RDN1_MEDTR
ID RDN1_MEDTR Reviewed; 357 AA.
AC E9KID2; G7K339;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Hydroxyproline O-arabinosyltransferase RDN1 {ECO:0000305};
DE EC=2.4.2.58 {ECO:0000305};
DE AltName: Full=Protein ROOT DETERMINED NODULATION 1 {ECO:0000303|PubMed:21742814};
DE Short=MtRDN1 {ECO:0000303|PubMed:21742814};
GN Name=RDN1 {ECO:0000303|PubMed:21742814};
GN OrderedLocusNames=MTR_5g089520 {ECO:0000312|EMBL:AET00211.1};
GN ORFNames=MtrunA17_Chr5g0441831 {ECO:0000312|EMBL:RHN57566.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21742814; DOI=10.1104/pp.111.178756;
RA Schnabel E.L., Kassaw T.K., Smith L.S., Marsh J.F., Oldroyd G.E.,
RA Long S.R., Frugoli J.A.;
RT "The ROOT DETERMINED NODULATION1 gene regulates nodule number in roots of
RT Medicago truncatula and defines a highly conserved, uncharacterized plant
RT gene family.";
RL Plant Physiol. 157:328-340(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 4:1017-1025(2018).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22301956; DOI=10.4161/psb.7.1.18491;
RA Schnabel E., Karve A., Kassaw T., Mukherjee A., Zhou X., Hall T.,
RA Frugoli J.;
RT "The M. truncatula SUNN gene is expressed in vascular tissue, similarly to
RT RDN1, consistent with the role of these nodulation regulation genes in long
RT distance signaling.";
RL Plant Signal. Behav. 7:4-6(2012).
RN [6]
RP FUNCTION.
RX PubMed=27135324; DOI=10.3390/plants4020209;
RA Kassaw T., Bridges W. Jr., Frugoli J.;
RT "Multiple Autoregulation of Nodulation (AON) signals identified through
RT split root analysis of Medicago truncatula sunn and rdn1 mutants.";
RL Plants (Basel) 4:209-224(2015).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=28592666; DOI=10.1104/pp.17.00278;
RA Kassaw T., Nowak S., Schnabel E., Frugoli J.;
RT "ROOT DETERMINED NODULATION1 is required for M. truncatula CLE12, but not
RT CLE13, peptide signaling through the SUNN receptor kinase.";
RL Plant Physiol. 174:2445-2456(2017).
CC -!- FUNCTION: Probable glycosyltransferase involved in the O-
CC arabinosylation of several proteins including extensins and small
CC signaling peptides (Probable). Catalyzes the transfer of the initial L-
CC arabinose to the hydroxyl group of Hyp residues (Probable). Probably
CC involved in the arabinosylation of CLE12, a signaling peptide that
CC moves from root to shoot, to interact with SUNN receptor kinase
CC signaling that regulates nodulation (Probable). Involved in long
CC distance nodulation signaling events (Probable) (PubMed:21742814).
CC Involved in the autoregulation of nodulation (AON), a long distance
CC systemic signaling from root to shoot and back again, which allows
CC legumes to limit the number of root nodules formed based on available
CC nitrogen and previous rhizobial colonization (PubMed:27135324,
CC PubMed:28592666). Functions in the root, upstream of the shoot receptor
CC kinase SUNN and via CLE peptide, to control AON (PubMed:28592666).
CC {ECO:0000269|PubMed:21742814, ECO:0000269|PubMed:27135324,
CC ECO:0000269|PubMed:28592666, ECO:0000305|PubMed:22301956,
CC ECO:0000305|PubMed:28592666}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=trans-4-hydroxy-L-prolyl-[protein] + UDP-beta-L-
CC arabinofuranose = H(+) + O-(beta-L-arabinofuranosyl)-trans-4-hydroxy-
CC L-prolyl-[protein] + UDP; Xref=Rhea:RHEA:49472, Rhea:RHEA-COMP:12408,
CC Rhea:RHEA-COMP:12409, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:61463, ChEBI:CHEBI:61965, ChEBI:CHEBI:131610;
CC EC=2.4.2.58; Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49473;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:28592666}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the vasculature of leaves, petioles,
CC stems and roots (PubMed:22301956). Expressed in the vascular cylinder
CC throughout the root, and nodule vasculature (PubMed:21742814).
CC {ECO:0000269|PubMed:21742814, ECO:0000269|PubMed:22301956}.
CC -!- DISRUPTION PHENOTYPE: Dramatic increase in root nodule number when
CC inoculated with Sinorhizobium medicae (PubMed:21742814,
CC PubMed:28592666). Inhibition of root growth in both the presence and
CC absence of rhizobia (PubMed:21742814, PubMed:28592666).
CC {ECO:0000269|PubMed:21742814, ECO:0000269|PubMed:28592666}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AET00211.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; GU580937; ADV35716.2; -; mRNA.
DR EMBL; CM001221; AET00211.1; ALT_INIT; Genomic_DNA.
DR EMBL; PSQE01000005; RHN57566.1; -; Genomic_DNA.
DR RefSeq; XP_003617252.1; XM_003617204.1.
DR AlphaFoldDB; E9KID2; -.
DR STRING; 3880.AET00211; -.
DR EnsemblPlants; AET00211; AET00211; MTR_5g089520.
DR GeneID; 11432343; -.
DR Gramene; AET00211; AET00211; MTR_5g089520.
DR KEGG; mtr:MTR_5g089520; -.
DR eggNOG; ENOG502QQNK; Eukaryota.
DR HOGENOM; CLU_065254_0_0_1; -.
DR OrthoDB; 897130at2759; -.
DR Proteomes; UP000002051; Chromosome 5.
DR Proteomes; UP000265566; Chromosome 5.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102562; F:hydroxyproline O-arbinofuranose transferase activity; IEA:RHEA.
DR InterPro; IPR044845; HPAT/SRGT1-like.
DR PANTHER; PTHR31485; PTHR31485; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..357
FT /note="Hydroxyproline O-arabinosyltransferase RDN1"
FT /id="PRO_0000448631"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 357 AA; 40980 MW; 07AA75552DBE4F0A CRC64;
MIVRKSMGRV KSLLMLLMVL GFSFATYNLV FMMMEHKAGN DLGSFDGKAM EIRNTNSKYH
VAVTATDAAY SQWQCRIMYY WYKKTKDMPG SAMGKFTRIL HSGRGDQLMN EIPTFVVDPL
PEGLDRGYIV LNRPWAFVQW LEKAVIDEEY ILMAEPDHIF VNPLPNLATE NEPAGYPFFY
IKPAENEKIM RKFYPKENGP VTDVDPIGNS PVIIHKYMLE EIAPTWVNIS LRMKDDPETD
KAFGWVLEMY AYAVASALHG IKHILRKDFM LQPPWDLDVG KKFIIHFTYG CDYNLKGKLT
YGKIGEWRFD KRSYLMGPPP KNLSLPPPGV PESVVRLVKM VNEATANIPN WDSLNRS
