RETOL_ARATH
ID RETOL_ARATH Reviewed; 570 AA.
AC Q9SVG4; B9DFM8; Q3E9Y2; Q8H7B5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Berberine bridge enzyme-like 19 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 19 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 20 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE AltName: Full=Reticuline oxidase-like protein;
DE EC=1.21.-.-;
DE Flags: Precursor;
GN OrderedLocusNames=At4g20830; ORFNames=F21C20.180;
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] (ISOFORM 2).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-175.
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=26037923; DOI=10.1074/jbc.m115.659631;
RA Daniel B., Pavkov-Keller T., Steiner B., Dordic A., Gutmann A.,
RA Nidetzky B., Sensen C.W., van der Graaff E., Wallner S., Gruber K.,
RA Macheroux P.;
RT "Oxidation of monolignols by members of the berberine bridge enzyme family
RT suggests a role in plant cell wall metabolism.";
RL J. Biol. Chem. 290:18770-18781(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P30986};
CC Note=Binds 1 FAD per subunit in a bicovalent manner.
CC {ECO:0000250|UniProtKB:P30986};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:O64743}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=AtBBE-like 19;
CC IsoId=Q9SVG4-1; Sequence=Displayed;
CC Name=2; Synonyms=AtBBE-like 20;
CC IsoId=Q9SVG4-2; Sequence=VSP_021389, VSP_021390;
CC -!- PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-
CC N1-histidyl FAD linkage. {ECO:0000250|UniProtKB:P30986}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AL080254; CAB45849.1; -; Genomic_DNA.
DR EMBL; AL161553; CAB79083.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84365.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84366.1; -; Genomic_DNA.
DR EMBL; AY133533; AAM91363.1; -; mRNA.
DR EMBL; AY062595; AAL32673.1; -; mRNA.
DR EMBL; AF424621; AAL11614.1; -; mRNA.
DR EMBL; AK316833; BAH19545.1; -; mRNA.
DR EMBL; AF083756; AAN60314.1; -; mRNA.
DR PIR; T10625; T10625.
DR RefSeq; NP_193815.2; NM_118201.3. [Q9SVG4-1]
DR RefSeq; NP_974580.1; NM_202851.1. [Q9SVG4-2]
DR AlphaFoldDB; Q9SVG4; -.
DR SMR; Q9SVG4; -.
DR BioGRID; 13122; 1.
DR STRING; 3702.AT4G20830.1; -.
DR SwissPalm; Q9SVG4; -.
DR PaxDb; Q9SVG4; -.
DR PRIDE; Q9SVG4; -.
DR ProteomicsDB; 236852; -. [Q9SVG4-1]
DR EnsemblPlants; AT4G20830.1; AT4G20830.1; AT4G20830. [Q9SVG4-1]
DR EnsemblPlants; AT4G20830.2; AT4G20830.2; AT4G20830. [Q9SVG4-2]
DR GeneID; 827831; -.
DR Gramene; AT4G20830.1; AT4G20830.1; AT4G20830. [Q9SVG4-1]
DR Gramene; AT4G20830.2; AT4G20830.2; AT4G20830. [Q9SVG4-2]
DR KEGG; ath:AT4G20830; -.
DR Araport; AT4G20830; -.
DR TAIR; locus:2121539; AT4G20830.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR InParanoid; Q9SVG4; -.
DR OMA; GYPFPGG; -.
DR OrthoDB; 1049549at2759; -.
DR PhylomeDB; Q9SVG4; -.
DR BioCyc; ARA:AT4G20830-MON; -.
DR PRO; PR:Q9SVG4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SVG4; baseline and differential.
DR Genevisible; Q9SVG4; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA: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; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016899; F:oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor; IDA:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell wall; Disulfide bond; FAD; Flavoprotein;
KW Glycoprotein; Nucleotide-binding; Oxidoreductase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..570
FT /note="Berberine bridge enzyme-like 19"
FT /id="PRO_0000259448"
FT DOMAIN 83..257
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 42..105
FT /evidence="ECO:0000250|UniProtKB:O64743"
FT CROSSLNK 120..182
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000250|UniProtKB:P30986"
FT VAR_SEQ 538..540
FT /note="NEK -> SKA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_021389"
FT VAR_SEQ 541..570
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_021390"
FT CONFLICT 14
FT /note="Missing (in Ref. 5; AAN60314)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="D -> E (in Ref. 5; AAN60314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 63559 MW; 5898D6128F79735A CRC64;
MLTTPPRTFV SVPFFFFFLL FLSLPLSSFS QSNSVYNSFL KCFSDKTKSP QSQITDNVFS
QTNPAFSSVL RAYIRNARFN TSSTLKPTII ITPRSESHVS AAVTCSKTLN FLLKIRSGGH
DYDGLSYISD KPFFILDMSN IRDVSVDIAS NSAWISAGAT LGEVYYRIWE KSRVHGFPAG
VCPTVGVGGH LSGGGYGNMV RKFGLSVDYV EDAKIVDVNG RVLDRKAMGE DLFWAITGGG
GGSYGVVLGY KVKLVPVPSV VTVFRVEQYM DSGAVDMVHK WQSVGPKTDP NLFMRMLIQP
VTRKKVKTVR ASVVALFLGR ADEVVALLSK EFPELGLKKE NCSEMTWFQS ALWWDNRLNA
TQVDPKVFLD RNLDTSSFGK RKSDYVATAI PKKGIESLFK KMIELGKIGL VFNPYGGKMA
EVAVNAKPFP HRNKLFKIQY SVNWKENSAE IEKGYLNQAK VLYSFMTGFV SKNPRSSYFN
YRDVDIGVND HGANSYKEGE VYGRKYFGEN FDRLVKIKTA VDPGNFFRNE QSIPTLKNEK
GMLLPEPGKA RRWSRVGGAT VVATVVLHVF
