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PMEI3_ARATH
ID   PMEI3_ARATH             Reviewed;         205 AA.
AC   Q84WE4; Q8LE11;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Pectinesterase inhibitor 3 {ECO:0000305};
DE   AltName: Full=Pectin methylesterase inhibitor 3 {ECO:0000303|PubMed:19097903};
DE            Short=AtPMEI3 {ECO:0000303|PubMed:28082716};
DE   Flags: Precursor;
GN   Name=PMEI3 {ECO:0000303|PubMed:19097903};
GN   OrderedLocusNames=At5g20740 {ECO:0000312|Araport:AT5G20740};
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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=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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=19097903; DOI=10.1016/j.cub.2008.10.065;
RA   Peaucelle A., Louvet R., Johansen J.N., Hoefte H., Laufs P., Pelloux J.,
RA   Mouille G.;
RT   "Arabidopsis phyllotaxis is controlled by the methyl-esterification status
RT   of cell-wall pectins.";
RL   Curr. Biol. 18:1943-1948(2008).
RN   [7]
RP   INDUCTION.
RX   PubMed=28082716; DOI=10.1104/pp.16.01185;
RA   Lionetti V., Fabri E., De Caroli M., Hansen A.R., Willats W.G., Piro G.,
RA   Bellincampi D.;
RT   "Three pectin methyl esterase inhibitors protect cell wall integrity for
RT   immunity to Botrytis.";
RL   Plant Physiol. 173:1844-1863(2017).
CC   -!- FUNCTION: Pectin methylesterase (PME) inhibitor that regulates de-
CC       methylesterification of pectins in the apical meristem and affects
CC       primordia formation and phyllotactic patterning.
CC       {ECO:0000269|PubMed:19097903}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000250|UniProtKB:Q9STY5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences. {ECO:0000305};
CC       Name=1;
CC         IsoId=Q84WE4-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in apical meristem.
CC       {ECO:0000269|PubMed:19097903}.
CC   -!- INDUCTION: Down-regulated in leaves during infection with Botrytis
CC       cinerea. {ECO:0000269|PubMed:28082716}.
CC   -!- SIMILARITY: Belongs to the PMEI family. {ECO:0000305}.
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DR   EMBL; AF296832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED92888.1; -; Genomic_DNA.
DR   EMBL; BT003915; AAO41962.1; -; mRNA.
DR   EMBL; BT020562; AAW70408.1; -; mRNA.
DR   EMBL; AY085686; AAM62905.1; -; mRNA.
DR   RefSeq; NP_197574.1; NM_122081.3. [Q84WE4-1]
DR   AlphaFoldDB; Q84WE4; -.
DR   SMR; Q84WE4; -.
DR   STRING; 3702.AT5G20740.1; -.
DR   PaxDb; Q84WE4; -.
DR   ProteomicsDB; 236646; -. [Q84WE4-1]
DR   EnsemblPlants; AT5G20740.1; AT5G20740.1; AT5G20740. [Q84WE4-1]
DR   GeneID; 832197; -.
DR   Gramene; AT5G20740.1; AT5G20740.1; AT5G20740. [Q84WE4-1]
DR   KEGG; ath:AT5G20740; -.
DR   Araport; AT5G20740; -.
DR   TAIR; locus:2180484; AT5G20740.
DR   eggNOG; ENOG502RXR5; Eukaryota.
DR   HOGENOM; CLU_033761_0_2_1; -.
DR   InParanoid; Q84WE4; -.
DR   OMA; WQMSNAE; -.
DR   PhylomeDB; Q84WE4; -.
DR   PRO; PR:Q84WE4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q84WE4; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IBA:GO_Central.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; IBA:GO_Central.
DR   GO; GO:1902183; P:regulation of shoot apical meristem development; IMP:UniProtKB.
DR   Gene3D; 1.20.140.40; -; 1.
DR   InterPro; IPR035513; Invertase/methylesterase_inhib.
DR   InterPro; IPR006501; Pectinesterase_inhib_dom.
DR   Pfam; PF04043; PMEI; 1.
DR   SMART; SM00856; PMEI; 1.
DR   SUPFAM; SSF101148; SSF101148; 1.
DR   TIGRFAMs; TIGR01614; PME_inhib; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Apoplast; Disulfide bond; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..205
FT                   /note="Pectinesterase inhibitor 3"
FT                   /id="PRO_5008428148"
FT   DISULFID        38..47
FT                   /evidence="ECO:0000250|UniProtKB:Q9LNF2"
FT   DISULFID        104..156
FT                   /evidence="ECO:0000250|UniProtKB:Q9LNF2"
FT   CONFLICT        4
FT                   /note="T -> P (in Ref. 5; AAM62905)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        22
FT                   /note="T -> I (in Ref. 5; AAM62905)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="E -> G (in Ref. 5; AAM62905)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190
FT                   /note="V -> I (in Ref. 5; AAM62905)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   205 AA;  22329 MW;  0CA6D118B9CE904E CRC64;
     MAPTQNLFLV AIAFAVIFTA STVHGRHNGA EDIVHSSCEH ASYPSLCVRT LSSYSGPTIT
     NRRDLAQAAI KISLSHAQSA AKKLAVVRDS VGKKKQEKAA LVDCVEMIGD SVDELSRTLG
     VLKHLRVSGG SAKEFRWQMS NAQTWASAAL TDDDTCLDGF QGMDDGEIKT EVKQWMTKVA
     RVTSNALYMV NQLDETRGKP HDVHL
 
 
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