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PMEI7_ARATH
ID   PMEI7_ARATH             Reviewed;         201 AA.
AC   Q9SB37;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Pectinesterase inhibitor 7 {ECO:0000305};
DE   AltName: Full=Pectin methylesterase inhibitor 7 {ECO:0000303|PubMed:26183897};
DE            Short=AtPMEI7 {ECO:0000303|PubMed:26183897};
DE   Flags: Precursor;
GN   Name=PMEI7 {ECO:0000303|PubMed:26183897};
GN   OrderedLocusNames=At4g25260 {ECO:0000312|Araport:AT4G25260};
GN   ORFNames=F24A6.100 {ECO:0000312|EMBL:CAA23067.1};
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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   FUNCTION.
RX   PubMed=26183897; DOI=10.1074/jbc.m115.639534;
RA   Senechal F., L'Enfant M., Domon J.M., Rosiau E., Crepeau M.J., Surcouf O.,
RA   Esquivel-Rodriguez J., Marcelo P., Mareck A., Guerineau F., Kim H.R.,
RA   Mravec J., Bonnin E., Jamet E., Kihara D., Lerouge P., Ralet M.C.,
RA   Pelloux J., Rayon C.;
RT   "Tuning of pectin methylesterification: Pectin methylesterase inhibitor 7
RT   modulates the processive activity of co-expressed pectin methylesterase 3
RT   in a ph-dependent manner.";
RL   J. Biol. Chem. 290:23320-23335(2015).
CC   -!- FUNCTION: Pectin methylesterase (PME) inhibitor that can target the
CC       PME3 and may regulate homogalacturonan methylesterification during
CC       plant development. {ECO:0000269|PubMed:26183897}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000250|UniProtKB:Q9STY5}.
CC   -!- SIMILARITY: Belongs to the PMEI family. {ECO:0000305}.
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DR   EMBL; AL035396; CAA23067.1; -; Genomic_DNA.
DR   EMBL; AL161563; CAB81337.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85032.1; -; Genomic_DNA.
DR   EMBL; AY058853; AAL24241.1; -; mRNA.
DR   EMBL; AY079038; AAL79588.1; -; mRNA.
DR   PIR; T05547; T05547.
DR   RefSeq; NP_194256.1; NM_118658.4.
DR   AlphaFoldDB; Q9SB37; -.
DR   SMR; Q9SB37; -.
DR   STRING; 3702.AT4G25260.1; -.
DR   PaxDb; Q9SB37; -.
DR   PRIDE; Q9SB37; -.
DR   ProteomicsDB; 234781; -.
DR   DNASU; 828629; -.
DR   EnsemblPlants; AT4G25260.1; AT4G25260.1; AT4G25260.
DR   GeneID; 828629; -.
DR   Gramene; AT4G25260.1; AT4G25260.1; AT4G25260.
DR   KEGG; ath:AT4G25260; -.
DR   Araport; AT4G25260; -.
DR   TAIR; locus:2122624; AT4G25260.
DR   eggNOG; ENOG502QXIN; Eukaryota.
DR   HOGENOM; CLU_033761_0_2_1; -.
DR   InParanoid; Q9SB37; -.
DR   OMA; EMTDYKG; -.
DR   OrthoDB; 1528760at2759; -.
DR   PhylomeDB; Q9SB37; -.
DR   PRO; PR:Q9SB37; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SB37; 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:0046910; F:pectinesterase inhibitor activity; IDA:TAIR.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; IDA:TAIR.
DR   GO; GO:0009641; P:shade avoidance; IEP:TAIR.
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   Apoplast; Disulfide bond; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..201
FT                   /note="Pectinesterase inhibitor 7"
FT                   /id="PRO_5008430271"
FT   DISULFID        42..51
FT                   /evidence="ECO:0000250|UniProtKB:Q9LNF2"
FT   DISULFID        108..159
FT                   /evidence="ECO:0000250|UniProtKB:Q9LNF2"
SQ   SEQUENCE   201 AA;  22173 MW;  5FECD024BE040D97 CRC64;
     MARNFELSLI LFVLYLSTAA IVMARNLEEE SSGDTEFIKA SCETTSYPDR CFQSLSSYAS
     EIKKQPRKLA ETALAVSIAR AKSAKTYVSE MTDYKGITKR QHEAVADCLE EMGDTVDRLS
     NSLKELKHLE EGDSGEDFWF CLSNVRTWTS AALTDETACM DGFGGKAMAG ELKSLIRTHI
     VSVAEETSNA LALINDFASK H
 
 
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