PDLP5_ARATH
ID PDLP5_ARATH Reviewed; 299 AA.
AC Q8GUJ2; A8WAS5; Q8LA52; Q9CAB9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Plasmodesmata-located protein 5 {ECO:0000303|PubMed:27078071};
DE Short=PD-located protein 5 {ECO:0000303|PubMed:20886105};
DE AltName: Full=Cysteine-rich repeat protein HWI1;
DE AltName: Full=Cysteine-rich repeat secretory protein 2 {ECO:0000303|PubMed:11402176};
DE AltName: Full=Plasmodesmata localizing protein 5 {ECO:0000303|PubMed:27078071};
DE AltName: Full=Protein HOPW1-1-INDUCED 1 {ECO:0000303|PubMed:18266921, ECO:0000303|PubMed:21934146};
DE Flags: Precursor;
GN Name=PDLP5 {ECO:0000303|PubMed:20886105};
GN Synonyms=CRRSP2 {ECO:0000303|PubMed:11402176}, HWI1;
GN OrderedLocusNames=At1g70690; ORFNames=F5A18.13;
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 [MRNA], AND INDUCTION BY PATHOGEN INFECTION.
RX PubMed=18266921; DOI=10.1111/j.1365-313x.2008.03439.x;
RA Lee M.W., Jelenska J., Greenberg J.T.;
RT "Arabidopsis proteins important for modulating defense responses to
RT Pseudomonas syringae that secrete HopW1-1.";
RL Plant J. 54:452-465(2008).
RN [2]
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 [3]
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 [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 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 [6]
RP GENE FAMILY ORGANIZATION, NOMENCLATURE, AND CAUTION.
RX PubMed=11402176; DOI=10.1104/pp.126.2.473;
RA Chen Z.;
RT "A superfamily of proteins with novel cysteine-rich repeats.";
RL Plant Physiol. 126:473-476(2001).
RN [7]
RP INDUCTION BY PATHOGEN INFECTION.
RX PubMed=16531493; DOI=10.1105/tpc.105.039982;
RA Bartsch M., Gobbato E., Bednarek P., Debey S., Schultze J.L., Bautor J.,
RA Parker J.E.;
RT "Salicylic acid-independent ENHANCED DISEASE SUSCEPTIBILITY1 signaling in
RT Arabidopsis immunity and cell death is regulated by the monooxygenase FMO1
RT and the Nudix hydrolase NUDT7.";
RL Plant Cell 18:1038-1051(2006).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=19704520; DOI=10.4161/psb.3.10.6020;
RA Bayer E., Thomas C., Maule A.;
RT "Symplastic domains in the Arabidopsis shoot apical meristem correlate with
RT PDLP1 expression patterns.";
RL Plant Signal. Behav. 3:853-855(2008).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=18215111; DOI=10.1371/journal.pbio.0060007;
RA Thomas C.L., Bayer E.M., Ritzenthaler C., Fernandez-Calvino L., Maule A.J.;
RT "Specific targeting of a plasmodesmal protein affecting cell-to-cell
RT communication.";
RL PLoS Biol. 6:E7-E7(2008).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GRAPEVINE FANLEAF VIRUS 2B-MP
RP PROTEIN.
RC STRAIN=cv. Columbia;
RX PubMed=20886105; DOI=10.1371/journal.ppat.1001119;
RA Amari K., Boutant E., Hofmann C., Schmitt-Keichinger C.,
RA Fernandez-Calvino L., Didier P., Lerich A., Mutterer J., Thomas C.L.,
RA Heinlein M., Mely Y., Maule A.J., Ritzenthaler C.;
RT "A family of plasmodesmal proteins with receptor-like properties for plant
RT viral movement proteins.";
RL PLoS Pathog. 6:E1001119-E1001119(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY SALICYLIC ACID, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21934146; DOI=10.1105/tpc.111.087742;
RA Lee J.Y., Wang X., Cui W., Sager R., Modla S., Czymmek K., Zybaliov B.,
RA van Wijk K., Zhang C., Lu H., Lakshmanan V.;
RT "A plasmodesmata-localized protein mediates crosstalk between cell-to-cell
RT communication and innate immunity in Arabidopsis.";
RL Plant Cell 23:3353-3373(2011).
RN [12]
RP FUNCTION, INDUCTION BY SALICYLIC ACID, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=23749844; DOI=10.1105/tpc.113.110676;
RA Wang X., Sager R., Cui W., Zhang C., Lu H., Lee J.Y.;
RT "Salicylic acid regulates Plasmodesmata closure during innate immune
RT responses in Arabidopsis.";
RL Plant Cell 25:2315-2329(2013).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PDLP1, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27078071; DOI=10.1016/j.chom.2016.03.006;
RA Lim G.H., Shine M.B., de Lorenzo L., Yu K., Cui W., Navarre D., Hunt A.G.,
RA Lee J.Y., Kachroo A., Kachroo P.;
RT "Plasmodesmata localizing proteins regulate transport and signaling during
RT systemic acquired immunity in plants.";
RL Cell Host Microbe 19:541-549(2016).
RN [14]
RP CRYSTALLIZATION OF 26-241, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBUNIT.
RX PubMed=28876233; DOI=10.1107/s2053230x1701250x;
RA Wang X., Zhu P., Qu S., Zhao J., Singh P.K., Wang W.;
RT "Ectodomain of plasmodesmata-localized protein 5 in Arabidopsis:
RT expression, purification, crystallization and crystallographic analysis.";
RL Acta Crystallogr. F Struct. Biol. Commun. 73:532-535(2017).
CC -!- FUNCTION: Modulates cell-to-cell trafficking. Has a positive role in
CC innate immunity. Required for systemic acquired resistance (SAR) which
CC is mediated by the signaling molecules azelaic acid (AzA), glycerol-3-
CC phosphate (G3P), and salicylic acid (SA) (PubMed:27078071). Negative
CC regulator of plasmodesmata permeability triggered by SA during immune
CC responses, through regulation of callose deposition (PubMed:21934146,
CC PubMed:23749844). Delays the trafficking of Tobacco Mosaic Virus (TMV)
CC movement protein (MP). Required for symplastic signal transport
CC (PubMed:27078071). {ECO:0000269|PubMed:21934146,
CC ECO:0000269|PubMed:23749844, ECO:0000269|PubMed:27078071}.
CC -!- SUBUNIT: Monomer (PubMed:28876233). Interacts with PDLP1
CC (PubMed:27078071). {ECO:0000269|PubMed:27078071,
CC ECO:0000269|PubMed:28876233}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Grapevine fanleaf virus
CC (GFLV) 2B-MP. {ECO:0000305|PubMed:20886105}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein {ECO:0000250|UniProtKB:Q8GXV7}. Cell junction, plasmodesma
CC {ECO:0000269|PubMed:18215111, ECO:0000269|PubMed:20886105,
CC ECO:0000269|PubMed:21934146}. Note=Located in cell wall junctions
CC between leaf epidermal and mesophyl cells. Located to the central
CC region of plasmodesmata. Co-localizes with the Grapevine fanleaf virus
CC (GFLV) 2B-MP at the base of tubules within modified plasmodesmata.
CC -!- TISSUE SPECIFICITY: Highly expressed in inflorescence nodes and rosette
CC senescent leaves. Mostly expressed in cell wall junctions between leaf
CC epidermal and mesophyl cells, and to a lesser extent at the cross walls
CC between epidermal or cortex cells within the hypocotyl (at protein
CC level). Low vascular expression in seedling and mature leaf, but high
CC expression in senescing leaves (at protein level).
CC {ECO:0000269|PubMed:19704520, ECO:0000269|PubMed:21934146}.
CC -!- INDUCTION: By the Pseudomonas syringae pv. maculicola effector HopW1-1
CC (PubMed:18266921, PubMed:16531493). By salicylic acid (PubMed:21934146,
CC PubMed:23749844). {ECO:0000269|PubMed:16531493,
CC ECO:0000269|PubMed:18266921, ECO:0000269|PubMed:21934146,
CC ECO:0000269|PubMed:23749844}.
CC -!- DISRUPTION PHENOTYPE: No growth defects (PubMed:21934146). Two-fold
CC lower callose accumulation in plasmodesmata than wild type
CC (PubMed:21934146). More susceptible to infection by the plant pathogen
CC Pseudomonas syringae pv. maculicola (PubMed:21934146). Level of
CC salicylic acid (SA) is comparable to wild type but plasmodesmata
CC closure is impaired (PubMed:21934146, PubMed:23749844). However,
CC overexpression leads to growth inhibition and chlorosis in seedling
CC stage, with levels of SA fifteen-fold higher than wild type including
CC all forms of SA, and probably triggering cell death (PubMed:23749844).
CC Ectopic expression affects trafficking of MP from TMV, and shows four-
CC fold accumulation of callose in plasmodesmata than wild type
CC (PubMed:21934146). Compromised systemic acquired resistance (SAR)
CC (PubMed:27078071). {ECO:0000269|PubMed:21934146,
CC ECO:0000269|PubMed:23749844, ECO:0000269|PubMed:27078071}.
CC -!- SIMILARITY: Belongs to the cysteine-rich repeat secretory protein
CC family. Plasmodesmata-located proteins (PDLD) subfamily. {ECO:0000305}.
CC -!- CAUTION: PDLPs were initially named Cysteine-rich secretory proteins
CC based on a classification work that failed to predict the transmembrane
CC region at the C-terminus (PubMed:11402176). However, it was later shown
CC that PDLPs are membrane proteins. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52335.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EU214911; ABW84227.1; -; mRNA.
DR EMBL; AC011663; AAG52335.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35100.1; -; Genomic_DNA.
DR EMBL; BT002470; AAO00830.1; -; mRNA.
DR EMBL; BT006325; AAP13433.1; -; mRNA.
DR EMBL; AY088027; AAM65573.1; -; mRNA.
DR PIR; C96731; C96731.
DR RefSeq; NP_564997.1; NM_105737.4.
DR PDB; 6GRE; X-ray; 1.29 A; A/B=26-241.
DR PDBsum; 6GRE; -.
DR AlphaFoldDB; Q8GUJ2; -.
DR SMR; Q8GUJ2; -.
DR BioGRID; 28626; 1.
DR STRING; 3702.AT1G70690.1; -.
DR TCDB; 1.I.2.1.1; the plant plasmodesmata (ppd) family.
DR PaxDb; Q8GUJ2; -.
DR PRIDE; Q8GUJ2; -.
DR ProteomicsDB; 224524; -.
DR EnsemblPlants; AT1G70690.1; AT1G70690.1; AT1G70690.
DR GeneID; 843406; -.
DR Gramene; AT1G70690.1; AT1G70690.1; AT1G70690.
DR KEGG; ath:AT1G70690; -.
DR Araport; AT1G70690; -.
DR TAIR; locus:2033614; AT1G70690.
DR eggNOG; ENOG502QWR4; Eukaryota.
DR HOGENOM; CLU_000288_33_0_1; -.
DR InParanoid; Q8GUJ2; -.
DR OMA; ANCSQAR; -.
DR OrthoDB; 1279011at2759; -.
DR PhylomeDB; Q8GUJ2; -.
DR PRO; PR:Q8GUJ2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GUJ2; baseline and differential.
DR Genevisible; Q8GUJ2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
DR GO; GO:0051707; P:response to other organism; IEP:TAIR.
DR Gene3D; 3.30.430.20; -; 2.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
DR Pfam; PF01657; Stress-antifung; 2.
DR PROSITE; PS51473; GNK2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Disulfide bond;
KW Host-virus interaction; Membrane; Plant defense; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..299
FT /note="Plasmodesmata-located protein 5"
FT /id="PRO_0000296130"
FT TOPO_DOM 26..264
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV7"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV7"
FT DOMAIN 29..135
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 137..237
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT REGION 265..285
FT /note="Necessary and sufficient for plasmodesmal targeting"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV7"
FT DISULFID 36..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 89..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 101..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 148..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 191..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 203..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT CONFLICT 77
FT /note="P -> S (in Ref. 5; AAM65573)"
FT /evidence="ECO:0000305"
FT CONFLICT 271..272
FT /note="IV -> MI (in Ref. 5; AAM65573)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="L -> F (in Ref. 5; AAM65573)"
FT /evidence="ECO:0000305"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:6GRE"
FT HELIX 46..61
FT /evidence="ECO:0007829|PDB:6GRE"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:6GRE"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:6GRE"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:6GRE"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:6GRE"
FT HELIX 95..113
FT /evidence="ECO:0007829|PDB:6GRE"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:6GRE"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:6GRE"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:6GRE"
FT HELIX 157..172
FT /evidence="ECO:0007829|PDB:6GRE"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:6GRE"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:6GRE"
FT HELIX 197..215
FT /evidence="ECO:0007829|PDB:6GRE"
FT STRAND 221..234
FT /evidence="ECO:0007829|PDB:6GRE"
SQ SEQUENCE 299 AA; 31804 MW; DA126B3BE4EC82BB CRC64;
MIKTKTTSLL CFLLTAVILM NPSSSSPTDN YIYAVCSPAK FSPSSGYETN LNSLLSSFVT
STAQTRYANF TVPTGKPEPT VTVYGIYQCR GDLDPTACST CVSSAVAQVG ALCSNSYSGF
LQMENCLIRY DNKSFLGVQD KTLILNKCGQ PMEFNDQDAL TKASDVIGSL GTGDGSYRTG
GNGNVQGVAQ CSGDLSTSQC QDCLSDAIGR LKSDCGMAQG GYVYLSKCYA RFSVGGSHAR
QTPGPNFGHE GEKGNKDDNG VGKTLAIIIG IVTLIILLVV FLAFVGKCCR KLQDEKWCK
