PDLP1_ARATH
ID PDLP1_ARATH Reviewed; 303 AA.
AC Q8GXV7; Q9FNC8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Plasmodesmata-located protein 1 {ECO:0000303|PubMed:18215111, ECO:0000303|PubMed:27078071};
DE Short=PD-located protein 1 {ECO:0000303|PubMed:20886105};
DE AltName: Full=Cysteine-rich repeat secretory protein 56 {ECO:0000303|PubMed:11402176};
DE AltName: Full=Plasmodesmata localizing protein 1 {ECO:0000303|PubMed:27078071};
DE AltName: Full=Plasmodesmata-located protein 1a;
DE Short=PDLP1a {ECO:0000303|PubMed:18215111};
DE Flags: Precursor;
GN Name=PDLP1 {ECO:0000303|PubMed:18215111};
GN Synonyms=CRRSP56 {ECO:0000303|PubMed:11402176};
GN OrderedLocusNames=At5g43980; ORFNames=MRH10.9;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 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 [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF LEU-287; VAL-288 AND LEU-289.
RC STRAIN=cv. Columbia;
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 [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH VIRAL MOVEMENT PROTEINS, AND
RP DISRUPTION PHENOTYPE.
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 [8]
RP FUNCTION, INDUCTION BY FUNGAL INFECTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=25393742; DOI=10.1371/journal.ppat.1004496;
RA Caillaud M.C., Wirthmueller L., Sklenar J., Findlay K., Piquerez S.J.,
RA Jones A.M., Robatzek S., Jones J.D., Faulkner C.;
RT "The plasmodesmal protein PDLP1 localises to haustoria-associated membranes
RT during downy mildew infection and regulates callose deposition.";
RL PLoS Pathog. 10:E1004496-E1004496(2014).
RN [9]
RP FUNCTION, INTERACTION WITH AZI1 AND PDLP5, LACK OF INTERACTION WITH DIR1,
RP AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Modulates cell-to-cell trafficking (PubMed:18215111).
CC Required for systemic acquired resistance (SAR) which is mediated by
CC the signaling molecules azelaic acid (AzA), glycerol-3-phosphate (G3P),
CC and salicylic acid (SA). Required for the proper localization and
CC stability of AZI1 which is involved in SAR (PubMed:27078071). Mediates
CC callose deposition during downy mildew fungal infection around
CC haustoria. Haustoria are unicellular protrusions from hyphae and
CC function as the site of molecular exchange of nutrients and effectors
CC between host and pathogen (PubMed:25393742).
CC {ECO:0000269|PubMed:18215111, ECO:0000269|PubMed:25393742,
CC ECO:0000269|PubMed:27078071}.
CC -!- SUBUNIT: Interacts with AZI1 (PubMed:27078071). Interacts with PDLP5
CC (PubMed:27078071). Does not interact with DIR1 (PubMed:27078071).
CC {ECO:0000269|PubMed:27078071}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Grapevine fanleaf virus
CC (GFLV) 2B-MP (PubMed:20886105). Interacts with Cauliflower mosaic virus
CC (CaMV) movement protein (PubMed:20886105).
CC {ECO:0000269|PubMed:20886105}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein {ECO:0000269|PubMed:18215111}. Cell junction, plasmodesma
CC {ECO:0000269|PubMed:18215111, ECO:0000269|PubMed:20886105,
CC ECO:0000269|PubMed:25393742, ECO:0000269|PubMed:27078071}. Note=Co-
CC localizes with the Grapevine fanleaf virus 2B-MP at the base of tubules
CC within modified plasmodesmata. Co-localizes with Cauliflower mosaic
CC virus movement protein. Utilizes the secretory pathway for delivery to
CC plasmodesmata. {ECO:0000269|PubMed:20886105}.
CC -!- TISSUE SPECIFICITY: Highly expressed in cell suspension. Expressed in
CC epidermal and spongy mesophyll cells, and the cell wall interface at
CC the base of the leaf trichome (at protein level) (PubMed:19704520,
CC PubMed:18215111). Expressed in haustoria-containing cells
CC (PubMed:25393742). {ECO:0000269|PubMed:18215111,
CC ECO:0000269|PubMed:19704520, ECO:0000269|PubMed:25393742}.
CC -!- INDUCTION: By downy mildew fungal infection.
CC {ECO:0000269|PubMed:25393742}.
CC -!- DISRUPTION PHENOTYPE: pdlp1 and pdlp3 double mutant shows altered
CC protein diffusion (measured using GFP). In pdlp1, pdlp2 and pdlp3
CC triple mutant there is inhibition of GFLV 2BMP tubule formation. Virus
CC cell-to-cell movement is negatively affected. There is a 22% reduction
CC in mean surface area of infection foci by GFLV and an approximately 12
CC h delay in long distance movement in comparison to wild-type plants.
CC There is also a systemic delay in systemic Cauliflower mosaic virus
CC (CaMV) spread. Overexpression shows a reduced-growth phenotype that
CC correlates with transgene copy number and cell-to-cell trafficking of
CC GFP, used to measure protein transport, is significantly impaired.
CC {ECO:0000269|PubMed:18215111, ECO:0000269|PubMed:20886105}.
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 (PubMed:18215111, PubMed:20886105).
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09058.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC42649.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB006703; BAB09058.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95040.1; -; Genomic_DNA.
DR EMBL; AK118016; BAC42649.1; ALT_FRAME; mRNA.
DR RefSeq; NP_199211.2; NM_123765.3.
DR AlphaFoldDB; Q8GXV7; -.
DR SMR; Q8GXV7; -.
DR BioGRID; 19671; 36.
DR STRING; 3702.AT5G43980.1; -.
DR TCDB; 1.I.2.1.1; the plant plasmodesmata (ppd) family.
DR PaxDb; Q8GXV7; -.
DR PRIDE; Q8GXV7; -.
DR ProteomicsDB; 224379; -.
DR EnsemblPlants; AT5G43980.1; AT5G43980.1; AT5G43980.
DR GeneID; 834421; -.
DR Gramene; AT5G43980.1; AT5G43980.1; AT5G43980.
DR KEGG; ath:AT5G43980; -.
DR Araport; AT5G43980; -.
DR TAIR; locus:2172492; AT5G43980.
DR eggNOG; ENOG502QWKZ; Eukaryota.
DR HOGENOM; CLU_000288_33_1_1; -.
DR InParanoid; Q8GXV7; -.
DR OMA; SADCEKC; -.
DR OrthoDB; 1077702at2759; -.
DR PhylomeDB; Q8GXV7; -.
DR PRO; PR:Q8GXV7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GXV7; baseline and differential.
DR Genevisible; Q8GXV7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IGI:TAIR.
DR GO; GO:0046739; P:transport of virus in multicellular host; IGI: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 Cell junction; Cell membrane; Disulfide bond; Host-virus interaction;
KW Membrane; Plant defense; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..303
FT /note="Plasmodesmata-located protein 1"
FT /id="PRO_0000296172"
FT TOPO_DOM 22..268
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:18215111"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18215111"
FT DOMAIN 27..136
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 141..248
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT REGION 269..289
FT /note="Necessary and sufficient for plasmodesmal targeting"
FT /evidence="ECO:0000269|PubMed:18215111"
FT DISULFID 33..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 84..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 96..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 149..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 202..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 214..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT MUTAGEN 287
FT /note="L->A: No effect on targeting to plasmodesma."
FT /evidence="ECO:0000269|PubMed:18215111"
FT MUTAGEN 288
FT /note="V->A: Retention in the endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:18215111"
FT MUTAGEN 289
FT /note="L->A: No effect on targeting to plasmodesma."
FT /evidence="ECO:0000269|PubMed:18215111"
SQ SEQUENCE 303 AA; 32607 MW; 9A550F396871C8D8 CRC64;
MKLTYQFFIF WFFLPFFAIS GDDDYKNLIF KGCANQKSPD PTGVFSQNLK NLFTSLVSQS
SQSSFASVTS GTDNTTAVIG VFQCRGDLQN AQCYDCVSKI PKLVSKLCGG GRDDGNVVAA
RVHLAGCYIR YESSGFRQTS GTEMLFRVCG KKDSNDPGFV GKRETAFGMA ENGVKTGSSG
GGGGGGGFYA GQYESVYVLG QCEGSLGNSD CGECVKDGFE KAKSECGESN SGQVYLQKCF
VSYSYYSHGV PNIEPLSGGE KRQHTERTIA LAVGGVFVLG FVIVCLLVLR SAMKKKSNKY
DAY
