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TBL45_ARATH
ID   TBL45_ARATH             Reviewed;         398 AA.
AC   O80872;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Protein trichome birefringence-like 45;
GN   Name=TBL45; OrderedLocusNames=At2g30010; ORFNames=F23F1.7;
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].
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].
RA   Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; AC004680; AAC31851.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08335.1; -; Genomic_DNA.
DR   EMBL; AF428324; AAL16254.1; -; mRNA.
DR   EMBL; BT020370; AAV85725.1; -; mRNA.
DR   PIR; T02484; T02484.
DR   RefSeq; NP_565692.1; NM_128556.3.
DR   AlphaFoldDB; O80872; -.
DR   SMR; O80872; -.
DR   STRING; 3702.AT2G30010.1; -.
DR   iPTMnet; O80872; -.
DR   PaxDb; O80872; -.
DR   ProteomicsDB; 234137; -.
DR   EnsemblPlants; AT2G30010.1; AT2G30010.1; AT2G30010.
DR   GeneID; 817552; -.
DR   Gramene; AT2G30010.1; AT2G30010.1; AT2G30010.
DR   KEGG; ath:AT2G30010; -.
DR   Araport; AT2G30010; -.
DR   TAIR; locus:2045688; AT2G30010.
DR   eggNOG; ENOG502QR9P; Eukaryota.
DR   HOGENOM; CLU_020953_3_0_1; -.
DR   InParanoid; O80872; -.
DR   PhylomeDB; O80872; -.
DR   PRO; PR:O80872; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O80872; baseline and differential.
DR   Genevisible; O80872; 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   Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..398
FT                   /note="Protein trichome birefringence-like 45"
FT                   /id="PRO_0000425410"
FT   TRANSMEM        1..21
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   MOTIF           131..133
FT                   /note="GDS motif"
FT   MOTIF           375..389
FT                   /note="DCXHWCLPGXXDXWN motif"
SQ   SEQUENCE   398 AA;  45477 MW;  F55EBBFA49C1C1D9 CRC64;
     MAAVQCLTFL FLFLLQNATS ASPLPLFRRP IQSNHSNFVK HPRRSQVVFP VNHSSCDLFA
     GEWVRDETYP LYRSKECGRG IIDPGFDCQT YGRPDSDYLK FRWKPFNCNV PRFNGVKFLQ
     EMRDKTIMFV GDSLGRNQWE SLICMISSSA PSINTHIIHE DPLSTFKILD YNVKVSFYRA
     PYLVDIDKIN GKTTLKLDEI SVDASNAWRT ADVLLFNTGH WWSHTGSLRG WEQMETGGRY
     YGDMDRLVAL RKGLGTWSSW VLRYINSPLT RVFFLSVSPT HYNPNEWTSR SKTSTITQGG
     KSCYGQTTPF SGTTYPTSSY VNQKKVIDDV VKEMKSHVSL MDITMLSALR VDGHPSIYSG
     DLNPSLKRNP DRSSDCSHWC LPGLPDTWNQ LFYAALLY
 
 
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