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PDLP3_ARATH
ID   PDLP3_ARATH             Reviewed;         304 AA.
AC   O22784; Q94B68;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Plasmodesmata-located protein 3;
DE            Short=PD-located protein 3 {ECO:0000303|PubMed:20886105};
DE   AltName: Full=Cysteine-rich repeat secretory protein 11 {ECO:0000303|PubMed:11402176};
DE   Flags: Precursor;
GN   Name=PDLP3 {ECO:0000303|PubMed:20886105};
GN   Synonyms=CRRSP11 {ECO:0000303|PubMed:11402176};
GN   OrderedLocusNames=At2g33330; ORFNames=F4P9.10;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   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 DEVELOPMENTAL STAGE.
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   SUBCELLULAR LOCATION, AND 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:18215111,
CC       ECO:0000269|PubMed:20886105, ECO:0000269|PubMed:25393742}. Note=Co-
CC       localizes with the Grapevine fanleaf virus (GFLV) 2B-MP at the base of
CC       tubules within modified plasmodesmata.
CC   -!- TISSUE SPECIFICITY: Highly expressed in inflorescence pedacel and shoot
CC       apex. Expressed in the outermost L1 layer of the shoot apical meristem
CC       and in the epidermis of bulging floral primordia. Within the L1,
CC       expression was restricted to the peripheral zone (at protein level).
CC       {ECO:0000269|PubMed:19704520}.
CC   -!- DEVELOPMENTAL STAGE: Expression in the epidermis of floral primordia
CC       changes through development from being weakly expressed in the youngest
CC       the floral organs, with possibly a stronger expression on the abaxial
CC       side (P1, P2 stage) to being relatively strongly expressed in both the
CC       adaxial and abaxial epidermis at later stages.
CC       {ECO:0000269|PubMed:19704520}.
CC   -!- DISRUPTION PHENOTYPE: Both pdlp2 and pdlp3, and pdlp1 and pdlp3 double
CC       mutants show altered protein diffusion (measured using GFP). In pdlp1,
CC       pdlp2 and pdlp3 triple mutant there is inhibition of GFLV 2BMP tubule
CC       formation. Virus cell-to-cell movement is negatively affected. There is
CC       a 22% reduction in mean surface area of infection foci by GFLV and an
CC       approximately 12 h delay in long distance movement in comparison to
CC       wild-type plants. There is also a systemic delay in Cauliflower mosaic
CC       virus (CaMV) spread. {ECO:0000269|PubMed:18215111,
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}.
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DR   EMBL; AC002332; AAB80651.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08816.1; -; Genomic_DNA.
DR   EMBL; AY042813; AAK68753.1; -; mRNA.
DR   EMBL; AY081690; AAM10252.1; -; mRNA.
DR   PIR; B84744; B84744.
DR   RefSeq; NP_565764.1; NM_128893.4.
DR   AlphaFoldDB; O22784; -.
DR   SMR; O22784; -.
DR   BioGRID; 3243; 6.
DR   IntAct; O22784; 5.
DR   STRING; 3702.AT2G33330.1; -.
DR   TCDB; 1.I.2.1.1; the plant plasmodesmata (ppd) family.
DR   PaxDb; O22784; -.
DR   PRIDE; O22784; -.
DR   ProteomicsDB; 224523; -.
DR   EnsemblPlants; AT2G33330.1; AT2G33330.1; AT2G33330.
DR   GeneID; 817896; -.
DR   Gramene; AT2G33330.1; AT2G33330.1; AT2G33330.
DR   KEGG; ath:AT2G33330; -.
DR   Araport; AT2G33330; -.
DR   TAIR; locus:2051089; AT2G33330.
DR   eggNOG; ENOG502QUWZ; Eukaryota.
DR   HOGENOM; CLU_000288_33_1_1; -.
DR   InParanoid; O22784; -.
DR   OMA; NDCYNCV; -.
DR   OrthoDB; 1077702at2759; -.
DR   PhylomeDB; O22784; -.
DR   PRO; PR:O22784; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O22784; baseline and differential.
DR   Genevisible; O22784; 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..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..304
FT                   /note="Plasmodesmata-located protein 3"
FT                   /id="PRO_0000296139"
FT   TOPO_DOM        27..272
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXV7"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        294..304
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXV7"
FT   DOMAIN          34..138
FT                   /note="Gnk2-homologous 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT   DOMAIN          143..242
FT                   /note="Gnk2-homologous 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT   REGION          273..293
FT                   /note="Necessary and sufficient for plasmodesmal targeting"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXV7"
FT   DISULFID        41..116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT   DISULFID        92..101
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT   DISULFID        104..129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT   DISULFID        151..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT   DISULFID        196..205
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT   DISULFID        208..233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
SQ   SEQUENCE   304 AA;  32658 MW;  795BB92F36018325 CRC64;
     MGFYSLKQLL LLYIIIMALF SDLKLAKSSS PEYTNLIYKG CARQRLSDPS GLYSQALSAM
     YGLLVTQSTK TRFYKTTTGT TSQTSVTGLF QCRGDLSNND CYNCVSRLPV LSGKLCGKTI
     AARVQLSGCY LLYEISGFAQ ISGMELLFKT CGKNNVAGTG FEQRRDTAFG VMQNGVVQGH
     GFYATTYESV YVLGQCEGDI GDSDCSGCIK NALQRAQVEC GSSISGQIYL HKCFVGYSFY
     PNGVPKRSSP YPSSGSSGSS SSSSSSGTTG KTVAIIVGGT AGVGFLVICL LFVKNLMKKK
     YDDY
 
 
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