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   27-MAR-2024, entry version 138.
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.Q5MFV8; -.
DR   GlyCosmos; Q5MFV8; 3 sites, No reported glycans.
DR   PaxDb; 3702-AT2G47040-1; -.
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; AT2G47040; VGD1.
DR   eggNOG; ENOG502QUTX; Eukaryota.
DR   HOGENOM; CLU_012243_9_0_1; -.
DR   InParanoid; Q5MFV8; -.
DR   OMA; EFCQATE; -.
DR   OrthoDB; 668039at2759; -.
DR   PhylomeDB; Q5MFV8; -.
DR   BioCyc; ARA:AT2G47040-MONOMER; -.
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   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:0004857; F:enzyme inhibitor activity; IEA:InterPro.
DR   GO; GO:0030599; F:pectinesterase activity; IMP:UniProtKB.
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   CDD; cd15798; PMEI-like_3; 1.
DR   Gene3D; 1.20.140.40; Invertase/pectin methylesterase inhibitor family protein; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 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   NCBIfam; TIGR01614; PME_inhib; 1.
DR   PANTHER; PTHR31707; PECTINESTERASE; 1.
DR   PANTHER; PTHR31707:SF164; PECTINESTERASE 4-RELATED; 1.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   Pfam; PF04043; PMEI; 1.
DR   SMART; SM00856; PMEI; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   SUPFAM; SSF101148; Plant invertase/pectin methylesterase inhibitor; 1.
DR   PROSITE; PS00800; PECTINESTERASE_1; 1.
DR   PROSITE; PS00503; PECTINESTERASE_2; 1.
DR   Genevisible; Q5MFV8; AT.
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
//