FOX1_ARATH
ID FOX1_ARATH Reviewed; 535 AA.
AC Q9FZC4;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Berberine bridge enzyme-like 3 {ECO:0000303|PubMed:26037923};
DE Short=AtBBE-like 3 {ECO:0000303|PubMed:26037923};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:O64743};
DE AltName: Full=FAD-linked oxidoreductase {ECO:0000303|PubMed:20164835};
DE EC=1.-.-.- {ECO:0000305|PubMed:26352477};
DE AltName: Full=Flavin-dependent oxidoreductase FOX1 {ECO:0000303|PubMed:26352477};
DE Flags: Precursor;
GN Name=FOX1 {ECO:0000303|PubMed:26352477};
GN Synonyms=FOX {ECO:0000303|PubMed:20164835};
GN OrderedLocusNames=At1g26380 {ECO:0000312|Araport:AT1G26380};
GN ORFNames=T1K7.24 {ECO:0000312|EMBL:AAF98578.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 INDUCTION BY MKK4.
RX PubMed=20164835; DOI=10.1038/nature08794;
RA Boudsocq M., Willmann M.R., McCormack M., Lee H., Shan L., He P., Bush J.,
RA Cheng S.H., Sheen J.;
RT "Differential innate immune signalling via Ca(2+) sensor protein kinases.";
RL Nature 464:418-422(2010).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=21443605; DOI=10.1111/j.1365-3040.2011.02323.x;
RA Inze A., Vanderauwera S., Hoeberichts F.A., Vandorpe M., Van Gaever T.,
RA Van Breusegem F.;
RT "A subcellular localization compendium of hydrogen peroxide-induced
RT proteins.";
RL Plant Cell Environ. 35:308-320(2012).
RN [6]
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).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26352477; DOI=10.1038/nature14907;
RA Rajniak J., Barco B., Clay N.K., Sattely E.S.;
RT "A new cyanogenic metabolite in Arabidopsis required for inducible pathogen
RT defence.";
RL Nature 525:376-379(2015).
CC -!- FUNCTION: Flavin-dependent oxidoreductase involved in the biosynthetic
CC pathway to 4-hydroxyindole-3-carbonyl nitrile (4-OH-ICN), a cyanogenic
CC metabolite required for inducible pathogen defense. Converts indole
CC cyanohydrin into indole-3-carbonyl nitrile (ICN).
CC {ECO:0000269|PubMed:26352477}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O64743};
CC Note=Binds 1 FAD per subunit in a bicovalent manner.
CC {ECO:0000250|UniProtKB:O64743};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:21443605}. Cell membrane
CC {ECO:0000269|PubMed:21443605}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:O64743}.
CC -!- INDUCTION: Up-regulated by MKK4. {ECO:0000269|PubMed:20164835}.
CC -!- PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-
CC N1-histidyl FAD linkage. {ECO:0000250|UniProtKB:O64743}.
CC -!- DISRUPTION PHENOTYPE: Three- to fivefold reduction in levels of ICN
CC metabolites and accumulation of indole cyanogenic glycosides.
CC {ECO:0000269|PubMed:26352477}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC013427; AAF98578.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30684.1; -; Genomic_DNA.
DR EMBL; AF360332; AAK26042.1; -; mRNA.
DR EMBL; AY113892; AAM44940.1; -; mRNA.
DR PIR; E86390; E86390.
DR RefSeq; NP_564244.1; NM_102402.4.
DR AlphaFoldDB; Q9FZC4; -.
DR SMR; Q9FZC4; -.
DR STRING; 3702.AT1G26380.1; -.
DR PaxDb; Q9FZC4; -.
DR PRIDE; Q9FZC4; -.
DR ProteomicsDB; 228942; -.
DR EnsemblPlants; AT1G26380.1; AT1G26380.1; AT1G26380.
DR GeneID; 839180; -.
DR Gramene; AT1G26380.1; AT1G26380.1; AT1G26380.
DR KEGG; ath:AT1G26380; -.
DR Araport; AT1G26380; -.
DR TAIR; locus:2197950; AT1G26380.
DR eggNOG; ENOG502QVGN; Eukaryota.
DR HOGENOM; CLU_018354_6_0_1; -.
DR InParanoid; Q9FZC4; -.
DR OMA; VICAKES; -.
DR OrthoDB; 1049549at2759; -.
DR PhylomeDB; Q9FZC4; -.
DR BioCyc; ARA:AT1G26380-MON; -.
DR BioCyc; MetaCyc:AT1G26380-MON; -.
DR PRO; PR:Q9FZC4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZC4; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0071456; P:cellular response to hypoxia; 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 2: Evidence at transcript level;
KW Cell membrane; Cell wall; Disulfide bond; Endoplasmic reticulum; FAD;
KW Flavoprotein; Glycoprotein; Membrane; Nucleotide-binding; Oxidoreductase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..535
FT /note="Berberine bridge enzyme-like 3"
FT /id="PRO_5004329558"
FT DOMAIN 73..247
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 321
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 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 32..95
FT /evidence="ECO:0000250|UniProtKB:P30986"
FT CROSSLNK 110..172
FT /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT Cys)"
FT /evidence="ECO:0000250|UniProtKB:O64743"
SQ SEQUENCE 535 AA; 59818 MW; F2110DC7DCD9D2AE CRC64;
MKEALFGLYL VLLVSGLEAA VTKPNSGNFI ECLRYQASPE NPITDAIFTV DNTTTFLSSY
VSYTKNTRFS NPNNKNLLAI VVAKDVSHVQ ATVVCAKSNG IQIRIRSGGH DNEGLSYVSS
VPFVILDMHK LRDITVDVSS KKAWVQAGAT LGELYVKIDE ASQTLAFPAG ICATVGAGGH
ISGGGYGNLM RKFGTTVDHV IDAELVDVNG KLLNRSTMGE DLFWAIRGGG GASFGVILSW
KINLVEVPKI FTVFQVNKTL EQGGTDVVYK WQLVANKFPD NLFLRAMPQV VNGTKHGERT
IAIVFWAQFL GRTDELMEIM NQSFPELGLR REDCQEMSWL NTTLFWAMLP AGTPKTVLLG
RPTDPVFFKS KSDYVKKPIP KEGLEKIWKT MLKFNNIVWL HFNPYGGMMD RIPSNATAFP
HRKGNLFKVQ YYTTWLDPNA TESNLSIMKE LYEVAEPYVS SNPREAFFNY RDIDIGSNPS
GETDVDEAKI YGYKYFLGNL KRLMDVKAKS DPENFFKNEQ SIPPLLSRVR RDDEL
