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Pectinesterase 5 (PE 5) (EC 3.1.1.11) (Pectin methylesterase 5) (AtPME5) (Pectin methylesterase 67) (AtPME67) (Protein VANGUARD 1)

 PME5_ARATH              Reviewed;         595 AA.
Q5MFV8; O80721; Q9SMV9;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 2.
25-OCT-2017, entry version 107.
RecName: Full=Pectinesterase 5;
Short=PE 5;
EC=3.1.1.11;
AltName: Full=Pectin methylesterase 5;
Short=AtPME5;
AltName: Full=Pectin methylesterase 67;
Short=AtPME67;
AltName: Full=Protein VANGUARD 1;
Flags: Precursor;
Name=PME5; Synonyms=ARATH67, VGD1; OrderedLocusNames=At2g47040;
ORFNames=F14M4.13;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
STRAIN=cv. Landsberg erecta;
PubMed=15659637; DOI=10.1105/tpc.104.027631;
Jiang L., Yang S.-L., Xie L.-F., Puah C.S., Zhang X.-Q., Yang W.-C.,
Sundaresan V., Ye D.;
"VANGUARD1 encodes a pectin methylesterase that enhances pollen tube
growth in the Arabidopsis style and transmitting tract.";
Plant Cell 17:584-596(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Flower bud;
Torki M., Mache R., Mandaron P., Falconet D.;
"Characterization of a flower-specific gene encoding pectin
methylesterase in Arabidopsis thaliana.";
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15337457; DOI=10.1016/j.carres.2004.06.023;
Markovic O., Janecek S.;
"Pectin methylesterases: sequence-structural features and phylogenetic
relationships.";
Carbohydr. Res. 339:2281-2295(2004).
[7]
DEVELOPMENTAL STAGE.
PubMed=16622707; DOI=10.1007/s00425-006-0261-9;
Louvet R., Cavel E., Gutierrez L., Guenin S., Roger D., Gillet F.,
Guerineau F., Pelloux J.;
"Comprehensive expression profiling of the pectin methylesterase gene
family during silique development in Arabidopsis thaliana.";
Planta 224:782-791(2006).
[8]
INTERACTION WITH SBT6.1, SUBCELLULAR LOCATION, DOMAIN, AND CLEAVAGE BY
SBT6.1.
PubMed=19144003; DOI=10.1111/j.1365-313X.2009.03784.x;
Wolf S., Rausch T., Greiner S.;
"The N-terminal pro region mediates retention of unprocessed type-I
PME in the Golgi apparatus.";
Plant J. 58:361-375(2009).
[9]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=21673079; DOI=10.1105/tpc.110.082651;
Phan H.A., Iacuone S., Li S.F., Parish R.W.;
"The MYB80 transcription factor is required for pollen development and
the regulation of tapetal programmed cell death in Arabidopsis
thaliana.";
Plant Cell 23:2209-2224(2011).
-!- FUNCTION: Acts in the modification of cell walls via
demethylesterification of cell wall pectin. Plays an important
role in growth of pollen tubes in female floral tissues, possibly
via enhancing the interaction between the pollen tube and female
floral tissues by modification of the cell walls
(PubMed:15659637). May be regulated by MYB80 during anther
development and play a role in tapetum and pollen development
(PubMed:21673079). {ECO:0000269|PubMed:15659637,
ECO:0000269|PubMed:21673079}.
-!- CATALYTIC ACTIVITY: Pectin + n H(2)O = n methanol + pectate.
-!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-
D-gluconate from pectin: step 1/5.
-!- SUBUNIT: Interacts with SBT6.1. {ECO:0000269|PubMed:19144003}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15659637}.
Secreted, cell wall {ECO:0000269|PubMed:15659637}. Golgi apparatus
membrane {ECO:0000269|PubMed:19144003}. Note=Distributed in the
whole pollen tube, including the plasma membrane and pollen tube
wall (PubMed:15659637). Cleaved in the Golgi apparatus by SBT6.1
(S1P) after the Arg-Arg-Leu-Leu (RRLL) and Arg-Lys-Leu-Met (RKLM)
motifs. This processing is required for extracellular targeting
(PubMed:19144003). {ECO:0000269|PubMed:15659637,
ECO:0000269|PubMed:19144003}.
-!- TISSUE SPECIFICITY: Expressed in pollen grains and pollen tubes.
{ECO:0000269|PubMed:15659637}.
-!- DEVELOPMENTAL STAGE: Expressed throughout silique development
(PubMed:16622707). During anther development, expressed from stage
9 to stage 11 in late tapetum, and mature pollen grains
(PubMed:21673079). {ECO:0000269|PubMed:16622707,
ECO:0000269|PubMed:21673079}.
-!- DOMAIN: The PMEI region may act as an autoinhibitory domain and
prevent untimely PME activity during transport. The PMEI region is
cleaved by SBT6.1 (S1P) in the Golgi apparatus prior to cell wall
targeting. {ECO:0000305|PubMed:19144003}.
-!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
{ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the
pectinesterase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=When tough is soft
- Issue 106 of June 2009;
URL="http://web.expasy.org/spotlight/back_issues/106";
-----------------------------------------------------------------------
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EMBL; AY830948; AAV91508.1; -; mRNA.
EMBL; AJ250430; CAB58974.1; -; mRNA.
EMBL; AC004411; AAC34240.1; -; Genomic_DNA.
EMBL; CP002685; AEC10791.1; -; Genomic_DNA.
EMBL; AY091768; AAM10316.1; -; mRNA.
EMBL; BT001120; AAN64511.1; -; mRNA.
PIR; T02183; T02183.
PIR; T52327; T52327.
RefSeq; NP_182227.1; NM_130272.4.
UniGene; At.24875; -.
ProteinModelPortal; Q5MFV8; -.
SMR; Q5MFV8; -.
BioGrid; 4653; 2.
STRING; 3702.AT2G47040.1; -.
PaxDb; Q5MFV8; -.
PRIDE; Q5MFV8; -.
EnsemblPlants; AT2G47040.1; AT2G47040.1; AT2G47040.
GeneID; 819318; -.
Gramene; AT2G47040.1; AT2G47040.1; AT2G47040.
KEGG; ath:AT2G47040; -.
Araport; AT2G47040; -.
TAIR; locus:2041364; AT2G47040.
eggNOG; ENOG410JB1S; Eukaryota.
eggNOG; COG4677; LUCA.
HOGENOM; HOG000217409; -.
InParanoid; Q5MFV8; -.
OMA; WAKMARS; -.
OrthoDB; EOG093606UI; -.
PhylomeDB; Q5MFV8; -.
BioCyc; ARA:AT2G47040-MONOMER; -.
BRENDA; 3.1.1.11; 399.
UniPathway; UPA00545; UER00823.
PRO; PR:Q5MFV8; -.
Proteomes; UP000006548; Chromosome 2.
Genevisible; Q5MFV8; AT.
GO; GO:0071944; C:cell periphery; IBA:GO_Central.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0090406; C:pollen tube; IDA:TAIR.
GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
GO; GO:0030599; F:pectinesterase activity; IMP:UniProtKB.
GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
GO; GO:0042545; P:cell wall modification; IEA:InterPro.
GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0009860; P:pollen tube growth; TAS:TAIR.
Gene3D; 1.20.140.40; -; 1.
Gene3D; 2.160.20.10; -; 1.
InterPro; IPR035513; Invertase/methylesterase_inhib.
InterPro; IPR012334; Pectin_lyas_fold.
InterPro; IPR011050; Pectin_lyase_fold/virulence.
InterPro; IPR033131; Pectinesterase_Asp_AS.
InterPro; IPR000070; Pectinesterase_cat.
InterPro; IPR006501; Pectinesterase_inhib_dom.
InterPro; IPR018040; Pectinesterase_Tyr_AS.
Pfam; PF01095; Pectinesterase; 1.
Pfam; PF04043; PMEI; 1.
SMART; SM00856; PMEI; 1.
SUPFAM; SSF101148; SSF101148; 1.
SUPFAM; SSF51126; SSF51126; 1.
TIGRFAMs; TIGR01614; PME_inhib; 1.
PROSITE; PS00800; PECTINESTERASE_1; 1.
PROSITE; PS00503; PECTINESTERASE_2; 1.
1: Evidence at protein level;
Aspartyl esterase; Cell membrane; Cell wall;
Cell wall biogenesis/degradation; Complete proteome; Glycoprotein;
Golgi apparatus; Hydrolase; Membrane; Reference proteome; Secreted;
Signal.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 595 Pectinesterase 5.
/FTId=PRO_0000023477.
MOTIF 243 246 RRLL cleavage motif.
{ECO:0000305|PubMed:19144003}.
MOTIF 263 266 RKLM cleavage motif.
{ECO:0000305|PubMed:19144003}.
ACT_SITE 413 413 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10040}.
ACT_SITE 434 434 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10040}.
BINDING 360 360 Substrate. {ECO:0000250}.
BINDING 390 390 Substrate. {ECO:0000250}.
BINDING 503 503 Substrate. {ECO:0000250}.
BINDING 505 505 Substrate. {ECO:0000250}.
SITE 412 412 Transition state stabilizer.
{ECO:0000250}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 349 349 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 50 50 D -> V (in Ref. 1; AAV91508).
{ECO:0000305}.
CONFLICT 93 93 G -> E (in Ref. 2; CAB58974).
{ECO:0000305}.
CONFLICT 138 138 K -> E (in Ref. 1; AAV91508).
{ECO:0000305}.
CONFLICT 267 267 T -> A (in Ref. 1; AAV91508 and 2;
CAB58974). {ECO:0000305}.
CONFLICT 537 537 K -> Q (in Ref. 1; AAV91508).
{ECO:0000305}.
CONFLICT 545 545 N -> S (in Ref. 1; AAV91508).
{ECO:0000305}.
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


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