-specific gene encoding pectin methylesterase
RT in Arabidopsis thaliana.";
RL Submitted (OCT-1999) 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).
RN [8]
RP INTERACTION WITH SBT6.1, SUBCELLULAR LOCATION, DOMAIN, AND CLEAVAGE BY
RP SBT6.1.
RX PubMed=19144003; DOI=10.1111/j.1365-313x.2009.03784.x;
RA Wolf S., Rausch T., Greiner S.;
RT "The N-terminal pro region mediates retention of unprocessed type-I PME in
RT the Golgi apparatus.";
RL Plant J. 58:361-375(2009).
RN [9]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=21673079; DOI=10.1105/tpc.110.082651;
RA Phan H.A., Iacuone S., Li S.F., Parish R.W.;
RT "The MYB80 transcription factor is required for pollen development and the
RT regulation of tapetal programmed cell death in Arabidopsis thaliana.";
RL Plant Cell 23:2209-2224(2011).
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 (PubMed:15659637). May be regulated by
CC MYB80 during anther development and play a role in tapetum and pollen
CC development (PubMed:21673079). {ECO:0000269|PubMed:15659637,
CC ECO:0000269|PubMed:21673079}.
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 -!- SUBUNIT: Interacts with SBT6.1. {ECO:0000269|PubMed:19144003}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15659637}.
CC Secreted, cell wall {ECO:0000269|PubMed:15659637}. Golgi apparatus
CC membrane {ECO:0000269|PubMed:19144003}. Note=Distributed in the whole
CC pollen tube, including the plasma membrane and pollen tube wall
CC (PubMed:15659637). Cleaved in the Golgi apparatus by SBT6.1 (S1P) after
CC the Arg-Arg-Leu-Leu (RRLL) and Arg-Lys-Leu-Met (RKLM) motifs. This
CC processing is required for extracellular targeting (PubMed:19144003).
CC {ECO:0000269|PubMed:15659637, ECO:0000269|PubMed:19144003}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen grains and pollen tubes.
CC {ECO:0000269|PubMed:15659637}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout silique development
CC (PubMed:16622707). During anther development, expressed from stage 9 to
CC stage 11 in late tapetum, and mature pollen grains (PubMed:21673079).
CC {ECO:0000269|PubMed:16622707, ECO:0000269|PubMed:21673079}.
CC -!- DOMAIN: The PMEI region may act as an autoinhibitory domain and prevent
CC untimely PME activity during transport. The PMEI region is cleaved by
CC SBT6.1 (S1P) in the Golgi apparatus prior to cell wall targeting.
CC {ECO:0000305|PubMed:19144003}.
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 -!- WEB RESOURCE: Name=Protein Spotlight; Note=When tough is soft - Issue
CC 106 of June 2009;
CC URL="https://web.expasy.org/spotlight/back_issues/106";
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DR EMBL; AY830948; AAV91508.1; -; mRNA.
DR EMBL; AJ250430; CAB58974.1; -; mRNA.
DR EMBL; AC004411; AAC34240.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10791.1; -; Genomic_DNA.
DR EMBL; AY091768; AAM10316.1; -; mRNA.
DR EMBL; BT001120; AAN64511.1; -; mRNA.
DR PIR; T02183; T02183.
DR PIR; T52327; T52327.
DR RefSeq; NP_182227.1; NM_130272.4.
DR AlphaFoldDB; Q5MFV8; -.
DR SMR; Q5MFV8; -.
DR BioGRID; 4653; 2.
DR STRING; 3702.AT2G47040.1; -.
DR PaxDb; Q5MFV8; -.
DR PRIDE; Q5MFV8; -.
DR ProteomicsDB; 234777; -.
DR EnsemblPlants; AT2G47040.1; AT2G47040.1; AT2G47040.
DR GeneID; 819318; -.
DR Gramene; AT2G47040.1; AT2G47040.1; AT2G47040.
DR KEGG; ath:AT2G47040; -.
DR Araport; AT2G47040; -.
DR TAIR; locus:2041364; AT2G47040.
DR eggNOG; ENOG502QUTX; Eukaryota.
DR HOGENOM; CLU_012243_9_0_1; -.
DR InParanoid; Q5MFV8; -.
DR OMA; YSHEIGA; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q5MFV8; -.
DR BioCyc; ARA:AT2G47040-MON; -.
DR BRENDA; 3.1.1.11; 399.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q5MFV8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q5MFV8; baseline and differential.
DR Genevisible; Q5MFV8; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IMP:UniProtKB.
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:0009860; P:pollen tube growth; TAS: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 1: Evidence at protein level;
KW Aspartyl esterase; Cell membrane; Cell wall;
KW Cell wall biogenesis/degradation; Glycoprotein; Golgi apparatus; Hydrolase;
KW Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..595
FT /note="Pectinesterase 5"
FT /id="PRO_0000023477"
FT REGION 215..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 243..246
FT /note="RRLL cleavage motif"
FT /evidence="ECO:0000305|PubMed:19144003"
FT MOTIF 263..266
FT /note="RKLM cleavage motif"
FT /evidence="ECO:0000305|PubMed:19144003"
FT ACT_SITE 413
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT ACT_SITE 434
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 505
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 412
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 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 50
FT /note="D -> V (in Ref. 1; AAV91508)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="G -> E (in Ref. 2; CAB58974)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="K -> E (in Ref. 1; AAV91508)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="T -> A (in Ref. 1; AAV91508 and 2; CAB58974)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="K -> Q (in Ref. 1; AAV91508)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="N -> S (in Ref. 1; AAV91508)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 64728 MW; E314E53201F3CD77 CRC64;
MIGKVVVSVA SILLIVGVAI GVVAYINKNG DANLSPQMKA VRGICEATSD KASCVKTLEP
VKSDDPNKLI KAFMLATRDA ITQSSNFTGK TEGNLGSGIS PNNKAVLDYC KKVFMYALED
LSTIVEEMGE DLNQIGSKID QLKQWLTGVY NYQTDCLDDI EEDDLRKTIG EGIASSKILT
SNAIDIFHTV VSAMAKLNLK VEDFKNMTGG IFAPSDKGAA PVNKGTPPVA DDSPVADPDG
PARRLLEDID ETGIPTWVSG ADRKLMTKAG RGSNDGGARI RATFVVAKDG SGQFKTVQQA
VNACPEKNPG RCIIHIKAGI YREQVIIPKK KNNIFMFGDG ARKTVISYNR SVKLSPGTTT
SLSGTVQVES EGFMAKWIGF KNTAGPMGHQ AVAIRVNGDR AVIFNCRFDG YQDTLYVNNG
RQFYRNIVVS GTVDFIFGKS ATVIQNSLIV VRKGNKGQFN TVTADGNEKG LAMKIGIVLQ
NCRIVPDKKL AAERLIVESY LGRPWKKFST TVIINSEIGD VIRPEGWKIW DGESFHKSCR
YVEYNNRGPG AITNRRVNWV KIARSAAEVN DFTVANWLGP INWIQEANVP VTLGL
