ID   PDCB2_ARATH             Reviewed;         194 AA.
AC   Q9SD84; Q8LBE9;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   04-NOV-2026, entry version 118.
DE   RecName: Full=PLASMODESMATA CALLOSE-BINDING PROTEIN 2;
DE            Short=AtPDCB2;
DE   AltName: Full=Glucan endo-1,3-beta-glucosidase-like protein 3;
DE   Flags: Precursor;
GN   Name=PDCB2; OrderedLocusNames=At5g08000; ORFNames=F13G24.200;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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   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   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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   GENE FAMILY, NOMENCLATURE, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, INDUCTION BY HEAT, 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).
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   -!- INDUCTION: Down-regulated by heat treatment.
CC       {ECO:0000269|PubMed:19223515}.
CC   -!- PTM: Contains two additional disulfide bonds. {ECO:0000250}.
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DR   EMBL; AL133421; CAB62612.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91233.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7051484.1; -; Genomic_DNA.
DR   EMBL; BT003716; AAO39944.1; -; mRNA.
DR   EMBL; AK118578; BAC43178.1; -; mRNA.
DR   EMBL; AY087253; AAM64809.1; -; mRNA.
DR   PIR; T45625; T45625.
DR   AlphaFoldDB; Q9SD84; -.
DR   SMR; Q9SD84; -.
DR   FunCoup; Q9SD84; 287.
DR   IntAct; Q9SD84; 1.
DR   STRING; 3702.Q9SD84; -.
DR   TCDB; 1.I.2.1.1; the plant plasmodesmata (ppd) family.
DR   GlyCosmos; Q9SD84; 2 sites, No reported glycans.
DR   GlyGen; Q9SD84; 4 sites.
DR   PaxDb; 3702-Q9SD84; -.
DR   GeneID; 830694; -.
DR   KEGG; ath:AT5G08000; -.
DR   Araport; AT5G08000; -.
DR   TAIR; AT5G08000; E13L3.
DR   eggNOG; ENOG502RYRZ; Eukaryota.
DR   HOGENOM; CLU_031666_1_0_1; -.
DR   InParanoid; Q9SD84; -.
DR   OMA; AAAQWCV; -.
DR   PhylomeDB; Q9SD84; -.
DR   PRO; PR:Q9SD84; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Proteomes; UP001984100; Chromosome 5.
DR   ExpressionAtlas; Q9SD84; baseline and differential.
DR   GO; GO:0016020; C:membrane; TAS:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; IDA: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; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IEP:UniProtKB.
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:SF137; PLASMODESMATA CALLOSE-BINDING PROTEIN 2; 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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..171
FT                   /note="PLASMODESMATA CALLOSE-BINDING PROTEIN 2"
FT                   /id="PRO_0000254003"
FT   PROPEP          172..194
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000254004"
FT   REGION          106..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..116
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           171
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        22..84
FT                   /evidence="ECO:0000250"
FT   CONFLICT        3
FT                   /note="P -> A (in Ref. 6; AAM64809)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        17
FT                   /note="T -> S (in Ref. 6; AAM64809)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143
FT                   /note="S -> T (in Ref. 6; AAM64809)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   194 AA;  19900 MW;  3C0A089C3452662A CRC64;
     MAPLVLYLLT LLMAGHTSAS WCVCKTGLSD SVLQKTLDYA CGNGADCNPT HPKGSCFNPD
     NVRAHCNYAV NSFFQKKGQA SESCNFTGTA TLTTTDPSYT GCAFPSSASG SSGSGSTTVT
     PGKNSPKGSN SITTFPGGNS PYSGTPSTGL LGGNITDATG TGLNPDYSTE SSGFALYYSN
     NLLLTGFCSL VMML
//