PME21_ARATH
ID PME21_ARATH Reviewed; 669 AA.
AC Q8GX86; Q9M9W6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable pectinesterase/pectinesterase inhibitor 21;
DE Includes:
DE RecName: Full=Pectinesterase inhibitor 21;
DE AltName: Full=Pectin methylesterase inhibitor 21;
DE Includes:
DE RecName: Full=Pectinesterase 21;
DE Short=PE 21;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 21;
DE Short=AtPME21;
GN Name=PME21; Synonyms=ARATH21; OrderedLocusNames=At3g05610;
GN ORFNames=F18C1.12;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
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 [6]
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: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flower buds.
CC {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}.
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DR EMBL; AC011620; AAF26136.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74266.1; -; Genomic_DNA.
DR EMBL; AK118374; BAC42986.1; -; mRNA.
DR EMBL; BT005948; AAO64883.1; -; mRNA.
DR RefSeq; NP_187212.1; NM_111434.3.
DR AlphaFoldDB; Q8GX86; -.
DR SMR; Q8GX86; -.
DR STRING; 3702.AT3G05610.1; -.
DR PaxDb; Q8GX86; -.
DR PRIDE; Q8GX86; -.
DR ProteomicsDB; 234930; -.
DR EnsemblPlants; AT3G05610.1; AT3G05610.1; AT3G05610.
DR GeneID; 819727; -.
DR Gramene; AT3G05610.1; AT3G05610.1; AT3G05610.
DR KEGG; ath:AT3G05610; -.
DR Araport; AT3G05610; -.
DR TAIR; locus:2078057; AT3G05610.
DR eggNOG; ENOG502QPZF; Eukaryota.
DR HOGENOM; CLU_012243_9_0_1; -.
DR InParanoid; Q8GX86; -.
DR OMA; CEYSLIK; -.
DR OrthoDB; 714825at2759; -.
DR PhylomeDB; Q8GX86; -.
DR BioCyc; ARA:AT3G05610-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q8GX86; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GX86; baseline and differential.
DR Genevisible; Q8GX86; AT.
DR GO; GO:0016021; C:integral component of membrane; 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: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; 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.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..669
FT /note="Probable pectinesterase/pectinesterase inhibitor 21"
FT /id="PRO_0000371677"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 52..205
FT /note="Pectinesterase inhibitor 21"
FT REGION 255..551
FT /note="Pectinesterase 21"
FT REGION 615..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 383
FT /note="Proton donor; for pectinesterase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 404
FT /note="Nucleophile; for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="substrate"
FT /ligand_note="for pectinesterase activity"
FT /evidence="ECO:0000250"
FT SITE 382
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 397..417
FT /evidence="ECO:0000250"
FT CONFLICT 330
FT /note="T -> A (in Ref. 3; BAC42986 and 4; AAO64883)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="D -> N (in Ref. 3; BAC42986 and 4; AAO64883)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="S -> F (in Ref. 3; BAC42986 and 4; AAO64883)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 72917 MW; 2D7DC0FF415EB573 CRC64;
MSYGYDDESK RKRRYIVITI SSVLLISMVV AVTVGVSLNK HDGDSKGKAE VNASVKAVKD
VCAPTDYRKT CEDTLIKNGK NTTDPMELVK TAFNVTMKQI TDAAKKSQTI MELQKDSRTR
MALDQCKELM DYALDELSNS FEELGKFEFH LLDEALINLR IWLSAAISHE ETCLEGFQGT
QGNAGETMKK ALKTAIELTH NGLAIISEMS NFVGQMQIPG LNSRRLLAEG FPSWVDQRGR
KLLQAAAAYS DVKPDIVVAQ DGSGQYKTIN EALQFVPKKR NTTFVVHIKA GLYKEYVQVN
KTMSHLVFIG DGPDKTIISG NKNYKDGITT YRTATVAIVG NYFIAKNIGF ENTAGAIKHQ
AVAVRVQSDE SIFFNCRFDG YQDTLYTHSH RQFFRDCTIS GTIDFLFGDA AAVFQNCTLL
VRKPLPNQAC PITAHGRKDP RESTGFVFQG CTIAGEPDYL AVKETSKAYL GRPWKEYSRT
IIMNTFIPDF VQPQGWQPWL GDFGLKTLFY SEVQNTGPGS ALANRVTWAG IKTLSEEDIL
KFTPAQYIQG DDWIPGKGVP YTTGLLAGNP AAATTTPSVS AAAPGFSTFT DTSGADSIAP
TASPAASPES SISMAYTGTA SPESSIKVSS STETASPESS FTEASTASPE SSIMVASTES
SGSFFSMFT
