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   02-SEP-2026, entry version 121.
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
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   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.
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DR   EMBL; AB006696; BAB10375.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97424.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7057322.1; -; 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   FunCoup; Q9FNQ2; 611.
DR   STRING; 3702.Q9FNQ2; -.
DR   TCDB; 1.I.2.1.1; the plant plasmodesmata (ppd) family.
DR   GlyCosmos; Q9FNQ2; 2 sites, No reported glycans.
DR   GlyGen; Q9FNQ2; 3 sites.
DR   PaxDb; 3702-Q9FNQ2; -.
DR   ProteomicsDB; 236803; -.
DR   GeneID; 836234; -.
DR   KEGG; ath:AT5G61130; -.
DR   Araport; AT5G61130; -.
DR   TAIR; AT5G61130; PDCB1.
DR   eggNOG; ENOG502RYRZ; Eukaryota.
DR   HOGENOM; CLU_031666_1_0_1; -.
DR   InParanoid; Q9FNQ2; -.
DR   OMA; KQSCFNP; -.
DR   OrthoDB; 1930814at2759; -.
DR   PhylomeDB; Q9FNQ2; -.
DR   PRO; PR:Q9FNQ2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FNQ2; baseline and differential.
DR   GO; GO:0016020; C:membrane; TAS:TAIR.
DR   GO; GO:0005634; C:nucleus; ISM:TAIR.
DR   GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; 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   FunFam; 1.20.58.1040:FF:000001; Glucan endo-1,3-beta-glucosidase 4; 1.
DR   Gene3D; 1.20.58.1040; -; 1.
DR   InterPro; IPR012946; X8.
DR   InterPro; IPR044788; X8_dom_prot.
DR   PANTHER; PTHR31044; BETA-1,3 GLUCANASE; 1.
DR   PANTHER; PTHR31044:SF61; PLASMODESMATA CALLOSE-BINDING PROTEIN 1; 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   COMPBIAS        107..141
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..161
FT                   /note="Gly residues"
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
//