THA8L_ARATH
ID THA8L_ARATH Reviewed; 257 AA.
AC Q9STF9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Protein THYLAKOID ASSEMBLY 8-like, chloroplastic {ECO:0000303|PubMed:24047899};
DE Short=AtTHA8L {ECO:0000303|PubMed:24047899};
DE Flags: Precursor;
GN Name=THA8L {ECO:0000303|PubMed:24047899};
GN OrderedLocusNames=At3g46870 {ECO:0000312|Araport:AT3G46870};
GN ORFNames=T6H20.100 {ECO:0000312|EMBL:CAB51178.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
RP GENE FAMILY.
RX PubMed=15269332; DOI=10.1105/tpc.104.022236;
RA Lurin C., Andres C., Aubourg S., Bellaoui M., Bitton F., Bruyere C.,
RA Caboche M., Debast C., Gualberto J., Hoffmann B., Lecharny A., Le Ret M.,
RA Martin-Magniette M.-L., Mireau H., Peeters N., Renou J.-P., Szurek B.,
RA Taconnat L., Small I.;
RT "Genome-wide analysis of Arabidopsis pentatricopeptide repeat proteins
RT reveals their essential role in organelle biogenesis.";
RL Plant Cell 16:2089-2103(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION, AND MUTAGENESIS OF
RP LYS-75; ARG-86; LYS-93; LYS-96; ARG-104; ARG-119; LYS-155; LYS-157;
RP ARG-158; ARG-186; ARG-190; LYS-206; ARG-217 AND LYS-221.
RX PubMed=24047899; DOI=10.1074/jbc.m113.496828;
RA Ban T., Ke J., Chen R., Gu X., Tan M.H.E., Zhou X.E., Kang Y., Melcher K.,
RA Zhu J.-K., Xu H.E.;
RT "Structure of a PLS-class pentatricopeptide repeat protein provides
RT insights into mechanism of RNA recognition.";
RL J. Biol. Chem. 288:31540-31548(2013).
CC -!- FUNCTION: Binds weakly to specific single strand RNA (ssRNA).
CC {ECO:0000269|PubMed:24047899}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the PPR family. P subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Pentatricopeptide repeat proteins;
CC URL="https://ppr.plantenergy.uwa.edu.au";
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DR EMBL; AL096859; CAB51178.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78213.1; -; Genomic_DNA.
DR EMBL; AK117833; BAC42475.1; -; mRNA.
DR EMBL; BT005267; AAO63331.1; -; mRNA.
DR PIR; T12961; T12961.
DR RefSeq; NP_190271.1; NM_114554.4.
DR PDB; 4LEU; X-ray; 2.00 A; A=1-257.
DR PDBsum; 4LEU; -.
DR AlphaFoldDB; Q9STF9; -.
DR SMR; Q9STF9; -.
DR DIP; DIP-60556N; -.
DR STRING; 3702.AT3G46870.1; -.
DR PaxDb; Q9STF9; -.
DR PRIDE; Q9STF9; -.
DR EnsemblPlants; AT3G46870.1; AT3G46870.1; AT3G46870.
DR GeneID; 823840; -.
DR Gramene; AT3G46870.1; AT3G46870.1; AT3G46870.
DR KEGG; ath:AT3G46870; -.
DR Araport; AT3G46870; -.
DR TAIR; locus:2102832; AT3G46870.
DR eggNOG; ENOG502QPMB; Eukaryota.
DR HOGENOM; CLU_077248_1_0_1; -.
DR InParanoid; Q9STF9; -.
DR PhylomeDB; Q9STF9; -.
DR PRO; PR:Q9STF9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9STF9; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR044795; THA8L-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR46870; PTHR46870; 1.
DR Pfam; PF13041; PPR_2; 1.
DR TIGRFAMs; TIGR00756; PPR; 2.
DR PROSITE; PS51375; PPR; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Plastid; Reference proteome; Repeat;
KW RNA-binding; Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..257
FT /note="Protein THYLAKOID ASSEMBLY 8-like, chloroplastic"
FT /id="PRO_0000356125"
FT REPEAT 142..176
FT /note="PPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 177..211
FT /note="PPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT MUTAGEN 75
FT /note="K->E: Abolished RNA binding."
FT /evidence="ECO:0000269|PubMed:24047899"
FT MUTAGEN 86
FT /note="R->E: Reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:24047899"
FT MUTAGEN 93
FT /note="K->E: Reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:24047899"
FT MUTAGEN 96
FT /note="K->E: Reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:24047899"
FT MUTAGEN 104
FT /note="R->E: Abolished RNA binding."
FT /evidence="ECO:0000269|PubMed:24047899"
FT MUTAGEN 119
FT /note="R->E: Abolished RNA binding."
FT /evidence="ECO:0000269|PubMed:24047899"
FT MUTAGEN 155
FT /note="K->E: Abolished RNA binding."
FT /evidence="ECO:0000269|PubMed:24047899"
FT MUTAGEN 157
FT /note="K->E: Reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:24047899"
FT MUTAGEN 158
FT /note="R->E: Reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:24047899"
FT MUTAGEN 186
FT /note="R->E: Reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:24047899"
FT MUTAGEN 190
FT /note="R->E: Reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:24047899"
FT MUTAGEN 206
FT /note="K->E: Reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:24047899"
FT MUTAGEN 217
FT /note="R->E: Reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:24047899"
FT MUTAGEN 221
FT /note="K->E: Reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:24047899"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:4LEU"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:4LEU"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:4LEU"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:4LEU"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:4LEU"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:4LEU"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:4LEU"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:4LEU"
FT HELIX 194..205
FT /evidence="ECO:0007829|PDB:4LEU"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4LEU"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:4LEU"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:4LEU"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:4LEU"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:4LEU"
SQ SEQUENCE 257 AA; 30133 MW; C6D3D8189362F7F7 CRC64;
MTAIRVCSRK FPTFASIFFQ NITRNPSIHR ISFSNLKPKT LLHPIPPKPF TVFVSRFHDG
RPRGPLWRGK KLIGKEALFV ILGLKRLKED DEKLDKFIKT HVFRLLKLDM LAVIGELERQ
EETALAIKMF EVIQKQEWYQ PDVFMYKDLI VSLAKSKRMD EAMALWEKMK KENLFPDSQT
YTEVIRGFLR DGCPADAMNV YEDMLKSPDP PEELPFRVLL KGLLPHPLLR NKVKKDFEEL
FPEKHAYDPP EEIFGRC
