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AXY9_ARATH
ID   AXY9_ARATH              Reviewed;         368 AA.
AC   Q9M9N9; A0A178VCF2; Q8L7K6;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Protein ALTERED XYLOGLUCAN 9 {ECO:0000303|PubMed:25681330};
GN   Name=AXY9 {ECO:0000303|PubMed:25681330};
GN   OrderedLocusNames=At3g03210 {ECO:0000312|Araport:AT3G03210};
GN   ORFNames=T17B22.10 {ECO:0000312|EMBL:AAF26105.1};
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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   Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND DISRUPTION PHENOTYPE.
RX   PubMed=25681330; DOI=10.1104/pp.114.256479;
RA   Schultink A., Naylor D., Dama M., Pauly M.;
RT   "The role of the plant-specific ALTERED XYLOGLUCAN9 protein in Arabidopsis
RT   cell wall polysaccharide O-acetylation.";
RL   Plant Physiol. 167:1271-1283(2015).
RN   [6]
RP   FUNCTION.
RX   PubMed=30083810; DOI=10.1007/s00425-018-2972-0;
RA   Zhong R., Cui D., Ye Z.H.;
RT   "Xyloglucan O-acetyltransferases from Arabidopsis thaliana and Populus
RT   trichocarpa catalyze acetylation of fucosylated galactose residues on
RT   xyloglucan side chains.";
RL   Planta 248:1159-1171(2018).
CC   -!- FUNCTION: Component of the plant cell wall polysaccharide acetylation
CC       pathway (PubMed:25681330, PubMed:30083810). Does not directly catalyze
CC       O-acetylation of xyloglucan but exhibits weak acetylesterase activity
CC       in vitro (PubMed:30083810). {ECO:0000269|PubMed:25681330,
CC       ECO:0000269|PubMed:30083810}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:25681330}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Severe growth defects and collapsed xylem
CC       (PubMed:25681330). Decreased xyloglucan acetylation and decreased O-
CC       acetylation of xylan (PubMed:25681330). {ECO:0000269|PubMed:25681330}.
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DR   EMBL; AC012328; AAF26105.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE73913.1; -; Genomic_DNA.
DR   EMBL; AY128404; AAM91607.1; -; mRNA.
DR   EMBL; BT020433; AAW28560.1; -; mRNA.
DR   RefSeq; NP_186971.1; NM_111191.4.
DR   AlphaFoldDB; Q9M9N9; -.
DR   IntAct; Q9M9N9; 18.
DR   PaxDb; Q9M9N9; -.
DR   PRIDE; Q9M9N9; -.
DR   ProteomicsDB; 179688; -.
DR   EnsemblPlants; AT3G03210.1; AT3G03210.1; AT3G03210.
DR   GeneID; 821222; -.
DR   Gramene; AT3G03210.1; AT3G03210.1; AT3G03210.
DR   KEGG; ath:AT3G03210; -.
DR   Araport; AT3G03210; -.
DR   TAIR; locus:2097710; AT3G03210.
DR   eggNOG; ENOG502QSS7; Eukaryota.
DR   HOGENOM; CLU_761527_0_0_1; -.
DR   InParanoid; Q9M9N9; -.
DR   OMA; TVDGMHY; -.
DR   OrthoDB; 1034492at2759; -.
DR   PhylomeDB; Q9M9N9; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M9N9; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR   GO; GO:0005796; C:Golgi lumen; IDA:TAIR.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016407; F:acetyltransferase activity; IMP:TAIR.
DR   GO; GO:1990538; F:xylan O-acetyltransferase activity; TAS:TAIR.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0045492; P:xylan biosynthetic process; IMP:TAIR.
PE   1: Evidence at protein level;
KW   Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..368
FT                   /note="Protein ALTERED XYLOGLUCAN 9"
FT                   /id="PRO_0000453953"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:25681330"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..368
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:25681330"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        224
FT                   /note="G -> R (in Ref. 3; AAM91607)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   368 AA;  41337 MW;  BDD38A5D8126BCA9 CRC64;
     MLGAIHLGVL AACFVLFVPM AMAGWHLSRN KMLFFSGALF ISLAVCVHLT PYFPSVSDIV
     ASVSSVVVYD HRISCINEVN QIVWDVKPVP NPESVRRNNG STKLDYFVKN WDWMKSRKVL
     SCEFQKLDKF DVSDLLNGSW VVVAGDSQAR FVALSLLNLV LGSDSKAMDS VRGDLFRRHS
     DYSIVVKEIG MKLDFVWAPY EKDLDDLVVS YKKMKKYPDV VIMGTGLWHM LHVNNASDFG
     FRLRQLSSHV ESLVPLTPKE QEGGGSVSGR SVHLFWIGMP VLINGMLNTD EKKEKMSDTV
     WHEYDRSLGE SKILRQMGGP LILLDIQSFT WNCGPQCTLD GMHYDSAVYD AAVHVMLNAL
     LIESHQSL
 
 
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