RMS3_PEA
ID RMS3_PEA Reviewed; 267 AA.
AC A0A109QYD3;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Strigolactone esterase RMS3 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000305};
DE AltName: Full=Protein DWARF 14 homolog {ECO:0000305};
DE Short=PsD14 {ECO:0000303|PubMed:27479744};
DE AltName: Full=Protein RAMOSUS 3 {ECO:0000303|PubMed:27479744};
GN Name=RMS3 {ECO:0000303|PubMed:27479744};
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF GLY-15; GLY-28
RP AND SER-96, AND DISRUPTION PHENOTYPE.
RX PubMed=27479744; DOI=10.1038/nchembio.2147;
RA de Saint Germain A., Clave G., Badet-Denisot M.A., Pillot J.P., Cornu D.,
RA Le Caer J.P., Burger M., Pelissier F., Retailleau P., Turnbull C.,
RA Bonhomme S., Chory J., Rameau C., Boyer F.D.;
RT "An histidine covalent receptor and butenolide complex mediates
RT strigolactone perception.";
RL Nat. Chem. Biol. 12:787-794(2016).
CC -!- FUNCTION: Involved in strigolactone signaling pathway. Functions
CC downstream of strigolactone synthesis, as a component of hormone
CC signaling and as an enzyme that participates in the conversion of
CC strigolactones to the bioactive form. Binds and hydrolyzes the
CC synthetic strigolactone analog GR24 and its enantiomers in vitro. Forms
CC a stable covalent complex with the D-ring of strigolactone, which is
CC essential for hormone bioactivity. The D-ring is attached to His-247 of
CC the catalytic triad. The hydrolysis of strigolactone into a covalently
CC linked intermediate molecule is required to trigger strigolactone
CC signaling. This mechanism defines RMS3 as a non-canonical hormone
CC receptor with dual functions to generate and sense the active form of
CC strigolactone (PubMed:27479744). Strigolactones are hormones that
CC inhibit tillering and shoot branching through the MAX-dependent
CC pathway, contribute to the regulation of shoot architectural response
CC to phosphate-limiting conditions and function as rhizosphere signal
CC that stimulates hyphal branching of arbuscular mycorrhizal fungi and
CC trigger seed germination of root parasitic weeds (Probable).
CC {ECO:0000269|PubMed:27479744, ECO:0000305|PubMed:27479744}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9SQR3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9SQR3}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant height and extensive vegetative
CC branching from both basal and aerial nodes.
CC {ECO:0000269|PubMed:27479744}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; KT321518; AMB61024.1; -; Genomic_DNA.
DR EMBL; KT321521; AMB61027.1; -; Genomic_DNA.
DR EMBL; KT321524; AMB61030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109QYD3; -.
DR SMR; A0A109QYD3; -.
DR ESTHER; pea-RMS3; RsbQ-like.
DR EnsemblPlants; Psat6g018360.1; Psat6g018360.1.cds; Psat6g018360.
DR Gramene; Psat6g018360.1; Psat6g018360.1.cds; Psat6g018360.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0010223; P:secondary shoot formation; IEA:InterPro.
DR GO; GO:1901601; P:strigolactone biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR031143; D14_fam.
DR PANTHER; PTHR43039:SF4; PTHR43039:SF4; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Nucleus.
FT CHAIN 1..267
FT /note="Strigolactone esterase RMS3"
FT /id="PRO_0000437987"
FT ACT_SITE 96
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q10QA5"
FT ACT_SITE 218
FT /evidence="ECO:0000250|UniProtKB:Q10QA5"
FT ACT_SITE 247
FT /evidence="ECO:0000250|UniProtKB:Q10QA5"
FT MUTAGEN 15
FT /note="G->D: In rms3-3; ramosus phenotype, reduced plant
FT height and extensive vegetative branching from both basal
FT and aerial nodes."
FT /evidence="ECO:0000269|PubMed:27479744"
FT MUTAGEN 28
FT /note="G->D: In rms3-4; ramosus phenotype, reduced plant
FT height and extensive vegetative branching from both basal
FT and aerial nodes."
FT /evidence="ECO:0000269|PubMed:27479744"
FT MUTAGEN 96
FT /note="S->F: In rms3-5; loss of esterase activity. Ramosus
FT phenotype, reduced plant height and extensive vegetative
FT branching from both basal and aerial nodes."
FT /evidence="ECO:0000269|PubMed:27479744"
SQ SEQUENCE 267 AA; 29647 MW; 09066EB8F1C34635 CRC64;
MGTPILDAFN VRVEGSGDKY LVFAHGFGTD QSAWQRVLPY FTRSYKVILY DLVCAGSVNP
DHFDFRRYTT LDAYVDDLLN ILDSLHVTRC AYVGHSISAM TGMLASIRRP ELFSKLILIG
ASPRFLNDGE NYHGGFEQGE IEHVFSAMEA NYEAWVNGFA PLAVGADVPT AVREFSRTLF
NMRPDISLFV SRTVFNSDLR GILGLVNVPC CIMQTARDMS VPASVATYMK EHIGGKSTVQ
WLDTEGHLPH LSAPSYLAHQ LEIALSQ
