PP16B_ARATH
ID PP16B_ARATH Reviewed; 147 AA.
AC Q9C8S6; Q8LDR6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=16 kDa phloem protein 2 {ECO:0000303|PubMed:29320165};
DE Short=AtPP16-2 {ECO:0000303|PubMed:29320165};
DE Short=Phloem protein 16-2 {ECO:0000303|PubMed:29320165};
GN Name=PP16-2 {ECO:0000303|PubMed:29320165};
GN OrderedLocusNames=At1g63220 {ECO:0000312|Araport:AT1G63220};
GN ORFNames=F9N12.16 {ECO:0000312|EMBL:AAG52148.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=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, 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).
RN [6]
RP STRUCTURE BY NMR OF 2-125.
RG RIKEN structural genomics initiative (RSGI);
RT "C2 domain-containing protein from putative elicitor-responsive gene.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Binds to both sense and antisense RNA (By similarity). Can
CC also bind sheared DNA and dodecamer DNA with a low affinity (By
CC similarity). Interacts with mesophyll plasmodesmata to mediate its own
CC cell-to-cell transport and potentiate RNA trafficking (By similarity).
CC May play a role in plant defense signaling (By similarity).
CC {ECO:0000250|UniProtKB:Q0JHU5, ECO:0000250|UniProtKB:Q9M2T2,
CC ECO:0000250|UniProtKB:Q9ZT47}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9C8S6-1; Sequence=Displayed;
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DR EMBL; AC022355; AAG52148.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34071.1; -; Genomic_DNA.
DR EMBL; AY054623; AAK96814.1; -; mRNA.
DR EMBL; AY081504; AAM10066.1; -; mRNA.
DR EMBL; AY085843; AAM63058.1; -; mRNA.
DR PIR; H96657; H96657.
DR RefSeq; NP_176511.1; NM_105001.4. [Q9C8S6-1]
DR PDB; 1WFJ; NMR; -; A=2-124.
DR PDBsum; 1WFJ; -.
DR AlphaFoldDB; Q9C8S6; -.
DR BMRB; Q9C8S6; -.
DR SMR; Q9C8S6; -.
DR STRING; 3702.AT1G63220.1; -.
DR PaxDb; Q9C8S6; -.
DR PRIDE; Q9C8S6; -.
DR ProteomicsDB; 242387; -. [Q9C8S6-1]
DR EnsemblPlants; AT1G63220.1; AT1G63220.1; AT1G63220. [Q9C8S6-1]
DR GeneID; 842627; -.
DR Gramene; AT1G63220.1; AT1G63220.1; AT1G63220. [Q9C8S6-1]
DR KEGG; ath:AT1G63220; -.
DR Araport; AT1G63220; -.
DR TAIR; locus:2038461; AT1G63220.
DR eggNOG; KOG1030; Eukaryota.
DR HOGENOM; CLU_109145_1_0_1; -.
DR InParanoid; Q9C8S6; -.
DR OMA; VLTCRSQ; -.
DR PhylomeDB; Q9C8S6; -.
DR EvolutionaryTrace; Q9C8S6; -.
DR PRO; PR:Q9C8S6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8S6; baseline and differential.
DR Genevisible; Q9C8S6; AT.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; Alternative splicing; Calcium; Metal-binding; Plant defense;
KW Reference proteome; RNA-binding; Transport.
FT CHAIN 1..147
FT /note="16 kDa phloem protein 2"
FT /id="PRO_0000220593"
FT DOMAIN 1..103
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 126..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT CONFLICT 126
FT /note="E -> G (in Ref. 4; AAM63058)"
FT /evidence="ECO:0000305"
FT STRAND 3..15
FT /evidence="ECO:0007829|PDB:1WFJ"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:1WFJ"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1WFJ"
FT STRAND 51..63
FT /evidence="ECO:0007829|PDB:1WFJ"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1WFJ"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1WFJ"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:1WFJ"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:1WFJ"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:1WFJ"
FT STRAND 97..108
FT /evidence="ECO:0007829|PDB:1WFJ"
FT STRAND 111..124
FT /evidence="ECO:0007829|PDB:1WFJ"
SQ SEQUENCE 147 AA; 16266 MW; 8E051C9CAE217CAB CRC64;
MPHGTLEVVL VSAKGLEDAD FLNNMDPYVQ LTCRTQDQKS NVAEGMGTTP EWNETFIFTV
SEGTTELKAK IFDKDVGTED DAVGEATIPL EPVFVEGSIP PTAYNVVKDE EYKGEIWVAL
SFKPSENRSR GMDEESYGGW KNSEASY
