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PAE8_ARATH
ID   PAE8_ARATH              Reviewed;         397 AA.
AC   Q6DBP4; F4JT68; O65713;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Pectin acetylesterase 8 {ECO:0000303|PubMed:25115560};
DE            EC=3.1.1.- {ECO:0000305};
DE   Flags: Precursor;
GN   Name=PAE8 {ECO:0000303|PubMed:25115560};
GN   OrderedLocusNames=At4g19420 {ECO:0000312|Araport:AT4G19420};
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;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GENE FAMILY, DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=25115560; DOI=10.1007/s00425-014-2139-6;
RA   de Souza A., Hull P.A., Gille S., Pauly M.;
RT   "Identification and functional characterization of the distinct plant
RT   pectin esterases PAE8 and PAE9 and their deletion mutants.";
RL   Planta 240:1123-1138(2014).
CC   -!- FUNCTION: Hydrolyzes acetyl esters in homogalacturonan regions of
CC       pectin. In type I primary cell wall, galacturonic acid residues of
CC       pectin can be acetylated at the O-2 and O-3 positions. Decreasing the
CC       degree of acetylation of pectin gels in vitro alters their physical
CC       properties. {ECO:0000269|PubMed:25115560}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced.According to EST sequences.
CC         {ECO:0000305};
CC       Name=1;
CC         IsoId=Q6DBP4-1; Sequence=Displayed;
CC   -!- DISRUPTION PHENOTYPE: Reduced inflorescence stem growth and increased
CC       levels of acetate in rosette leaves. {ECO:0000269|PubMed:25115560}.
CC   -!- SIMILARITY: Belongs to the pectinacetylesterase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA18629.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78944.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL022580; CAA18629.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161550; CAB78944.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84179.2; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84180.1; -; Genomic_DNA.
DR   EMBL; BT014978; AAT70429.1; -; mRNA.
DR   EMBL; BT015714; AAU45212.1; -; mRNA.
DR   PIR; T05825; T05825.
DR   RefSeq; NP_001319996.1; NM_001341336.1. [Q6DBP4-1]
DR   RefSeq; NP_193677.2; NM_118062.7. [Q6DBP4-1]
DR   AlphaFoldDB; Q6DBP4; -.
DR   SMR; Q6DBP4; -.
DR   STRING; 3702.AT4G19420.1; -.
DR   ESTHER; arath-o65713; Pectinacetylesterase-Notum.
DR   PaxDb; Q6DBP4; -.
DR   PRIDE; Q6DBP4; -.
DR   ProteomicsDB; 236319; -. [Q6DBP4-1]
DR   EnsemblPlants; AT4G19420.1; AT4G19420.1; AT4G19420. [Q6DBP4-1]
DR   EnsemblPlants; AT4G19420.2; AT4G19420.2; AT4G19420. [Q6DBP4-1]
DR   GeneID; 827683; -.
DR   Gramene; AT4G19420.1; AT4G19420.1; AT4G19420. [Q6DBP4-1]
DR   Gramene; AT4G19420.2; AT4G19420.2; AT4G19420. [Q6DBP4-1]
DR   KEGG; ath:AT4G19420; -.
DR   Araport; AT4G19420; -.
DR   TAIR; locus:2140436; AT4G19420.
DR   eggNOG; KOG4287; Eukaryota.
DR   InParanoid; Q6DBP4; -.
DR   OMA; GCRDDIT; -.
DR   PhylomeDB; Q6DBP4; -.
DR   PRO; PR:Q6DBP4; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q6DBP4; baseline and differential.
DR   Genevisible; Q6DBP4; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0052793; F:pectin acetylesterase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR004963; PAE/NOTUM.
DR   PANTHER; PTHR21562; PTHR21562; 1.
DR   Pfam; PF03283; PAE; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell wall; Cell wall biogenesis/degradation;
KW   Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..397
FT                   /note="Pectin acetylesterase 8"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431773"
FT   ACT_SITE        172
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   ACT_SITE        268
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   ACT_SITE        335
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   397 AA;  44439 MW;  DE9776B596206978 CRC64;
     MFKLKQWLIY LVCSLVIMNT EGLFVNITFV RNAVAKGAVC LDGSPPAYHL DRGSGTGINS
     WLIQLEGGGW CNNVTNCVSR MHTRLGSSKK MVENLAFSAI LSNKKQYNPD FYNWNRVKVR
     YCDGASFTGD VEAVNPATNL HFRGARVWLA VMQELLAKGM INAENAVLSG CSAGGLASLM
     HCDSFRALLP MGTKVKCLSD AGFFLNTRDV SGVQYIKTYF EDVVTLHGSA KNLPRSCTSR
     LTPAMCFFPQ YVARQIRTPL FILNAAYDSW QIKNILAPRA ADPYGKWQSC QLDIKNCHPS
     QIKVMQDFRL EFLSAVIGLG RSSSRGMFID SCYTHCQTET QTSWFWQDSP ILNRTTIAKA
     VGDWVYDRTL FQKIDCPYPC NPTCHHRVFT PLDAPPI
 
 
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