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PAE10_ARATH
ID   PAE10_ARATH             Reviewed;         416 AA.
AC   Q66GM8; B9DGF9; O65250; Q0WRK2;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Pectin acetylesterase 10 {ECO:0000303|PubMed:25115560};
DE            EC=3.1.1.- {ECO:0000305};
DE   Flags: Precursor;
GN   Name=PAE10 {ECO:0000303|PubMed:25115560};
GN   OrderedLocusNames=At5g26670 {ECO:0000312|Araport:AT5G26670};
GN   ORFNames=F21E10.11 {ECO:0000312|EMBL:AAC13595.1};
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=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] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   GENE FAMILY, AND DISRUPTION PHENOTYPE.
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:0000250|UniProtKB:B9DFR3}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q66GM8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q66GM8-2; Sequence=VSP_057379;
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. {ECO:0000269|PubMed:25115560}.
CC   -!- SIMILARITY: Belongs to the pectinacetylesterase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC13595.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF058914; AAC13595.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED93578.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93579.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM69252.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM69253.1; -; Genomic_DNA.
DR   EMBL; AK317140; BAH19826.1; -; mRNA.
DR   EMBL; BT015374; AAU05497.1; -; mRNA.
DR   EMBL; BT029367; ABK32181.1; -; mRNA.
DR   EMBL; AK228304; BAF00247.1; -; mRNA.
DR   PIR; T01197; T01197.
DR   RefSeq; NP_001318657.1; NM_001343974.1. [Q66GM8-2]
DR   RefSeq; NP_001330948.1; NM_001343975.1. [Q66GM8-2]
DR   RefSeq; NP_850878.2; NM_180547.3. [Q66GM8-1]
DR   RefSeq; NP_974837.1; NM_203108.2. [Q66GM8-2]
DR   AlphaFoldDB; Q66GM8; -.
DR   SMR; Q66GM8; -.
DR   STRING; 3702.AT5G26670.1; -.
DR   ESTHER; arath-q66gm8; Pectinacetylesterase-Notum.
DR   PaxDb; Q66GM8; -.
DR   PRIDE; Q66GM8; -.
DR   ProteomicsDB; 226045; -. [Q66GM8-1]
DR   EnsemblPlants; AT5G26670.1; AT5G26670.1; AT5G26670. [Q66GM8-1]
DR   EnsemblPlants; AT5G26670.2; AT5G26670.2; AT5G26670. [Q66GM8-2]
DR   EnsemblPlants; AT5G26670.3; AT5G26670.3; AT5G26670. [Q66GM8-2]
DR   EnsemblPlants; AT5G26670.4; AT5G26670.4; AT5G26670. [Q66GM8-2]
DR   GeneID; 832722; -.
DR   Gramene; AT5G26670.1; AT5G26670.1; AT5G26670. [Q66GM8-1]
DR   Gramene; AT5G26670.2; AT5G26670.2; AT5G26670. [Q66GM8-2]
DR   Gramene; AT5G26670.3; AT5G26670.3; AT5G26670. [Q66GM8-2]
DR   Gramene; AT5G26670.4; AT5G26670.4; AT5G26670. [Q66GM8-2]
DR   KEGG; ath:AT5G26670; -.
DR   Araport; AT5G26670; -.
DR   TAIR; locus:2146814; AT5G26670.
DR   eggNOG; KOG4287; Eukaryota.
DR   InParanoid; Q66GM8; -.
DR   OMA; MARVFWT; -.
DR   PhylomeDB; Q66GM8; -.
DR   PRO; PR:Q66GM8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q66GM8; baseline and differential.
DR   Genevisible; Q66GM8; 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; IPR004963; PAE/NOTUM.
DR   PANTHER; PTHR21562; PTHR21562; 1.
DR   Pfam; PF03283; PAE; 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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..416
FT                   /note="Pectin acetylesterase 10"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431775"
FT   ACT_SITE        198
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   ACT_SITE        294
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   ACT_SITE        361
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   VAR_SEQ         1..118
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_057379"
FT   CONFLICT        156
FT                   /note="S -> G (in Ref. 3; BAH19826)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   416 AA;  46562 MW;  DFED3E3674873190 CRC64;
     MRKLFLLGFI VAGLVLGNEA NGYLEFNVTE LDRIEDLEFG FSKFSSNFNP LMVGLTLIRG
     AGSKGAVCLD GTLPGYHLHR GHGSGANSWL IQLEGGGWCD NIRNCVYRKK SRRGSSNYME
     KQIQFTGILS NKAQENPDFF NWNRVKLRYC DGGSFSGDSQ NKAARLQFRG EKIWRAAMDD
     LKAKGMRNAK QALLSGCSAG GLAVILRCDE FRNLFSGWTR VKCLSDAGLF LDTPDVSGGH
     TIRNLYNGVV QLQGVKNNLP HLCTNHLNPT SCFFPQNLIS QMKTPLFIVN AAYDIWQIQS
     SIAPPSADPS GYWHECRLNH GRCTPAQIRF LQGFRNQMLR AVSGFSNSKK NGLFINSCFA
     HCQTERQDTW FADDSPVIHK KAVAIAVGDW YFDRAEVKLI DCPYPCDRSC HNLVFR
 
 
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