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TBL10_ARATH
ID   TBL10_ARATH             Reviewed;         469 AA.
AC   Q9LDG2; Q93YQ2;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Protein trichome birefringence-like 10;
GN   Name=TBL10; OrderedLocusNames=At3g06080; ORFNames=F24F17.6, F28L1.1;
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] (ISOFORM 2).
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.
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   [5]
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   [6]
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=Q9LDG2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LDG2-2; Sequence=VSP_053687, VSP_053688;
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}.
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DR   EMBL; AC018907; AAF30301.1; -; Genomic_DNA.
DR   EMBL; AC068073; AAF66136.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74340.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74341.1; -; Genomic_DNA.
DR   EMBL; AY059837; AAL24319.1; -; mRNA.
DR   EMBL; BT008735; AAP42748.1; -; mRNA.
DR   RefSeq; NP_566270.1; NM_111483.3. [Q9LDG2-2]
DR   RefSeq; NP_974235.1; NM_202506.2. [Q9LDG2-1]
DR   AlphaFoldDB; Q9LDG2; -.
DR   SMR; Q9LDG2; -.
DR   STRING; 3702.AT3G06080.2; -.
DR   iPTMnet; Q9LDG2; -.
DR   PaxDb; Q9LDG2; -.
DR   PRIDE; Q9LDG2; -.
DR   ProteomicsDB; 233011; -. [Q9LDG2-1]
DR   EnsemblPlants; AT3G06080.1; AT3G06080.1; AT3G06080. [Q9LDG2-2]
DR   EnsemblPlants; AT3G06080.2; AT3G06080.2; AT3G06080. [Q9LDG2-1]
DR   GeneID; 819781; -.
DR   Gramene; AT3G06080.1; AT3G06080.1; AT3G06080. [Q9LDG2-2]
DR   Gramene; AT3G06080.2; AT3G06080.2; AT3G06080. [Q9LDG2-1]
DR   KEGG; ath:AT3G06080; -.
DR   Araport; AT3G06080; -.
DR   TAIR; locus:2080389; AT3G06080.
DR   eggNOG; ENOG502QPPC; Eukaryota.
DR   InParanoid; Q9LDG2; -.
DR   OMA; KWIQNEV; -.
DR   OrthoDB; 667501at2759; -.
DR   PhylomeDB; Q9LDG2; -.
DR   PRO; PR:Q9LDG2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LDG2; baseline and differential.
DR   Genevisible; Q9LDG2; 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   GO; GO:0007623; P:circadian rhythm; IEP: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   Alternative splicing; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..469
FT                   /note="Protein trichome birefringence-like 10"
FT                   /id="PRO_0000425376"
FT   TRANSMEM        33..53
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   MOTIF           176..178
FT                   /note="GDS motif"
FT   MOTIF           424..438
FT                   /note="DCXHWCLPGXXDXWN motif"
FT   VAR_SEQ         341..346
FT                   /note="GGDWKT -> FVRYYS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_053687"
FT   VAR_SEQ         347..469
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_053688"
SQ   SEQUENCE   469 AA;  53649 MW;  AFDE9FD427304E3E CRC64;
     MSKNSNVEEN GGAKPICEAL RRFKRSRLVF EPSLGVLGFF LVGVCLVCSF FFFDYRSVAK
     SYGLSDKSER FVWLKFDNIS SSSSSSSNSS KRVGFLEESG SGCDVFDGDW VWDESYPLYQ
     SKDCRFLDEG FRCSDFGRSD LFYTQWRWQP RHCNLPRFDA KLMLEKLRDK RLVFVGDSIG
     RNQWESLLCL LSSAVKNESL IYEINGSPIT KHKGFLVFKF EEYNCTVEYY RSPFLVPQSR
     PPIGSPGKVK TSLKLDTMDW TSSKWRDADV LVLNTGHWWN EGKTTRTGCY FQEGEEVKLK
     MNVDDAYKRA LNTVVKWIHT ELDSNKTQVF FRTFAPVHFR GGDWKTGGTC HMETLPEIGT
     SLASSETWEQ LKILRDVLSH NSNRSETVKV KLLNITAMAA QRKDGHPSLY YLGPHGPAPL
     HRQDCSHWCL PGVPDTWNEL FYALFMKQEA PSSSKRVEEA NSTGNVTMS
 
 
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