ID   PLP3B_ARATH             Reviewed;         230 AA.
AC   Q8LCV1; Q9FJZ8;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Thioredoxin domain-containing protein PLP3B;
DE   AltName: Full=Phosducin-like protein 3B;
GN   Name=PLP3B; OrderedLocusNames=At5g66410; ORFNames=K1F13.6;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
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   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=18390592; DOI=10.1105/tpc.107.057737;
RA   Castellano M.M., Sablowski R.;
RT   "Phosducin-Like Protein 3 is required for microtubule-dependent steps of
RT   cell division but not for meristem growth in Arabidopsis.";
RL   Plant Cell 20:969-981(2008).
CC   -!- FUNCTION: Tubulin-binding protein involved in microtubule formation.
CC       {ECO:0000269|PubMed:18390592}.
CC   -!- SUBUNIT: Interacts with TUBB2, TUBB3, TUBB4 and TUBB5. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, leaves, stems and
CC       flowers. {ECO:0000269|PubMed:18390592}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but plants with reduced levels of both PLP3A and PLP3B show
CC       defects in cytokinesis, cortical microtubule array formation, oriented
CC       cell growth, and maintenance of proper ploidy.
CC       {ECO:0000269|PubMed:18390592}.
CC   -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB10917.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB013389; BAB10917.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED98210.1; -; Genomic_DNA.
DR   EMBL; BT003998; AAO42037.1; -; mRNA.
DR   EMBL; BT005683; AAO64103.1; -; mRNA.
DR   EMBL; AY086393; AAM64460.1; -; mRNA.
DR   RefSeq; NP_569033.1; NM_126039.4.
DR   AlphaFoldDB; Q8LCV1; -.
DR   SMR; Q8LCV1; -.
DR   BioGRID; 22015; 3.
DR   IntAct; Q8LCV1; 2.
DR   STRING; 3702.AT5G66410.1; -.
DR   PaxDb; Q8LCV1; -.
DR   PRIDE; Q8LCV1; -.
DR   ProteomicsDB; 226202; -.
DR   EnsemblPlants; AT5G66410.1; AT5G66410.1; AT5G66410.
DR   GeneID; 836773; -.
DR   Gramene; AT5G66410.1; AT5G66410.1; AT5G66410.
DR   KEGG; ath:AT5G66410; -.
DR   Araport; AT5G66410; -.
DR   TAIR; locus:2154945; AT5G66410.
DR   eggNOG; KOG1672; Eukaryota.
DR   HOGENOM; CLU_072378_3_0_1; -.
DR   InParanoid; Q8LCV1; -.
DR   OMA; CHFFHRE; -.
DR   OrthoDB; 1444223at2759; -.
DR   PhylomeDB; Q8LCV1; -.
DR   PRO; PR:Q8LCV1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8LCV1; baseline and differential.
DR   Genevisible; Q8LCV1; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048487; F:beta-tubulin binding; ISS:TAIR.
DR   GO; GO:0043622; P:cortical microtubule organization; IGI:TAIR.
DR   GO; GO:0000911; P:cytokinesis by cell plate formation; IGI:TAIR.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Microtubule; Nucleus; Reference proteome.
FT   CHAIN           1..230
FT                   /note="Thioredoxin domain-containing protein PLP3B"
FT                   /id="PRO_0000428877"
FT   DOMAIN          89..173
FT                   /note="Thioredoxin"
FT   REGION          199..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   230 AA;  26368 MW;  A4DFE050A2679995 CRC64;
     MDPDTVKSTL SNLAFGNVLA AAARDYKKEV LANEKAQGSR PVNEEVDLDE LMDDPELEKL
     HADRIAALRR EVEKREAFKR QGHGEYREVS EGDFLGEVTR SEKVICHFYH KEFYRCKIMD
     KHLKTLAPRH VDTKFIKMDA ENAPFFVTKL AIKTLPCVIL FSKGIAMDRL VGFQDLGAKD
     DFSTTKLENL LVKKGMLSEK RKEEDEEDYE YQESIRRSVR SSANVDSDSD