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TBL43_ARATH
ID   TBL43_ARATH             Reviewed;         368 AA.
AC   Q6DR10; O80855; Q84N42; Q84N43;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Protein trichome birefringence-like 43;
GN   Name=TBL43; OrderedLocusNames=At2g30900; ORFNames=AT1G29050.1;
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=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   [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;
RA   Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA   Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=16244158; DOI=10.1104/pp.105.063479;
RA   Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA   Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT   "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT   reveals numerous transcript variants.";
RL   Plant Physiol. 139:1323-1337(2005).
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).
CC   -!- FUNCTION: May act as a bridging protein that binds pectin and other
CC       cell wall polysaccharides. Probably involved in maintaining
CC       esterification of pectins (By similarity). May be involved in the
CC       specific O-acetylation of cell wall polymers (By similarity).
CC       {ECO:0000250|UniProtKB:Q9FG35, ECO:0000250|UniProtKB:Q9LY46}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6DR10-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6DR10-2; Sequence=VSP_053699;
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=AAC20724.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAP22495.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC004669; AAC20724.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002685; AEC08454.1; -; Genomic_DNA.
DR   EMBL; AY649305; AAT69222.1; -; mRNA.
DR   EMBL; AY262050; AAP22494.1; -; mRNA.
DR   EMBL; AY262051; AAP22495.1; ALT_INIT; mRNA.
DR   PIR; A84714; A84714.
DR   RefSeq; NP_180647.2; NM_128642.2. [Q6DR10-1]
DR   AlphaFoldDB; Q6DR10; -.
DR   SMR; Q6DR10; -.
DR   STRING; 3702.AT2G30900.1; -.
DR   iPTMnet; Q6DR10; -.
DR   PaxDb; Q6DR10; -.
DR   PRIDE; Q6DR10; -.
DR   ProteomicsDB; 234136; -. [Q6DR10-1]
DR   EnsemblPlants; AT2G30900.1; AT2G30900.1; AT2G30900. [Q6DR10-1]
DR   GeneID; 817640; -.
DR   Gramene; AT2G30900.1; AT2G30900.1; AT2G30900. [Q6DR10-1]
DR   KEGG; ath:AT2G30900; -.
DR   Araport; AT2G30900; -.
DR   TAIR; locus:2052856; AT2G30900.
DR   eggNOG; ENOG502QVJM; Eukaryota.
DR   HOGENOM; CLU_020953_3_0_1; -.
DR   InParanoid; Q6DR10; -.
DR   OMA; CNITRFN; -.
DR   OrthoDB; 730219at2759; -.
DR   PhylomeDB; Q6DR10; -.
DR   PRO; PR:Q6DR10; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q6DR10; baseline and differential.
DR   Genevisible; Q6DR10; AT.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016413; F:O-acetyltransferase activity; IBA:GO_Central.
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   Alternative splicing; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..368
FT                   /note="Protein trichome birefringence-like 43"
FT                   /id="PRO_0000425408"
FT   TRANSMEM        9..25
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   MOTIF           117..119
FT                   /note="GDS motif"
FT   MOTIF           344..358
FT                   /note="DCXHWCLPGXXDXWN motif"
FT   VAR_SEQ         216..368
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16244158"
FT                   /id="VSP_053699"
FT   CONFLICT        205
FT                   /note="H -> R (in Ref. 4; AAP22494/AAP22495)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   368 AA;  41248 MW;  8CB29EEB50FAA811 CRC64;
     MMRGAAPTGV VSVMVLMILV LLKQIESASA NGSSLGLPPR KFCNIYQGSW VYDKSYPLYD
     SKNCPFIERQ FNCKSNGRPD SEYLKYRWQP SGCNLPRFNG LDFLGRIMKG KKLMFVGDSL
     SLNQWQSLTC LLHNAAPKAN STSTRSPSGL SVFSFPAYNS SIMFSRNAFL VDIVGAPPKR
     VMKLDSISSG SLWKTADVLV FNSWHWWLHT DRKQPWDAIM SGNVTVKDMD RLVAYEKAMM
     TWAKWIDQNI DPSKTKVFFQ GISPDHGRAR EWSKQGGKGS CIGETKPIMG SSYLAGPHAA
     EMVVAKVIKT MKNQARLMDV TLMSQLRKDG HPSVYGFGGH RMADCSHWCL SGVPDSWNQL
     LYSELFHS
 
 
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