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TBL33_ARATH
ID   TBL33_ARATH             Reviewed;         425 AA.
AC   F4IH21; Q84W34; Q9SIZ1; Q9XEF9;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Protein trichome birefringence-like 33 {ECO:0000303|PubMed:20388664};
GN   Name=TBL33 {ECO:0000303|PubMed:20388664};
GN   OrderedLocusNames=At2g40320 {ECO:0000312|Araport:AT2G40320};
GN   ORFNames=T07M07.22, T7M7.12;
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 [GENOMIC DNA].
RX   PubMed=10207155;
RA   Wang M.L., Belmonte S., Kim U., Dolan M., Morris J.W., Goodman H.M.;
RT   "A cluster of ABA-regulated genes on Arabidopsis thaliana BAC T07M07.";
RL   Genome Res. 9:325-333(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
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   [4]
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   [5]
RP   GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=17316173; DOI=10.1111/j.1365-313x.2006.02994.x;
RA   Xin Z., Mandaokar A., Chen J., Last R.L., Browse J.;
RT   "Arabidopsis ESK1 encodes a novel regulator of freezing tolerance.";
RL   Plant J. 49:786-799(2007).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=20388664; DOI=10.1104/pp.110.153320;
RA   Bischoff V., Nita S., Neumetzler L., Schindelasch D., Urbain A., Eshed R.,
RA   Persson S., Delmer D., Scheible W.R.;
RT   "TRICHOME BIREFRINGENCE and its homolog AT5G01360 encode plant-specific
RT   DUF231 proteins required for cellulose biosynthesis in Arabidopsis.";
RL   Plant Physiol. 153:590-602(2010).
RN   [7]
RP   3D-STRUCTURE MODELING.
RX   PubMed=20657172; DOI=10.4161/psb.5.8.12414;
RA   Bischoff V., Selbig J., Scheible W.R.;
RT   "Involvement of TBL/DUF231 proteins into cell wall biology.";
RL   Plant Signal. Behav. 5:1057-1059(2010).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=26745802; DOI=10.1371/journal.pone.0146460;
RA   Yuan Y., Teng Q., Zhong R., Haghighat M., Richardson E.A., Ye Z.H.;
RT   "Mutations of Arabidopsis TBL32 and TBL33 affect xylan acetylation and
RT   secondary wall deposition.";
RL   PLoS ONE 11:e0146460-e0146460(2016).
CC   -!- FUNCTION: Probable xylan acetyltransferase that plays a role in xylan
CC       acetylation and normal deposition of secondary cell walls
CC       (PubMed:26745802). Required for 2-O-monoacetylation, 3-O-
CC       monoacetylation and 2,3-O-diacetylation of xylosyl residues in xylan
CC       (PubMed:26745802). Required for the formation of 3-O-acetylated, 2-O-
CC       glucoronic acid-substituted xylosyl residues (PubMed:26745802). May act
CC       as a bridging protein that binds pectin and other cell wall
CC       polysaccharides. Probably involved in maintaining esterification of
CC       pectins (By similarity). {ECO:0000250|UniProtKB:Q9FG35,
CC       ECO:0000269|PubMed:26745802}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000305|PubMed:26745802}; Single-pass type II membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in inflorescence stems undergoing
CC       secondary wall deposition. {ECO:0000269|PubMed:26745802}.
CC   -!- MISCELLANEOUS: Contains 2 motifs that are conserved in esterases, but
CC       it is unlikely that this protein belongs to the catalytically active
CC       pectin esterases. {ECO:0000305|PubMed:20657172}.
CC   -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD25667.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAD25949.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF085279; AAD25949.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC007020; AAD25667.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC09814.1; -; Genomic_DNA.
DR   EMBL; BT004282; AAO42282.1; -; mRNA.
DR   PIR; A84828; A84828.
DR   RefSeq; NP_181563.2; NM_129592.4.
DR   AlphaFoldDB; F4IH21; -.
DR   SMR; F4IH21; -.
DR   STRING; 3702.AT2G40320.1; -.
DR   iPTMnet; F4IH21; -.
DR   PaxDb; F4IH21; -.
DR   PRIDE; F4IH21; -.
DR   ProteomicsDB; 234161; -.
DR   EnsemblPlants; AT2G40320.1; AT2G40320.1; AT2G40320.
DR   GeneID; 818625; -.
DR   Gramene; AT2G40320.1; AT2G40320.1; AT2G40320.
DR   KEGG; ath:AT2G40320; -.
DR   Araport; AT2G40320; -.
DR   TAIR; locus:2063125; AT2G40320.
DR   eggNOG; ENOG502QTQP; Eukaryota.
DR   HOGENOM; CLU_020953_3_1_1; -.
DR   InParanoid; F4IH21; -.
DR   OMA; CRKSIME; -.
DR   OrthoDB; 635575at2759; -.
DR   PRO; PR:F4IH21; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; F4IH21; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; 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:0016413; F:O-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:1990538; F:xylan O-acetyltransferase activity; IMP:TAIR.
DR   GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IGI:TAIR.
DR   GO; GO:1990937; P:xylan acetylation; IMP:TAIR.
DR   InterPro; IPR026057; PC-Esterase.
DR   InterPro; IPR029962; TBL.
DR   InterPro; IPR025846; TBL_N.
DR   PANTHER; PTHR32285; PTHR32285; 1.
DR   Pfam; PF13839; PC-Esterase; 1.
DR   Pfam; PF14416; PMR5N; 1.
PE   2: Evidence at transcript level;
KW   Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..425
FT                   /note="Protein trichome birefringence-like 33"
FT                   /id="PRO_0000425398"
FT   TOPO_DOM        1..26
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        27..47
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..425
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   MOTIF           155..157
FT                   /note="GDS motif"
FT                   /evidence="ECO:0000305|PubMed:20657172"
FT   MOTIF           401..415
FT                   /note="DCXHWCLPGXXDXWN motif"
FT                   /evidence="ECO:0000305|PubMed:20657172"
FT   CONFLICT        310
FT                   /note="T -> A (in Ref. 4; AAO42282)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   425 AA;  49319 MW;  EADD9CDB4A645DBF CRC64;
     MKPSSPISLT SSSIARKARF SPYLFTLLAF ILFVSVLYGE DFMCIFGQLE PNFVLPPSRT
     PEKNKKSEKL AFAIGKTEES CDVFSGKWVR DEVSRPLYEE WECPYIQPQL TCQEHGRPDK
     DYQFWRWQPN HCDLPSFNAS LMLETLRGKR MMYVGDSLNR GMFVSMICLL HRLIPEDQKS
     IKTNGSLTVF TAKEYNATIE FYWAPFLLES NSDDAIVHRI SDRVVRKGSI NKHGRHWKGV
     DIIIFNTYLW WMTGLKMNIL QGSFDDKEKN IVEVSTEDAY RMGMKSMLRW VKNNMDRKKT
     RVFFTSMSPT HAKGIDWGGE PGQNCYNQTT LIEDPSYWGS DCRKSIMKVI GEVFGRSKTP
     ITLLNITQMS NYRKDAHTSI YKKQWSPLTA EQLENPTSYA DCVHWCLPGL QDTWNELLFA
     KLFYT
 
 
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