RRT2_ARATH
ID RRT2_ARATH Reviewed; 512 AA.
AC Q93ZR8; Q8LFC3; Q9SRU1;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Rhamnogalacturonan I rhamnosyltransferase 1 {ECO:0000303|PubMed:30082766};
DE EC=2.4.1.351 {ECO:0000269|PubMed:30082766};
DE AltName: Full=O-fucosyltransferase 21 {ECO:0000305};
DE Short=O-FucT-21 {ECO:0000305};
DE AltName: Full=O-fucosyltransferase family protein {ECO:0000312|EMBL:ARJ31427.1};
GN Name=RRT2 {ECO:0000303|PubMed:30082766}; Synonyms=OFUT21 {ECO:0000305};
GN OrderedLocusNames=At3g02250 {ECO:0000312|Araport:AT3G02250};
GN ORFNames=F14P3.10 {ECO:0000312|EMBL:AAF02113.1};
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;
RA Zeng W., Gluza P., Heazlewood J.;
RT "Arabidopsis glycosyltransferases: an update.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 253-512.
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND REVIEW.
RX PubMed=22629278; DOI=10.3389/fpls.2012.00059;
RA Hansen S.F., Harholt J., Oikawa A., Scheller H.V.;
RT "Plant glycosyltransferases beyond CAZy: a perspective on DUF families.";
RL Front. Plant Sci. 3:59-59(2012).
RN [7]
RP GENE FAMILY.
RX PubMed=22916179; DOI=10.1371/journal.pone.0042914;
RA Neumetzler L., Humphrey T., Lumba S., Snyder S., Yeats T.H., Usadel B.,
RA Vasilevski A., Patel J., Rose J.K., Persson S., Bonetta D.;
RT "The FRIABLE1 gene product affects cell adhesion in Arabidopsis.";
RL PLoS ONE 7:E42914-E42914(2012).
RN [8]
RP GENE FAMILY.
RX PubMed=23272088; DOI=10.1371/journal.pone.0051129;
RA Voxeur A., Andre A., Breton C., Lerouge P.;
RT "Identification of putative rhamnogalacturonan-II specific
RT glycosyltransferases in Arabidopsis using a combination of bioinformatics
RT approaches.";
RL PLoS ONE 7:E51129-E51129(2012).
RN [9]
RP GENE FAMILY.
RX PubMed=22966747; DOI=10.1111/tpj.12019;
RA Wang Y., Mortimer J.C., Davis J., Dupree P., Keegstra K.;
RT "Identification of an additional protein involved in mannan biosynthesis.";
RL Plant J. 73:105-117(2013).
RN [10]
RP WEB RESOURCE.
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 [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30082766; DOI=10.1038/s41477-018-0217-7;
RA Takenaka Y., Kato K., Ogawa-Ohnishi M., Tsuruhama K., Kajiura H., Yagyu K.,
RA Takeda A., Takeda Y., Kunieda T., Hara-Nishimura I., Kuroha T.,
RA Nishitani K., Matsubayashi Y., Ishimizu T.;
RT "Pectin RG-I rhamnosyltransferases represent a novel plant-specific
RT glycosyltransferase family.";
RL Nat. Plants 4:669-676(2018).
CC -!- FUNCTION: Glycosyltransferase involved in the formation of
CC rhamnogalacturonan I (RG-I) oligosaccharides in the seed coat mucilage,
CC which is a specialized cell wall with abundant RG-I (By similarity).
CC Transfers the rhamnose residue from UDP-beta-L-rhamnose to RG-I
CC oligosaccharides (PubMed:30082766). {ECO:0000250|UniProtKB:Q4V398,
CC ECO:0000269|PubMed:30082766}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galacturonosyl-[(1->2)-alpha-L-rhamnosyl-(1->4)-alpha-
CC D-galacturonosyl](n) + UDP-beta-L-rhamnose = [(1->2)-alpha-L-
CC rhamnosyl-(1->4)-alpha-D-galacturonosyl](n+1) + H(+) + UDP;
CC Xref=Rhea:RHEA:55736, Rhea:RHEA-COMP:14274, Rhea:RHEA-COMP:14276,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:83836,
CC ChEBI:CHEBI:139158, ChEBI:CHEBI:139159; EC=2.4.1.351;
CC Evidence={ECO:0000269|PubMed:30082766};
CC -!- PATHWAY: Glycan metabolism; pectin biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q4V398}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase GT106 family.
CC {ECO:0000305|PubMed:30082766}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF02113.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=The Arabidopsis GT Collection;
CC URL="http://gt.jbei.org/arabidopsis.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KY906063; ARJ31427.1; -; mRNA.
DR EMBL; AC009755; AAF02113.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73784.1; -; Genomic_DNA.
DR EMBL; AY056304; AAL07153.1; -; mRNA.
DR EMBL; AY140026; AAM98167.1; -; mRNA.
DR EMBL; AY084929; AAM67354.1; -; mRNA.
DR RefSeq; NP_566168.2; NM_111092.4.
DR AlphaFoldDB; Q93ZR8; -.
DR STRING; 3702.AT3G02250.1; -.
DR iPTMnet; Q93ZR8; -.
DR PaxDb; Q93ZR8; -.
DR PRIDE; Q93ZR8; -.
DR ProteomicsDB; 236200; -.
DR EnsemblPlants; AT3G02250.1; AT3G02250.1; AT3G02250.
DR GeneID; 821223; -.
DR Gramene; AT3G02250.1; AT3G02250.1; AT3G02250.
DR KEGG; ath:AT3G02250; -.
DR Araport; AT3G02250; -.
DR TAIR; locus:2076552; AT3G02250.
DR eggNOG; ENOG502QRT0; Eukaryota.
DR HOGENOM; CLU_018420_0_0_1; -.
DR InParanoid; Q93ZR8; -.
DR OMA; CRANFNG; -.
DR OrthoDB; 477315at2759; -.
DR PhylomeDB; Q93ZR8; -.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q93ZR8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93ZR8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045489; P:pectin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd11299; O-FucT_plant; 1.
DR InterPro; IPR024709; FucosylTrfase_pln.
DR InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR Pfam; PF10250; O-FucT; 1.
DR PIRSF; PIRSF009360; UCP009360; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Fucose metabolism; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..512
FT /note="Rhamnogalacturonan I rhamnosyltransferase 1"
FT /id="PRO_0000442083"
FT TRANSMEM 41..63
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT BINDING 277..279
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 512 AA; 59731 MW; B8ED33F2D9219B88 CRC64;
MCKAEKFLYH RKLWEMKVKF LGDSKIDKLK NSLVLRSRMS LWMIRAMTIL LLWSCFVHLV
AVGEMWGPRL LKGWPSCFNH HDFPIAAEMT SLPMKIALPP KRIYQNNGYL MVSCNGGLNQ
MRAAICDMVT IARYMNVTLI VPELDKTSFW NDPSEFKDIF DVDHFISSLR DEVRILKELP
PRLKRRVRLG LYHTMPPISW SNMSYYQDQI LPLVKKYKVV HLNKTDTRLA NNELPVEIQK
LRCRANFNGL RFTPKIEELG RRVVKILREK GPFLVLHLRY EMDMLAFSGC SHGCNRYEEE
ELTRMRYAYP WWKEKVIDSE LKRKEGLCPL TPEETALTLS ALGIDRNVQI YIAAGEIYGG
KRRLKALTDV FPNVVRKETL LDSSDLSFCK NHSSQMAALD YLISLESDIF VPTYYGNMAK
VVEGHRRFLG FKKTIELNRK LLVKLIDEYY EGLLSWEVFS TTVKAFHATR MGGPKRRLVI
PNKPKEEDYF YANPYECLQL LHENNGNSLE ET
