PP16A_ARATH
ID PP16A_ARATH Reviewed; 156 AA.
AC Q9M2T2; A0A178VK75;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=16 kDa phloem protein 1 {ECO:0000303|PubMed:29320165};
DE Short=AtPP16-1 {ECO:0000303|PubMed:29320165};
DE Short=Phloem protein 16-1 {ECO:0000303|PubMed:29320165};
DE AltName: Full=Elicitor-responsive protein FIERG2 {ECO:0000303|PubMed:15282545};
GN Name=PP16-1 {ECO:0000303|PubMed:29320165};
GN Synonyms=FIERG2 {ECO:0000303|PubMed:15282545};
GN OrderedLocusNames=At3g55470 {ECO:0000312|Araport:AT3G55470};
GN ORFNames=T22E16.130 {ECO:0000312|EMBL:CAB75905.1};
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;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP REGULATION BY ARR2.
RX PubMed=15282545; DOI=10.1038/sj.emboj.7600337;
RA Hass C., Lohrmann J., Albrecht V., Sweere U., Hummel F., Yoo S.D.,
RA Hwang I., Zhu T., Schaefer E., Kudla J., Harter K.;
RT "The response regulator 2 mediates ethylene signalling and hormone signal
RT integration in Arabidopsis.";
RL EMBO J. 23:3290-3302(2004).
RN [6]
RP STRUCTURE BY NMR, FUNCTION, AND NOMENCLATURE.
RX PubMed=29320165; DOI=10.1021/acs.biochem.7b01071;
RA Sashi P., Singarapu K.K., Bhuyan A.K.;
RT "Solution NMR structure and backbone dynamics of partially disordered
RT Arabidopsis thaliana phloem protein 16-1, a putative mRNA transporter.";
RL Biochemistry 57:912-924(2018).
CC -!- FUNCTION: Binds to both sense and antisense RNA (PubMed:29320165). Can
CC also bind sheared DNA and dodecamer DNA with a low affinity
CC (PubMed:29320165). Interacts with mesophyll plasmodesmata to mediate
CC its own cell-to-cell transport and potentiate RNA trafficking (By
CC similarity). May play a role in plant defense signaling (By
CC similarity). {ECO:0000250|UniProtKB:Q0JHU5,
CC ECO:0000250|UniProtKB:Q9ZT47, ECO:0000269|PubMed:29320165}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- INDUCTION: Regulated by ARR2. {ECO:0000269|PubMed:15282545}.
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DR EMBL; AL132975; CAB75905.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79388.1; -; Genomic_DNA.
DR EMBL; AK117139; BAC41817.1; -; mRNA.
DR EMBL; BT025730; ABF83620.1; -; mRNA.
DR PIR; T47686; T47686.
DR RefSeq; NP_191107.1; NM_115405.4.
DR PDB; 5YQ3; NMR; -; A=1-156.
DR PDBsum; 5YQ3; -.
DR AlphaFoldDB; Q9M2T2; -.
DR SMR; Q9M2T2; -.
DR STRING; 3702.AT3G55470.1; -.
DR PaxDb; Q9M2T2; -.
DR PRIDE; Q9M2T2; -.
DR ProteomicsDB; 189931; -.
DR EnsemblPlants; AT3G55470.1; AT3G55470.1; AT3G55470.
DR GeneID; 824713; -.
DR Gramene; AT3G55470.1; AT3G55470.1; AT3G55470.
DR KEGG; ath:AT3G55470; -.
DR Araport; AT3G55470; -.
DR TAIR; locus:2099946; AT3G55470.
DR eggNOG; KOG1030; Eukaryota.
DR InParanoid; Q9M2T2; -.
DR OrthoDB; 1430387at2759; -.
DR PhylomeDB; Q9M2T2; -.
DR PRO; PR:Q9M2T2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2T2; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR Pfam; PF00168; C2; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Metal-binding; Plant defense; Reference proteome;
KW RNA-binding; Transport.
FT CHAIN 1..156
FT /note="16 kDa phloem protein 1"
FT /id="PRO_0000447256"
FT DOMAIN 1..108
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:5YQ3"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:5YQ3"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5YQ3"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:5YQ3"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5YQ3"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:5YQ3"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:5YQ3"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5YQ3"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:5YQ3"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:5YQ3"
SQ SEQUENCE 156 AA; 17317 MW; CC7FAF03D600639B CRC64;
MAVGILEVSL ISGKGLKRSD FLGKIDPYVE IQYKGQTRKS SVAKEDGGRN PTWNDKLKWR
AEFPGSGADY KLIVKVMDHD TFSSDDFIGE ATVHVKELLE MGVEKGTAEL RPTKYNIVDS
DLSFVGELLI GVSYSLLQDR GMDGEQFGGW KHSQVD
