PDLP2_ARATH
ID PDLP2_ARATH Reviewed; 307 AA.
AC Q6NM73; P93806; P93807;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Plasmodesmata-located protein 2;
DE Short=PD-located protein 2 {ECO:0000303|PubMed:20886105};
DE AltName: Full=Cysteine-rich repeat secretory protein 3 {ECO:0000303|PubMed:11402176};
DE Flags: Precursor;
GN Name=PDLP2 {ECO:0000303|PubMed:20886105};
GN Synonyms=CRRSP3 {ECO:0000303|PubMed:11402176}; OrderedLocusNames=At1g04520;
GN ORFNames=F19P19.1;
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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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, AND DISRUPTION PHENOTYPE.
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 DISRUPTION PHENOTYPE.
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 GRAPEVINE FANLEAF VIRUS 2B-MP
RP PROTEIN, AND 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 SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Modulates cell-to-cell trafficking.
CC {ECO:0000250|UniProtKB:Q8GXV7}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Grapevine fanleaf virus
CC (GFLV) 2B-MP. {ECO:0000305|PubMed:20886105}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8GXV7};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8GXV7}.
CC Cell junction, plasmodesma {ECO:0000269|PubMed:20886105,
CC ECO:0000269|PubMed:25393742}. Note=Co-localizes with the Grapevine
CC fanleaf virus (GFLV) 2B-MP at the base of tubules within modified
CC plasmodesmata. {ECO:0000269|PubMed:20886105}.
CC -!- TISSUE SPECIFICITY: Highly expressed in inflorescence shoot apex.
CC Uniformly expressed within the inflorescence meristem with the
CC exception of a boundary zone between floral primordia and the meristem
CC where the expression is weaker (at protein level).
CC {ECO:0000269|PubMed:19704520}.
CC -!- DISRUPTION PHENOTYPE: Grows normally showing no detectable
CC abnormalities in leaf or flower development under short or long day
CC growth conditions. The pdlp2 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 Cauliflower mosaic virus (CaMV)
CC spread. {ECO:0000269|PubMed:18215111, ECO:0000269|PubMed:19704520,
CC 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. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70422.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC000104; AAB70422.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27709.1; -; Genomic_DNA.
DR EMBL; BT010866; AAR24233.1; -; mRNA.
DR EMBL; BT011789; AAS68113.1; -; mRNA.
DR PIR; F86177; F86177.
DR RefSeq; NP_171946.2; NM_100331.4.
DR AlphaFoldDB; Q6NM73; -.
DR SMR; Q6NM73; -.
DR STRING; 3702.AT1G04520.1; -.
DR TCDB; 1.I.2.1.1; the plant plasmodesmata (ppd) family.
DR PaxDb; Q6NM73; -.
DR PRIDE; Q6NM73; -.
DR ProteomicsDB; 220315; -.
DR EnsemblPlants; AT1G04520.1; AT1G04520.1; AT1G04520.
DR GeneID; 839502; -.
DR Gramene; AT1G04520.1; AT1G04520.1; AT1G04520.
DR KEGG; ath:AT1G04520; -.
DR Araport; AT1G04520; -.
DR TAIR; locus:2018314; AT1G04520.
DR eggNOG; ENOG502QUWZ; Eukaryota.
DR HOGENOM; CLU_000288_33_1_1; -.
DR InParanoid; Q6NM73; -.
DR OMA; LFKTCGT; -.
DR OrthoDB; 1077702at2759; -.
DR PhylomeDB; Q6NM73; -.
DR PRO; PR:Q6NM73; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NM73; baseline and differential.
DR Genevisible; Q6NM73; 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: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; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..307
FT /note="Plasmodesmata-located protein 2"
FT /id="PRO_0000296131"
FT TOPO_DOM 24..275
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV7"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV7"
FT DOMAIN 33..136
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 141..240
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT REGION 246..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..296
FT /note="Necessary and sufficient for plasmodesmal targeting"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV7"
FT DISULFID 40..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 90..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 102..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 149..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 194..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 206..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
SQ SEQUENCE 307 AA; 32764 MW; BC3482B696663E33 CRC64;
MGLSISFLSI IMMMCLLFPD LNVVVKSATT EYTTLIYKGC ARQQFSDPSG LYSQALSAMF
GSLVSQSTKT RFYKTTTGTS TTTITGLFQC RGDLSNHDCY NCVSRLPVLS DKLCGKTIAS
RVQLSGCYLL YEVSGFSQIS GMEMLFKTCG KNNIAGTGFE ERRDTAFGVM QNGVVSGHGF
YATTYESVYV LGQCEGDVGD TDCSGCVKNA LEKAQVECGS SISGQIYLHK CFIAYSYYPN
GVPRRSSSSS SSSSSSSSGS SNSDPSTSTG ATGKTVAIIV GGAAGVGFLV ICLLFAKNLM
RKKHDDY
