TPLAT_ARATH
ID TPLAT_ARATH Reviewed; 1176 AA.
AC F4J8D3; Q84W49; Q9S7T0;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Protein TPLATE;
GN Name=TPLATE; Synonyms=T22; OrderedLocusNames=At3g01780;
GN ORFNames=F28J7.11, F4P13.33;
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] OF 1-1135.
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 SUBCELLULAR LOCATION.
RX PubMed=15469496; DOI=10.1111/j.1365-313x.2004.02222.x;
RA Van Damme D., Bouget F.-Y., Van Poucke K., Inze D., Geelen D.;
RT "Molecular dissection of plant cytokinesis and phragmoplast structure: a
RT survey of GFP-tagged proteins.";
RL Plant J. 40:386-398(2004).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17189342; DOI=10.1105/tpc.106.040923;
RA Van Damme D., Coutuer S., De Rycke R., Bouget F.Y., Inze D., Geelen D.;
RT "Somatic cytokinesis and pollen maturation in Arabidopsis depend on TPLATE,
RT which has domains similar to coat proteins.";
RL Plant Cell 18:3502-3518(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CLC2 AND CHC2.
RX PubMed=21187379; DOI=10.1073/pnas.1017890108;
RA Van Damme D., Gadeyne A., Vanstraelen M., Inze D., Van Montagu M.C.,
RA De Jaeger G., Russinova E., Geelen D.;
RT "Adaptin-like protein TPLATE and clathrin recruitment during plant somatic
RT cytokinesis occurs via two distinct pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:615-620(2011).
CC -!- FUNCTION: Functions in vesicle-trafficking events required for site-
CC specific cell wall modifications during pollen germination and for
CC anchoring of the cell plate to the mother wall at the correct cortical
CC position. {ECO:0000269|PubMed:17189342}.
CC -!- SUBUNIT: Interacts with CLC2 and CHC2. {ECO:0000269|PubMed:21187379}.
CC -!- INTERACTION:
CC F4J8D3; Q0WLB5: CHC2; NbExp=2; IntAct=EBI-4412119, EBI-4412194;
CC F4J8D3; O04209: CLC2; NbExp=5; IntAct=EBI-4412119, EBI-4406025;
CC F4J8D3; Q9FKM4: MUA2.4; NbExp=10; IntAct=EBI-4412119, EBI-9346324;
CC F4J8D3; F4J8D3: TPLATE; NbExp=2; IntAct=EBI-4412119, EBI-4412119;
CC F4J8D3; Q0WLS8; NbExp=6; IntAct=EBI-4412119, EBI-9346344;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:15469496, ECO:0000269|PubMed:17189342,
CC ECO:0000269|PubMed:21187379}. Note=Localized in the forming cell plate
CC and the cortical division zone (CDZ) during cytokinesis.
CC -!- TISSUE SPECIFICITY: Expressed at the pollen tube exit site in
CC germinating pollen. {ECO:0000269|PubMed:17189342}.
CC -!- DISRUPTION PHENOTYPE: Male sterility due to the production of shriveled
CC pollen unable to germinate. {ECO:0000269|PubMed:17189342}.
CC -!- SIMILARITY: Belongs to the TPLATE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF01560.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF03433.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009325; AAF01560.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC010797; AAF03433.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73713.1; -; Genomic_DNA.
DR EMBL; BT004227; AAO42242.1; -; mRNA.
DR RefSeq; NP_186827.2; NM_111044.4.
DR AlphaFoldDB; F4J8D3; -.
DR BioGRID; 6414; 29.
DR DIP; DIP-59588N; -.
DR IntAct; F4J8D3; 11.
DR STRING; 3702.AT3G01780.1; -.
DR iPTMnet; F4J8D3; -.
DR PaxDb; F4J8D3; -.
DR PRIDE; F4J8D3; -.
DR ProteomicsDB; 232440; -.
DR EnsemblPlants; AT3G01780.1; AT3G01780.1; AT3G01780.
DR GeneID; 821081; -.
DR Gramene; AT3G01780.1; AT3G01780.1; AT3G01780.
DR KEGG; ath:AT3G01780; -.
DR Araport; AT3G01780; -.
DR TAIR; locus:2082299; AT3G01780.
DR eggNOG; ENOG502QPK6; Eukaryota.
DR HOGENOM; CLU_008706_0_0_1; -.
DR InParanoid; F4J8D3; -.
DR OMA; PESRWAG; -.
DR OrthoDB; 91762at2759; -.
DR PRO; PR:F4J8D3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J8D3; baseline and differential.
DR Genevisible; F4J8D3; AT.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR GO; GO:0006897; P:endocytosis; IDA:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR037501; TPLATE.
DR PANTHER; PTHR36029; PTHR36029; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Calcium; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1176
FT /note="Protein TPLATE"
FT /id="PRO_0000413982"
FT REGION 1088..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1071..1156
FT /evidence="ECO:0000255"
FT COMPBIAS 1099..1118
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
SQ SEQUENCE 1176 AA; 130908 MW; 5D1AB2378BD3CE19 CRC64;
MDILFAQIQA DLRSNDALRQ SSALLQALQQ SAAGRDISVI AKSAVEEIVA SPASAVCKKL
AFDLIRSTRL TPDLWDTVCS GVKTDLHFPD PDVTAAAVSI LAALPAFSLP KLISDCSSEI
ASCFDSPSDN LRFSITETLG CILARDDLVT LCENNVGLLD KVSNWWARIG QNMLDKSDAV
SKVAFESVGR LFQEFDSKRM SRLAGDKLVD SENSLAIRSK WVSSMVDIVW RKRSALMARS
LVLPVETFRA TVFPLVFAVK AVASGSVEVI RQLSKASSAA AAANATVVDS NAEKLVGVSD
LVTHLAPFLA SSLDPALIFE VGINMLYLAD VAGGKPEWAS QSIIAILTLW DRQEFSSARE
SIVRAVVTNL HLLDLHMQVS LFRRLLLMVR NLRAESDRMH ALACICRTAL CVHLFARESA
RRGQKPLPGT DIISLFEDAR IKDDLNSVTS KSLFREELVA MLVESCFQLS LPLPEQKNSG
MESRVIGALA YGTGYGALNW TEPALEVVEV CRPCVKWDCD GRTYAVDCYL KLLVRLCHIY
DTRGGVKRLK DGASQDQILN ETRLQNLQRE LVKDLQEVNT PRILGRLIWT IAEHIDLEGL
DPLLADDPDD PLNIIIANIH KVLFNLDAAA TTSNRLQDVQ AVLLCAQRMG SRHARAGQLL
TKELEEYRNH AAADTVSKHQ TRLILQRIKY VSNLPERKWA GVSETRGDYP FSHHKLTVQF
YEPSAAQDRK LEGLIHKAIL ELWRPKPTEL TLFLTKGVDS TSIKVPPTAY PLTGSSDPCY
IEAYHLADTN DGRVTLHLKI INLTELELNR VDIRVGLSGA LYFMDGSPQA VRQLRNLVSQ
DPVQCSVTVG VSQFERCGFW VQVLYYPFRG ARGEYDGDYI EEDPQIMKQK RGSKAELGEP
VILRCQPYKI PLTELLLPHK ISPVEFFRLW PSLPAVAEYT GTYMYEGSGF MATAAQQYGA
SPFLSGLKSL SSKPFHRVCS HIIRTVAGFQ LCYAAKTWHG GFVGMMIFGA SEVSRNMDLG
DETTTMMCKF VVRASEASIT KQIESDIQGW CDDLTDGGVE YMPEDEVKAT AAEKLKISME
RIALLKAAQP KKTSKIEEES ENEEEEEGEE EDDDEEVKEK KEKEEGKDKE EKKKKEKEKG
TFSKLTAEET EHMALQAAVL QEWHILCKDR KYTKVN
