ID   PLETY_LOTJA             Reviewed;         361 AA.
AC   A0A0A1H7M6;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Hydroxyproline O-arabinosyltransferase PLENTY {ECO:0000305};
DE            EC=2.4.2.58 {ECO:0000269|PubMed:30351431};
GN   Name=PLENTY {ECO:0000303|PubMed:30351431};
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
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; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, AND DISRUPTION PHENOTYPE.
RC   TISSUE=Root;
RX   PubMed=30351431; DOI=10.1093/jxb/ery364;
RA   Yoro E., Nishida H., Ogawa-Ohnishi M., Yoshida C., Suzaki T.,
RA   Matsubayashi Y., Kawaguchi M.;
RT   "PLENTY, a hydroxyproline O-arabinosyltransferase, negatively regulates
RT   root nodule symbiosis in Lotus japonicus.";
RL   J. Exp. Bot. 70:507-517(2019).
CC   -!- FUNCTION: Glycosyltransferase involved in the O-arabinosylation of
CC       several proteins including extensins and small signaling peptides
CC       (Probable). Catalyzes the transfer of the initial L-arabinose to the
CC       hydroxyl group of Hyp residues (PubMed:30351431). Probably involved in
CC       the arabinosylation of CLAVATA3/ESR-related (CLE) signaling peptides
CC       that move from root to shoot, to interact with receptor kinase
CC       signaling that regulates nodulation (PubMed:30351431). Involved in long
CC       distance nodulation signaling events (PubMed:30351431). 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:30351431). {ECO:0000269|PubMed:30351431,
CC       ECO:0000305|PubMed:30351431}.
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:0000269|PubMed:30351431};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49473;
CC         Evidence={ECO:0000269|PubMed:30351431};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:30351431}; Single-pass type II membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Dramatic increase in root nodule number when
CC       inoculated with Mesorhizobium loti (PubMed:30351431). Inhibition of
CC       root and shoot growth (PubMed:30351431). {ECO:0000269|PubMed:30351431}.
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DR   EMBL; LC010646; BAP90378.1; -; mRNA.
DR   AlphaFoldDB; A0A0A1H7M6; -.
DR   OMA; AGKDHGY; -.
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   1: Evidence at protein level;
KW   Glycosyltransferase; Golgi apparatus; Membrane; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..361
FT                   /note="Hydroxyproline O-arabinosyltransferase PLENTY"
FT                   /id="PRO_0000448630"
FT   TRANSMEM        13..33
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   361 AA;  41425 MW;  EF41C138E7759D07 CRC64;
     MIVRKNMGRA KSLLMLLMVL GFFFATYNLV SMIMDHRAGN WVADGLESFD RKMLGSASTN
     AKYHVALTAT DAAYSQWQCR IMYYWYKKVK DMPGSNMGKF TRILHSGRTD QLMDEIPTFV
     VDPLPEGLDR GYIVLNRPWA FVQWLEKADI EEEYILMAEP DHIFVNPLPN LASRTQPAGY
     PFFYIKPAEN EKIIRKFYPK DKGPVTDVDP IGNSPVIIQK SLIEEIAPTW VNVSLRMKDD
     PETDKAFGWV LEMYAYAVAS ALHGVKHILR KDFMLQPPWD RHVGKTFIIH YTYGCDYNLK
     GELTYGKIGE WRFDKRSYLM GPPPKNLSLP PPGVPESVVR LVKMVNEATA NIPEWDSLNR
     S