DIR6_ARATH
ID DIR6_ARATH Reviewed; 187 AA.
AC Q9SUQ8;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Dirigent protein 6;
DE Short=AtDIR6;
DE Flags: Precursor;
GN Name=DIR6; OrderedLocusNames=At4g23690; ORFNames=F9D16.160;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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].
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 [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, GLYCOSYLATION, SIGNAL SEQUENCE CLEAVAGE SITE, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=19946920; DOI=10.1002/anie.200904622;
RA Pickel B., Constantin M.A., Pfannstiel J., Conrad J., Beifuss U.,
RA Schaller A.;
RT "An enantiocomplementary dirigent protein for the enantioselective laccase-
RT catalyzed oxidative coupling of phenols.";
RL Angew. Chem. Int. Ed. Engl. 49:202-204(2010).
RN [7]
RP SUBUNIT, GLYCOSYLATION AT ASN-59 AND ASN-123, DISULFIDE BOND, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22443713; DOI=10.1111/j.1742-4658.2012.08580.x;
RA Pickel B., Pfannstiel J., Steudle A., Lehmann A., Gerken U., Pleiss J.,
RA Schaller A.;
RT "A model of dirigent proteins derived from structural and functional
RT similarities with allene oxide cyclase and lipocalins.";
RL FEBS J. 279:1980-1993(2012).
RN [8]
RP FUNCTION, 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. Enantiocomplementary dirigent protein that
CC mediates the laccase-catalyzed enantioselective oxidative phenol
CC coupling of (E)-coniferyl alcohol to (-)-pinoresinol.
CC {ECO:0000269|PubMed:19946920, ECO:0000269|PubMed:22854967}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22443713}.
CC -!- INTERACTION:
CC Q9SUQ8; Q9SUQ8: DIR6; NbExp=2; IntAct=EBI-7796038, EBI-7796038;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledon veins, leaf
CC trichomes, flowers, siliques, and meristems. Present in
CC interfascicular/vascular cambia and developing xylem.
CC {ECO:0000269|PubMed:22854967}.
CC -!- DEVELOPMENTAL STAGE: In flowers, expressed in the vasculature of
CC petals, stamen filaments, anther microsporangia, and papillar cells of
CC the stigma and style. In siliques, accumulates in the stigmatic region,
CC replum, funiculus, and valve. {ECO:0000269|PubMed:22854967}.
CC -!- SIMILARITY: Belongs to the plant dirigent protein family.
CC {ECO:0000305}.
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DR EMBL; AL035394; CAA23035.1; -; Genomic_DNA.
DR EMBL; AL161559; CAB79324.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84795.1; -; Genomic_DNA.
DR EMBL; BT002439; AAO00799.1; -; mRNA.
DR EMBL; AY088422; AAM65959.1; -; mRNA.
DR PIR; T05601; T05601.
DR RefSeq; NP_194100.1; NM_118500.3.
DR PDB; 5LAL; X-ray; 1.40 A; A/B=30-187.
DR PDBsum; 5LAL; -.
DR AlphaFoldDB; Q9SUQ8; -.
DR SMR; Q9SUQ8; -.
DR MINT; Q9SUQ8; -.
DR STRING; 3702.AT4G23690.1; -.
DR iPTMnet; Q9SUQ8; -.
DR PaxDb; Q9SUQ8; -.
DR PRIDE; Q9SUQ8; -.
DR ProteomicsDB; 224122; -.
DR DNASU; 828469; -.
DR EnsemblPlants; AT4G23690.1; AT4G23690.1; AT4G23690.
DR GeneID; 828469; -.
DR Gramene; AT4G23690.1; AT4G23690.1; AT4G23690.
DR KEGG; ath:AT4G23690; -.
DR Araport; AT4G23690; -.
DR TAIR; locus:2128469; AT4G23690.
DR eggNOG; ENOG502RXV9; Eukaryota.
DR HOGENOM; CLU_087111_0_0_1; -.
DR InParanoid; Q9SUQ8; -.
DR OMA; FNSWFSY; -.
DR OrthoDB; 1485252at2759; -.
DR PhylomeDB; Q9SUQ8; -.
DR PRO; PR:Q9SUQ8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUQ8; baseline and differential.
DR Genevisible; Q9SUQ8; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0042349; F:guiding stereospecific synthesis activity; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:1901599; P:(-)-pinoresinol biosynthetic process; IDA:TAIR.
DR GO; GO:0050790; P:regulation of catalytic activity; IDA:TAIR.
DR Gene3D; 2.40.480.10; -; 1.
DR InterPro; IPR044859; Allene_oxi_cyc_Dirigent.
DR InterPro; IPR004265; Dirigent.
DR PANTHER; PTHR46442; PTHR46442; 1.
DR Pfam; PF03018; Dirigent; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoplast; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:19946920"
FT CHAIN 30..187
FT /note="Dirigent protein 6"
FT /id="PRO_0000422837"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22443713"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22443713"
FT DISULFID 40..186
FT /evidence="ECO:0000269|PubMed:22443713"
FT STRAND 40..51
FT /evidence="ECO:0007829|PDB:5LAL"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:5LAL"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5LAL"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:5LAL"
FT STRAND 79..90
FT /evidence="ECO:0007829|PDB:5LAL"
FT STRAND 97..106
FT /evidence="ECO:0007829|PDB:5LAL"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:5LAL"
FT STRAND 114..126
FT /evidence="ECO:0007829|PDB:5LAL"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:5LAL"
FT STRAND 141..153
FT /evidence="ECO:0007829|PDB:5LAL"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:5LAL"
FT STRAND 159..170
FT /evidence="ECO:0007829|PDB:5LAL"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:5LAL"
FT STRAND 174..186
FT /evidence="ECO:0007829|PDB:5LAL"
SQ SEQUENCE 187 AA; 21412 MW; 1C54CA701F18223D CRC64;
MAFLVEKQLF KALFSFFLLV LLFSDTVLSF RKTIDQKKPC KHFSFYFHDI LYDGDNVANA
TSAAIVSPPG LGNFKFGKFV IFDGPITMDK NYLSKPVARA QGFYFYDMKM DFNSWFSYTL
VFNSTEHKGT LNIMGADLMM EPTRDLSVVG GTGDFFMARG IATFVTDLFQ GAKYFRVKMD
IKLYECY
