RDN2_MEDTR
ID RDN2_MEDTR Reviewed; 360 AA.
AC G7LG31;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Hydroxyproline O-arabinosyltransferase RDN2 {ECO:0000305};
DE EC=2.4.2.58 {ECO:0000305};
DE AltName: Full=Protein ROOT DETERMINED NODULATION 2 {ECO:0000303|PubMed:28592666};
DE Short=MtRDN2 {ECO:0000303|PubMed:28592666};
GN Name=RDN2 {ECO:0000303|PubMed:28592666};
GN OrderedLocusNames=MTR_8g039290 {ECO:0000312|EMBL:AET02336.1};
GN ORFNames=MtrunA17_Chr8g0353191 {ECO:0000312|EMBL:RHN40293.1};
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION.
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: Glycosyltransferase involved in the O-arabinosylation of
CC several proteins including extensins and small signaling peptides (By
CC similarity). Catalyzes the transfer of the initial L-arabinose to the
CC hydroxyl group of Hyp residues (By similarity). Probably involved in
CC the arabinosylation of CLAVATA3/ESR-related (CLE) signaling peptides
CC that move from root to shoot, to interact with SUNN receptor kinase
CC signaling that regulates nodulation (Probable). Involved in long
CC distance nodulation signaling events (PubMed:28592666). Involved in the
CC autoregulation of nodulation (AON), a long distance systemic signaling
CC from root to shoot and back again, which allows legumes to limit the
CC number of root nodules formed based on available nitrogen and previous
CC rhizobial colonization (PubMed:28592666). Functions in the root,
CC upstream of the shoot receptor kinase SUNN and via CLE peptide, to
CC control AON (PubMed:28592666). {ECO:0000250|UniProtKB:E9KID2,
CC ECO:0000269|PubMed:28592666, 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:0000250|UniProtKB:E9KID2}; Single-pass type II membrane protein
CC {ECO:0000255}.
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DR EMBL; CM001224; AET02336.1; -; Genomic_DNA.
DR EMBL; PSQE01000008; RHN40293.1; -; Genomic_DNA.
DR RefSeq; XP_003627860.1; XM_003627812.2.
DR AlphaFoldDB; G7LG31; -.
DR STRING; 3880.AET02336; -.
DR EnsemblPlants; AET02336; AET02336; MTR_8g039290.
DR GeneID; 11443987; -.
DR Gramene; AET02336; AET02336; MTR_8g039290.
DR KEGG; mtr:MTR_8g039290; -.
DR eggNOG; ENOG502QQNK; Eukaryota.
DR HOGENOM; CLU_065254_0_0_1; -.
DR OMA; TMIIHYG; -.
DR OrthoDB; 897130at2759; -.
DR Proteomes; UP000002051; Chromosome 8.
DR Proteomes; UP000265566; Chromosome 8.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; IEA:EnsemblPlants.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990585; F:hydroxyproline O-arabinosyltransferase activity; IEA:EnsemblPlants.
DR GO; GO:0102562; F:hydroxyproline O-arbinofuranose transferase activity; IEA:RHEA.
DR InterPro; IPR044845; HPAT/SRGT1-like.
DR PANTHER; PTHR31485; PTHR31485; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..360
FT /note="Hydroxyproline O-arabinosyltransferase RDN2"
FT /id="PRO_5014574267"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 360 AA; 41017 MW; 6B5A556F07E8642C CRC64;
MARASPLLMI CLVLGSSFAT YNLVTMIIHY GSADSLATED GGLFFDPIVE MPEHVKNTKT
SKAPFHIALT ATDAIYNKWQ CRIMYYWYKK QRSLPGSEMG GFTRILHSGK ADNLMDEIPT
VVVDPLPEGL DRGYVVLNRP WAFVQWLEKA NIEEEYILMA EPDHVFVRPL PNLAFGENPA
AFPFFYIKPK ENEKIVRKYY PEENGPVTNV DPIGNSPVII RKDLIAKIAP TWMNISMKMK
EDPETDKAFG WVLEMYGYAV ASALHGVRHI LRKDFMLQPP WDTETFNKYI IHYTYGCDYN
LKGELTYGKI GEWRFDKRSH LRGPPPRNLP LPPPGVPESV ATLVKMVNEA SANIPNWDTL
