MAX1_ARATH
ID MAX1_ARATH Reviewed; 522 AA.
AC B9DFU2; O64853; Q940L3;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Cytochrome P450 711A1;
DE EC=1.14.-.-;
DE AltName: Full=Protein MORE AXILLARY BRANCHES 1;
GN Name=CYP711A1; Synonyms=MAX1; OrderedLocusNames=At2g26170;
GN ORFNames=T19L18.2, T1D16.2;
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] (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;
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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15737939; DOI=10.1016/j.devcel.2005.01.009;
RA Booker J., Sieberer T., Wright W., Williamson L., Willett B., Stirnberg P.,
RA Turnbull C., Srinivasan M., Goddard P., Leyser O.;
RT "MAX1 encodes a cytochrome P450 family member that acts downstream of
RT MAX3/4 to produce a carotenoid-derived branch-inhibiting hormone.";
RL Dev. Cell 8:443-449(2005).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16387852; DOI=10.1073/pnas.0509463102;
RA Lazar G., Goodman H.M.;
RT "MAX1, a regulator of the flavonoid pathway, controls vegetative axillary
RT bud outgrowth in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:472-476(2006).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=20667910; DOI=10.1242/dev.051987;
RA Crawford S., Shinohara N., Sieberer T., Williamson L., George G.,
RA Hepworth J., Mueller D., Domagalska M.A., Leyser O.;
RT "Strigolactones enhance competition between shoot branches by dampening
RT auxin transport.";
RL Development 137:2905-2913(2010).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=21119045; DOI=10.1104/pp.110.164640;
RA Kohlen W., Charnikhova T., Liu Q., Bours R., Domagalska M.A., Beguerie S.,
RA Verstappen F., Leyser O., Bouwmeester H., Ruyter-Spira C.;
RT "Strigolactones are transported through the xylem and play a key role in
RT shoot architectural response to phosphate deficiency in nonarbuscular
RT mycorrhizal host Arabidopsis.";
RL Plant Physiol. 155:974-987(2011).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=23204501; DOI=10.1093/mp/sss138;
RA Fukui K., Ito S., Asami T.;
RT "Selective mimics of strigolactone actions and their potential use for
RT controlling damage caused by root parasitic weeds.";
RL Mol. Plant 6:88-99(2013).
RN [10]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=25425668; DOI=10.1073/pnas.1410801111;
RA Abe S., Sado A., Tanaka K., Kisugi T., Asami K., Ota S., Kim H.I.,
RA Yoneyama K., Xie X., Ohnishi T., Seto Y., Yamaguchi S., Akiyama K.,
RA Yoneyama K., Nomura T.;
RT "Carlactone is converted to carlactonoic acid by MAX1 in Arabidopsis and
RT its methyl ester can directly interact with AtD14 in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:18084-18089(2014).
CC -!- FUNCTION: Converts carlactone to carlactonoic acid by catalyzing
CC consecutive oxidations at C-19 to convert the C-19 methyl group into
CC carboxylic acid (PubMed:25425668). Prefers 11R-carlactone to 11S-
CC carlactone as substrate (PubMed:25425668). Acts downstream of CCD7/MAX3
CC and CCD8/MAX4 in strigolactone signaling pathway and may be implicated
CC in synthesis of carotenoid-derived branch regulators. Acts as a
CC positive regulator of the flavonoid pathway in the late vegetative
CC stage plant. Strigolactones are hormones that inhibit tillering and
CC shoot branching through the MAX-dependent pathway, contribute to the
CC regulation of shoot architectural response to phosphate-limiting
CC conditions and function as rhizosphere signal that stimulates hyphal
CC branching of arbuscular mycorrhizal fungi and trigger seed germination
CC of root parasitic weeds (PubMed:15737939, PubMed:16387852).
CC {ECO:0000269|PubMed:15737939, ECO:0000269|PubMed:16387852,
CC ECO:0000269|PubMed:25425668}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B9DFU2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B9DFU2-2; Sequence=VSP_046323;
CC -!- TISSUE SPECIFICITY: Expressed in the vascular cylinder (including the
CC pericycle) in roots, the cambial region of vascular bundles in
CC inflorescence stems and the vascular junctions of axillary regions in
CC leaves and flowers. {ECO:0000269|PubMed:15737939}.
CC -!- DISRUPTION PHENOTYPE: Increased shoot branching.
CC {ECO:0000269|PubMed:15737939, ECO:0000269|PubMed:16387852,
CC ECO:0000269|PubMed:20667910, ECO:0000269|PubMed:21119045,
CC ECO:0000269|PubMed:23204501}.
CC -!- MISCELLANEOUS: The branching phenotypes of the max1, ccd7/max3 and
CC ccd8/max4 mutants can be rescued by exogenous treatment with the
CC synthetic strigolactone analogs GR24 and 4BD.
CC {ECO:0000305|PubMed:23204501}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL91286.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC004484; AAC14532.2; -; Genomic_DNA.
DR EMBL; AC004747; AAM15001.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07803.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07804.1; -; Genomic_DNA.
DR EMBL; AY054283; AAL06942.1; -; mRNA.
DR EMBL; AY090384; AAL91286.1; ALT_FRAME; mRNA.
DR EMBL; AK316903; BAH19609.1; -; mRNA.
DR PIR; T02607; T02607.
DR RefSeq; NP_565617.2; NM_128175.3. [B9DFU2-1]
DR RefSeq; NP_850074.1; NM_179743.2. [B9DFU2-2]
DR AlphaFoldDB; B9DFU2; -.
DR SMR; B9DFU2; -.
DR BioGRID; 2509; 1.
DR STRING; 3702.AT2G26170.1; -.
DR PaxDb; B9DFU2; -.
DR PRIDE; B9DFU2; -.
DR ProteomicsDB; 238685; -. [B9DFU2-1]
DR EnsemblPlants; AT2G26170.1; AT2G26170.1; AT2G26170. [B9DFU2-1]
DR EnsemblPlants; AT2G26170.2; AT2G26170.2; AT2G26170. [B9DFU2-2]
DR GeneID; 817157; -.
DR Gramene; AT2G26170.1; AT2G26170.1; AT2G26170. [B9DFU2-1]
DR Gramene; AT2G26170.2; AT2G26170.2; AT2G26170. [B9DFU2-2]
DR KEGG; ath:AT2G26170; -.
DR Araport; AT2G26170; -.
DR TAIR; locus:2057361; AT2G26170.
DR eggNOG; KOG0158; Eukaryota.
DR InParanoid; B9DFU2; -.
DR OMA; PFHNMEL; -.
DR OrthoDB; 786853at2759; -.
DR PhylomeDB; B9DFU2; -.
DR PRO; PR:B9DFU2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; B9DFU2; baseline and differential.
DR Genevisible; B9DFU2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0016117; P:carotenoid biosynthetic process; TAS:TAIR.
DR GO; GO:0009963; P:positive regulation of flavonoid biosynthetic process; IEP:TAIR.
DR GO; GO:0009934; P:regulation of meristem structural organization; IMP:TAIR.
DR GO; GO:0010223; P:secondary shoot formation; IMP:TAIR.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..522
FT /note="Cytochrome P450 711A1"
FT /id="PRO_0000422062"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 467
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_046323"
SQ SEQUENCE 522 AA; 59425 MW; 77E46CD65838398F CRC64;
MKTQHQWWEV LDPFLTQHEA LIAFLTFAAV VIVIYLYRPS WSVCNVPGPT AMPLVGHLPL
MAKYGPDVFS VLAKQYGPIF RFQMGRQPLI IIAEAELCRE VGIKKFKDLP NRSIPSPISA
SPLHKKGLFF TRDKRWSKMR NTILSLYQPS HLTSLIPTMH SFITSATHNL DSKPRDIVFS
NLFLKLTTDI IGQAAFGVDF GLSGKKPIKD VEVTDFINQH VYSTTQLKMD LSGSLSIILG
LLIPILQEPF RQVLKRIPGT MDWRVEKTNA RLSGQLNEIV SKRAKEAETD SKDFLSLILK
ARESDPFAKN IFTSDYISAV TYEHLLAGSA TTAFTLSSVL YLVSGHLDVE KRLLQEIDGF
GNRDLIPTAH DLQHKFPYLD QVIKEAMRFY MVSPLVARET AKEVEIGGYL LPKGTWVWLA
LGVLAKDPKN FPEPEKFKPE RFDPNGEEEK HRHPYAFIPF GIGPRACVGQ RFALQEIKLT
LLHLYRNYIF RHSLEMEIPL QLDYGIILSF KNGVKLRTIK RF
