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PLP3A_ARATH
ID   PLP3A_ARATH             Reviewed;         230 AA.
AC   Q6NPL9; Q9SVK3;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Thioredoxin domain-containing protein PLP3A;
DE   AltName: Full=Phosducin-like protein 3A;
GN   Name=PLP3A; OrderedLocusNames=At3g50960; ORFNames=F18B3.240;
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].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, INTERACTION WITH TUBB2; TUBB3; TUBB4 AND TUBB5, SUBCELLULAR
RP   LOCATION, 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.
CC       {ECO:0000269|PubMed:18390592}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18390592}. Nucleus
CC       {ECO:0000269|PubMed:18390592}.
CC   -!- TISSUE SPECIFICITY: Expressed in embryos, shoot meristems, leaf
CC       primordia, root meristems, floral meristems and young floral buds.
CC       {ECO:0000269|PubMed:18390592}.
CC   -!- MISCELLANEOUS: Plant roots over-expressing PLP3A have increased
CC       microtubule resistance to propyzamide, an inhibitor of tubulin
CC       polymerization. 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 (PubMed:18390592).
CC       {ECO:0000305|PubMed:18390592}.
CC   -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB42925.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL049862; CAB42925.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE78732.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM63810.1; -; Genomic_DNA.
DR   EMBL; BT010901; AAR24679.1; -; mRNA.
DR   EMBL; AK229066; BAF00947.1; -; mRNA.
DR   PIR; T08417; T08417.
DR   RefSeq; NP_001325881.1; NM_001339487.1.
DR   RefSeq; NP_190665.2; NM_114956.3.
DR   AlphaFoldDB; Q6NPL9; -.
DR   SMR; Q6NPL9; -.
DR   BioGRID; 9578; 6.
DR   IntAct; Q6NPL9; 4.
DR   STRING; 3702.AT3G50960.1; -.
DR   PaxDb; Q6NPL9; -.
DR   PRIDE; Q6NPL9; -.
DR   ProteomicsDB; 234729; -.
DR   EnsemblPlants; AT3G50960.1; AT3G50960.1; AT3G50960.
DR   EnsemblPlants; AT3G50960.2; AT3G50960.2; AT3G50960.
DR   GeneID; 824260; -.
DR   Gramene; AT3G50960.1; AT3G50960.1; AT3G50960.
DR   Gramene; AT3G50960.2; AT3G50960.2; AT3G50960.
DR   KEGG; ath:AT3G50960; -.
DR   Araport; AT3G50960; -.
DR   TAIR; locus:2077942; AT3G50960.
DR   eggNOG; KOG1672; Eukaryota.
DR   HOGENOM; CLU_072378_3_0_1; -.
DR   InParanoid; Q6NPL9; -.
DR   OMA; SYGERNK; -.
DR   OrthoDB; 1444223at2759; -.
DR   PhylomeDB; Q6NPL9; -.
DR   PRO; PR:Q6NPL9; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q6NPL9; baseline and differential.
DR   Genevisible; Q6NPL9; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0048487; F:beta-tubulin binding; IPI:UniProtKB.
DR   GO; GO:0043622; P:cortical microtubule organization; 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   1: Evidence at protein level;
KW   Cytoplasm; Microtubule; Nucleus; Reference proteome.
FT   CHAIN           1..230
FT                   /note="Thioredoxin domain-containing protein PLP3A"
FT                   /id="PRO_0000428876"
FT   DOMAIN          89..173
FT                   /note="Thioredoxin"
FT   REGION          197..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   230 AA;  26263 MW;  292091CEE8345F8E CRC64;
     MDPDAVKSTL SNLAFGNVMA AAARNYQKEV LANEKAQGSN PVNEEVDLDE LMDDPELERL
     HADRIAALKR EVEKRESFKR QGHGEYREVS EGDFLGEVTR SEKVICHFYH KEFYRCKIMD
     KHLKTLAPRH VDTKFIKVDA ENAPFFVTKL AIKTLPCVVL FSKGVAMDRL VGFQDLGTKD
     DFTTNKLENV LLKKGMLSKK KKEEDDEDAE YQESIRRSVR SSENLDSDSD
 
 
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