ID   DIR10_ARATH             Reviewed;         447 AA.
AC   Q9SIA8; F4IIT2;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Dirigent protein 10;
DE            Short=AtDIR10;
DE   AltName: Full=Protein ENHANCED SUBERIN 1;
DE   Flags: Precursor;
GN   Name=DIR10; Synonyms=ESB1; OrderedLocusNames=At2g28670; ORFNames=T8O18.4;
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   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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17590394; DOI=10.1016/j.phytochem.2007.04.042;
RA   Ralph S.G., Jancsik S., Bohlmann J.;
RT   "Dirigent proteins in conifer defense II: Extended gene discovery,
RT   phylogeny, and constitutive and stress-induced gene expression in spruce
RT   (Picea spp.).";
RL   Phytochemistry 68:1975-1991(2007).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=19461889; DOI=10.1371/journal.pgen.1000492;
RA   Baxter I., Hosmani P.S., Rus A., Lahner B., Borevitz J.O., Muthukumar B.,
RA   Mickelbart M.V., Schreiber L., Franke R.B., Salt D.E.;
RT   "Root suberin forms an extracellular barrier that affects water relations
RT   and mineral nutrition in Arabidopsis.";
RL   PLoS Genet. 5:E1000492-E1000492(2009).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=21421706; DOI=10.1093/jxb/erq389;
RA   Ranathunge K., Schreiber L.;
RT   "Water and solute permeabilities of Arabidopsis roots in relation to the
RT   amount and composition of aliphatic suberin.";
RL   J. Exp. Bot. 62:1961-1974(2011).
RN   [8]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=22854967; DOI=10.1074/jbc.m112.387423;
RA   Kim K.-W., Moinuddin S.G.A., Atwell K.M., Costa M.A., Davin L.B.,
RA   Lewis N.G.;
RT   "Opposite stereoselectivities of dirigent proteins in Arabidopsis and
RT   schizandra species.";
RL   J. Biol. Chem. 287:33957-33972(2012).
CC   -!- FUNCTION: Dirigent proteins impart stereoselectivity on the phenoxy
CC       radical-coupling reaction, yielding optically active lignans from two
CC       molecules of coniferyl alcohol in the biosynthesis of lignans,
CC       flavonolignans, and alkaloids and thus plays a central role in plant
CC       secondary metabolism (By similarity). Regulates suberin accumulation in
CC       roots. {ECO:0000250, ECO:0000269|PubMed:19461889,
CC       ECO:0000269|PubMed:21421706}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9SIA8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9SIA8-2; Sequence=VSP_047338;
CC   -!- TISSUE SPECIFICITY: In roots, mostly detected in root endodermis and
CC       quiescent center, and, to a lower extent, in root stele and cortex.
CC       Expressed in root vascular cylinder, flowers, siliques, cotyledon and
CC       leaf veins, and leaf margins. Present in the basal region of rosette
CC       leaf trichomes and in developing xylem. {ECO:0000269|PubMed:22854967}.
CC   -!- DEVELOPMENTAL STAGE: In flowers, localized to vasculature of the stamen
CC       filament, in anthers and papillar cells of the stigma. In siliques,
CC       mostly expressed in the abscission zone. {ECO:0000269|PubMed:22854967}.
CC   -!- DISRUPTION PHENOTYPE: Increased root suberin accumulation characterized
CC       by an increased aliphatic monomer content in suberin. Reduced day time
CC       transpiration rates and increased water-use efficiency during the
CC       vegetative growth period. Decreases in the accumulation of Ca, Mn, and
CC       Zn and increases in the accumulation of Na, S, K, As, Se, and Mo in the
CC       shoot. {ECO:0000269|PubMed:19461889, ECO:0000269|PubMed:21421706}.
CC   -!- SIMILARITY: Belongs to the plant dirigent protein family.
CC       {ECO:0000305}.
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DR   EMBL; AC007171; AAD24368.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08158.1; -; Genomic_DNA.
DR   EMBL; BT002889; AAO22706.1; -; mRNA.
DR   EMBL; BT015768; AAU90058.1; -; mRNA.
DR   PIR; G84687; G84687.
DR   RefSeq; NP_001154539.1; NM_001161067.1. [Q9SIA8-2]
DR   AlphaFoldDB; Q9SIA8; -.
DR   SMR; Q9SIA8; -.
DR   STRING; 3702.AT2G28670.1; -.
DR   PaxDb; Q9SIA8; -.
DR   EnsemblPlants; AT2G28670.1; AT2G28670.1; AT2G28670.
DR   EnsemblPlants; AT2G28670.2; AT2G28670.2; AT2G28670. [Q9SIA8-2]
DR   GeneID; 817416; -.
DR   Gramene; AT2G28670.1; AT2G28670.1; AT2G28670.
DR   Gramene; AT2G28670.2; AT2G28670.2; AT2G28670. [Q9SIA8-2]
DR   KEGG; ath:AT2G28670; -.
DR   Araport; AT2G28670; -.
DR   TAIR; locus:2065521; AT2G28670.
DR   HOGENOM; CLU_059816_0_0_1; -.
DR   InParanoid; Q9SIA8; -.
DR   OMA; FTVYITY; -.
DR   PhylomeDB; Q9SIA8; -.
DR   PRO; PR:Q9SIA8; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SIA8; baseline and differential.
DR   Genevisible; Q9SIA8; AT.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0048226; C:Casparian strip; IDA:TAIR.
DR   GO; GO:0009809; P:lignin biosynthetic process; IMP:TAIR.
DR   GO; GO:0010345; P:suberin biosynthetic process; IMP:TAIR.
DR   Gene3D; 2.40.480.10; -; 1.
DR   InterPro; IPR044859; Allene_oxi_cyc_Dirigent.
DR   InterPro; IPR004265; Dirigent.
DR   PANTHER; PTHR46215; PTHR46215; 2.
DR   Pfam; PF03018; Dirigent; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Apoplast; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..447
FT                   /note="Dirigent protein 10"
FT                   /id="PRO_0000422841"
FT   REGION          74..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..221
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047338"
SQ   SEQUENCE   447 AA;  41507 MW;  467647CD2785A489 CRC64;
     MAGQKILSLL VIALVVTFAA AARLLDEENA FSATTTTLGS GSGSTGIGFG AGTGSSGSGS
     TGFGFGAGSG SSGSGSTGSG LGAGTGSIPS SGSGPGLLPT ASSVPGSLAG GGSGSLPTTG
     SATGAGAGTG SALGGGPGAG SALGGGAGAG PALGGGAGAG PALGGGAGAG SALGGGGAGA
     GPALGGGGAG AGPALGGGVA GSGSALGGGA SAGPDNTLVF FMHDILGGSN PTARAVTGVV
     ANPALSGQLP FAKPNGANLP VSNGVPSNNN NNGIVNNNNV PFLVGLGGTT ANILQNNNNG
     NNILNGFPVA SGGQLPSGSA LQMLMFGTMT VIDDELTEGH ELGSGLLGKA QGYYVASAID
     GTSQTMAFTA MFESGGYEDS ISFFGVLRTA VSESHIGVMG GTGKYVNARG FAILKTFTGS
     SGTQQNQPHQ FTDGLETVVE CTVYLSY