PDCB1_ARATH
ID PDCB1_ARATH Reviewed; 201 AA.
AC Q9FNQ2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=PLASMODESMATA CALLOSE-BINDING PROTEIN 1;
DE Short=AtPDCB1;
DE AltName: Full=Glucan endo-1,3-beta-glucosidase-like protein 2;
DE Flags: Precursor;
GN Name=PDCB1; OrderedLocusNames=At5g61130; ORFNames=MAF19.13;
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 [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=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, NOMENCLATURE, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND GPI-ANCHOR.
RX PubMed=19223515; DOI=10.1105/tpc.108.060145;
RA Simpson C., Thomas C., Findlay K., Bayer E., Maule A.J.;
RT "An Arabidopsis GPI-anchor plasmodesmal neck protein with callose binding
RT activity and potential to regulate cell-to-cell trafficking.";
RL Plant Cell 21:581-594(2009).
CC -!- FUNCTION: Able to bind (1->3)-beta-D-glucans (laminarin). Probably
CC involved in cell-to-cell trafficking regulation.
CC {ECO:0000269|PubMed:19223515}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19223515};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:19223515}. Cell junction,
CC plasmodesma {ECO:0000269|PubMed:19223515}.
CC -!- TISSUE SPECIFICITY: Expressed in the shoot apical region and in young
CC leaves but also detected in the laminar and vasculature of mature
CC leaves. {ECO:0000269|PubMed:19223515}.
CC -!- PTM: Contains two additional disulfide bonds. {ECO:0000250}.
CC -!- MISCELLANEOUS: Overexpression of PDCB1 results in callose accumulation
CC and decreased plasmodesmal molecular diffusion.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB006696; BAB10375.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97424.1; -; Genomic_DNA.
DR EMBL; BT005195; AAO50728.1; -; mRNA.
DR EMBL; BT003876; AAO41925.1; -; mRNA.
DR RefSeq; NP_200921.2; NM_125506.5.
DR AlphaFoldDB; Q9FNQ2; -.
DR SMR; Q9FNQ2; -.
DR STRING; 3702.AT5G61130.1; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR TCDB; 1.I.2.1.1; the plant plasmodesmata (ppd) family.
DR PaxDb; Q9FNQ2; -.
DR PRIDE; Q9FNQ2; -.
DR ProteomicsDB; 236803; -.
DR EnsemblPlants; AT5G61130.1; AT5G61130.1; AT5G61130.
DR GeneID; 836234; -.
DR Gramene; AT5G61130.1; AT5G61130.1; AT5G61130.
DR KEGG; ath:AT5G61130; -.
DR Araport; AT5G61130; -.
DR TAIR; locus:2159436; AT5G61130.
DR eggNOG; ENOG502RYRZ; Eukaryota.
DR HOGENOM; CLU_031666_1_0_1; -.
DR InParanoid; Q9FNQ2; -.
DR OMA; CQYPASA; -.
DR OrthoDB; 1526042at2759; -.
DR PhylomeDB; Q9FNQ2; -.
DR PRO; PR:Q9FNQ2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNQ2; baseline and differential.
DR Genevisible; Q9FNQ2; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0001872; F:(1->3)-beta-D-glucan binding; IDA:TAIR.
DR GO; GO:0030247; F:polysaccharide binding; IDA:TAIR.
DR GO; GO:0052543; P:callose deposition in cell wall; IMP:TAIR.
DR InterPro; IPR012946; X8.
DR InterPro; IPR044788; X8_dom_prot.
DR PANTHER; PTHR31044; PTHR31044; 1.
DR Pfam; PF07983; X8; 1.
DR SMART; SM00768; X8; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..172
FT /note="PLASMODESMATA CALLOSE-BINDING PROTEIN 1"
FT /id="PRO_0000254001"
FT PROPEP 173..201
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000254002"
FT REGION 107..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 172
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..84
FT /evidence="ECO:0000250"
SQ SEQUENCE 201 AA; 20365 MW; D7DD73D40B9F0930 CRC64;
MAALVLSLLL LSLAGHSSAS WCVCKTGLSD TVLQATLDYA CGNGADCNPT KPKQSCFNPD
NVRSHCNYAV NSFFQKKGQS PGSCNFDGTA TPTNSDPSYT GCAFPTSASG SSGSTTVTPG
TTNPKGSPTT TTLPGSGTNS PYSGNPTNGV FGGNSTGGTT GTGINPDYTT DSSAFALKNS
SKLFICLLLI ASSGFCSFLM L