位置:首页 > 蛋白库 > PAE2_ARATH
PAE2_ARATH
ID   PAE2_ARATH              Reviewed;         444 AA.
AC   F4I839; Q8L7Z5; Q9FVU3;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Pectin acetylesterase 2 {ECO:0000303|PubMed:25115560};
DE            EC=3.1.1.- {ECO:0000305};
DE   Flags: Precursor;
GN   Name=PAE2 {ECO:0000303|PubMed:25115560};
GN   OrderedLocusNames=At1g57590 {ECO:0000312|Araport:AT1G57590};
GN   ORFNames=T8L23.6 {ECO:0000312|EMBL:AAG50747.1};
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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] OF 21-444.
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   GENE FAMILY.
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   -!- SIMILARITY: Belongs to the pectinacetylesterase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG50747.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAM74495.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC079733; AAG50747.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002684; AEE33439.1; -; Genomic_DNA.
DR   EMBL; AY123981; AAM74495.1; ALT_INIT; mRNA.
DR   PIR; A96610; A96610.
DR   RefSeq; NP_176072.3; NM_104556.5.
DR   AlphaFoldDB; F4I839; -.
DR   SMR; F4I839; -.
DR   STRING; 3702.AT1G57590.1; -.
DR   ESTHER; arath-pae2; Pectinacetylesterase-Notum.
DR   PaxDb; F4I839; -.
DR   PRIDE; F4I839; -.
DR   ProteomicsDB; 248887; -.
DR   EnsemblPlants; AT1G57590.1; AT1G57590.1; AT1G57590.
DR   GeneID; 842135; -.
DR   Gramene; AT1G57590.1; AT1G57590.1; AT1G57590.
DR   KEGG; ath:AT1G57590; -.
DR   Araport; AT1G57590; -.
DR   TAIR; locus:2206490; AT1G57590.
DR   eggNOG; KOG4287; Eukaryota.
DR   HOGENOM; CLU_031008_0_0_1; -.
DR   InParanoid; F4I839; -.
DR   OMA; NGMMMEF; -.
DR   OrthoDB; 610784at2759; -.
DR   PRO; PR:F4I839; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4I839; baseline and differential.
DR   Genevisible; F4I839; 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   Cell wall; Cell wall biogenesis/degradation; Glycoprotein; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..45
FT                   /evidence="ECO:0000255"
FT   CHAIN           46..444
FT                   /note="Pectin acetylesterase 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431767"
FT   ACT_SITE        225
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   ACT_SITE        321
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   ACT_SITE        388
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        259
FT                   /note="D -> G (in Ref. 3; AAM74495)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   444 AA;  49915 MW;  22A7CD8986B6AE9B CRC64;
     MLLSHSRSPY KPRYVIKSKT SMIKKCKMKK LLWSWIILFN IHVNGMMMEF DEMEWFTVFN
     GTKVFQTQND VFSEAKFPMV GLTLIQSAAA KGAVCLDGSL PGYHLHRGFG SGANNWLVQL
     EGGGWCDTIR NCVYRKTTRR GSSSYMEKEI PFTGILSDKA ADNPDFYNWN RVKVRYCDGG
     SFSGDSENKA AQLQFRGKRI WLAAMEDLMA KGMRQAKQAL LSGCSAGGLA VILRCDDFGK
     LFPPSTRVKC LSDAGFFLDA IDVSGGRSLR RLYAGVVRLQ NLQTNLPQYC VNRLNPTSCF
     FPQNLINQVK TPLFILNAAY DSWQIQESLA PKSADPSGSW NDCRLNYAKC SASQIQFLQG
     FRTRMVNLVK GFAMPSKNGV FLNSCFAHCQ TERHDTWFAQ NSPAIKNKGI AVAVGDWYFE
     RGGAKLIDCA YPCDKTCHNL VFRR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024