ID   RAY1_ARATH              Reviewed;         537 AA.
AC   F4I6V0; Q9S7C7;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Beta-arabinofuranosyltransferase RAY1 {ECO:0000305};
DE            EC=2.4.2.- {ECO:0000305};
DE   AltName: Full=Protein REDUCED ARABINOSE YARIV 1 {ECO:0000303|PubMed:23396039};
GN   Name=RAY1 {ECO:0000303|PubMed:23396039};
GN   OrderedLocusNames=At1g70630 {ECO:0000312|Araport:AT1G70630};
GN   ORFNames=F24J13.20 {ECO:0000312|EMBL:AAG52475.1},
GN   F5A18.19 {ECO:0000312|EMBL:AAG52325.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=24905498; DOI=10.1111/tpj.12577;
RA   Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA   Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA   Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA   Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA   Loque D., Scheller H.V., Heazlewood J.L.;
RT   "The plant glycosyltransferase clone collection for functional genomics.";
RL   Plant J. 79:517-529(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=23396039; DOI=10.1093/mp/sst029;
RA   Gille S., Sharma V., Baidoo E.E., Keasling J.D., Scheller H.V., Pauly M.;
RT   "Arabinosylation of a Yariv-precipitable cell wall polymer impacts plant
RT   growth as exemplified by the Arabidopsis glycosyltransferase mutant ray1.";
RL   Mol. Plant 6:1369-1372(2013).
CC   -!- FUNCTION: Beta-arabinofuranosyltransferase that transfers specifically
CC       an arabinosyl residue from UDP-arabinofuranose to the monosaccharide
CC       galactose or beta-methyl-galactoside in vitro. Catalyzes the addition
CC       of a beta-arabinofuranose residue onto a beta-galactosyl residue of an
CC       Yariv-precipitable wall polymer in vivo. {ECO:0000269|PubMed:23396039}.
CC   -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC       {ECO:0000250|UniProtKB:Q9JI93}.
CC   -!- DISRUPTION PHENOTYPE: Reduced growth of primary root. Delayed
CC       flowering. {ECO:0000269|PubMed:23396039}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 77 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG52325.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG52475.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; KJ138944; AHL38884.1; -; mRNA.
DR   EMBL; AC010796; AAG52475.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC011663; AAG52325.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE35092.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM59749.1; -; Genomic_DNA.
DR   PIR; E96730; E96730.
DR   RefSeq; NP_001322086.1; NM_001334470.1.
DR   RefSeq; NP_177220.2; NM_105731.4.
DR   AlphaFoldDB; F4I6V0; -.
DR   STRING; 3702.AT1G70630.1; -.
DR   CAZy; GT77; Glycosyltransferase Family 77.
DR   iPTMnet; F4I6V0; -.
DR   PaxDb; F4I6V0; -.
DR   PRIDE; F4I6V0; -.
DR   ProteomicsDB; 236488; -.
DR   EnsemblPlants; AT1G70630.1; AT1G70630.1; AT1G70630.
DR   EnsemblPlants; AT1G70630.2; AT1G70630.2; AT1G70630.
DR   GeneID; 843400; -.
DR   Gramene; AT1G70630.1; AT1G70630.1; AT1G70630.
DR   Gramene; AT1G70630.2; AT1G70630.2; AT1G70630.
DR   KEGG; ath:AT1G70630; -.
DR   Araport; AT1G70630; -.
DR   TAIR; locus:2026831; AT1G70630.
DR   eggNOG; ENOG502QRDX; Eukaryota.
DR   HOGENOM; CLU_020968_1_0_1; -.
DR   InParanoid; F4I6V0; -.
DR   PRO; PR:F4I6V0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4I6V0; baseline and differential.
DR   Genevisible; F4I6V0; AT.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR   GO; GO:0016757; F:glycosyltransferase activity; IDA:TAIR.
DR   GO; GO:0042546; P:cell wall biogenesis; IMP:TAIR.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR005069; Nucl-diP-sugar_transferase.
DR   InterPro; IPR044575; RAY1-like.
DR   PANTHER; PTHR47483; PTHR47483; 1.
DR   Pfam; PF03407; Nucleotid_trans; 1.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..537
FT                   /note="Beta-arabinofuranosyltransferase RAY1"
FT                   /id="PRO_0000434536"
FT   MOTIF           370..372
FT                   /note="DXD motif"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   537 AA;  61922 MW;  57D84CE2B6AF2D55 CRC64;
     MMSRIEAYQS DIAVLMDPET VLLPDFISAL SYAHELGRDW LLVSSSVEIP RFPFHWDETR
     HFWRQDNGKR VRFRELQKMI SLRSLQSNSS ASKMIMAWNN IDMPLHCGVL PPFLYQRGTH
     NQWIINEAMS CKRRFVFDAT STISSFFLGN AENIYNRSDN VSEPKTRNWE YVGNSHLGQL
     YGSLYSRSYT LPKLLKCNRR YIFVSASERS TDLSIPKGKS LGFRTREKIS ACITRTKSRS
     LKLDFVQKDE TVPPLKFPFD LESLLPLVAD KNRTVVLSVA GYSYKDMLMS WVCRLRRLKV
     PNFLVCALDD ETYQFSILQG LPVFFDPYAP KNISFNDCHF GSKCFQRVTK VKSRTVLKIL
     KLGYNVLLSD VDVYWFRNPL PLLQSFGPSV LAAQSDEYNT TAPINRPRRL NSGFYFARSD
     SPTIAAMEKV VKHAATSGLS EQPSFYDTLC GEGGAYRLGD DRCVEPETNL TVQFLDRELF
     PNGAYGDLWL KEDVRAECEK KHCFVLHNNW ISGRLKKLER QMMKGLWEYD ASMRMCV