MAX2A_PETHY
ID MAX2A_PETHY Reviewed; 708 AA.
AC I1SSI5;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=F-box/LRR-repeat MAX2 homolog A;
DE AltName: Full=F-box and leucine-rich repeat MAX2 homolog A;
GN Name=MAX2A;
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22645562; DOI=10.3389/fpls.2011.00115;
RA Drummond R.S., Sheehan H., Simons J.L., Martinez-Sanchez N.M., Turner R.M.,
RA Putterill J., Snowden K.C.;
RT "The expression of Petunia strigolactone pathway genes is altered as part
RT of the endogenous developmental program.";
RL Front. Plant Sci. 2:115-115(2011).
RN [2]
RP INTERACTION WITH DAD2.
RX PubMed=22959345; DOI=10.1016/j.cub.2012.08.007;
RA Hamiaux C., Drummond R.S., Janssen B.J., Ledger S.E., Cooney J.M.,
RA Newcomb R.D., Snowden K.C.;
RT "DAD2 is an alpha/beta hydrolase likely to be involved in the perception of
RT the plant branching hormone, strigolactone.";
RL Curr. Biol. 22:2032-2036(2012).
CC -!- FUNCTION: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase
CC complexes, which may mediate the ubiquitination and subsequent
CC proteasomal degradation of target proteins. Is necessary for responses
CC to strigolactones and may be involved in the ubiquitin-mediated
CC degradation of specific proteins that activate axillary growth (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of a putative SCF (SKP1/Cullin/F-box) ubiquitin ligase
CC complex (By similarity). Interacts with DAD2. {ECO:0000250,
CC ECO:0000269|PubMed:22959345}.
CC -!- TISSUE SPECIFICITY: Expressed in lateral roots, internodes, nodes,
CC fully expanded leaves, axillary and shoot apex.
CC {ECO:0000269|PubMed:22645562}.
CC -!- DISRUPTION PHENOTYPE: Increased shoot branching.
CC {ECO:0000269|PubMed:22645562}.
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DR EMBL; HM117629; AEB97384.1; -; Genomic_DNA.
DR AlphaFoldDB; I1SSI5; -.
DR SMR; I1SSI5; -.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR041567; COI1_F-box.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF18511; F-box_5; 1.
DR SMART; SM00367; LRR_CC; 3.
PE 1: Evidence at protein level;
KW Leucine-rich repeat; Repeat; Ubl conjugation pathway.
FT CHAIN 1..708
FT /note="F-box/LRR-repeat MAX2 homolog A"
FT /id="PRO_0000422063"
FT DOMAIN 2..49
FT /note="F-box"
FT REPEAT 8..33
FT /note="LRR 1"
FT REPEAT 48..73
FT /note="LRR 2"
FT REPEAT 74..98
FT /note="LRR 3"
FT REPEAT 108..133
FT /note="LRR 4"
FT REPEAT 138..163
FT /note="LRR 5"
FT REPEAT 164..192
FT /note="LRR 6"
FT REPEAT 196..221
FT /note="LRR 7"
FT REPEAT 228..253
FT /note="LRR 8"
FT REPEAT 273..298
FT /note="LRR 9"
FT REPEAT 301..326
FT /note="LRR 10"
FT REPEAT 331..380
FT /note="LRR 12"
FT REPEAT 381..407
FT /note="LRR 13"
FT REPEAT 408..434
FT /note="LRR 14"
FT REPEAT 523..547
FT /note="LRR 16"
FT REPEAT 556..580
FT /note="LRR 17"
FT REPEAT 623..652
FT /note="LRR 18"
SQ SEQUENCE 708 AA; 79437 MW; BA61D872E82E17C5 CRC64;
MATQLNDLPD VILSNIIAAV TDVRSRNSTS FVCRKWLVLE RSTRVSLTLR GNVRDLFMLP
TCFRSITHLD LSLISPWGHP LLSPTTPDPS LTAHLLHHAF PFVTSLVVYT RHPFTLQLLP
PLWPQLKQIK LVRWHQRPQL ATGDEFNMLF ENCPNLSSLD LSTFYCWTDD IPTALVSHPM
VASNLVTLNL LNPCFSEGFK TDEIKAITLA CPNLKEFRVV CMFDPRYIGF VGDEGLVAVA
TNCPKLSTLH LADTSALSNS RGDINDDGFT QEDAKFGVST LIEVFSGLPL LEELVLDVCN
NVRDTGPALE ILNKKCPRLR SLKLGQFHGI SMPVESKLDG VALCQGLESL SIRNVGDLND
MGLIAIGRGC SRLAKFEVQG CKKITVRGMR TLASLLKKTL IDVKISCCKN LGAAYSLKAL
EPIQNRIQKL HIDCVWDSVE EFENLDGYGY GFDLNRRDGC EASSNFGDTF GCEEDAYLFK
EKKRCKFSYD LNSLYEEVNG HGNGYSGRSW DRLQYLSLWI GVGDLLTPLT AAGLEDCPNL
EEIKIRVEGD CRLWSKHSEQ AFGLSTLLHY PKLSKMHLDC GDTIGYAHTA PSGQVDLSLW
ERFYLLGIGT LSLTELDYWP PQDMDVNQRC LSLPAAGLLQ ECLTLRKLFI HGTAHEHFMM
FLLRIPNLRD VQLREDYYPA PENDMSTEMR ADSLSRFEAA LNRRPISD