RRT1_ARATH
ID RRT1_ARATH Reviewed; 508 AA.
AC Q4V398; Q9LFV2;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 34 {ECO:0000305};
DE Short=O-FucT-34 {ECO:0000305};
DE AltName: Full=O-fucosyltransferase family protein {ECO:0000312|EMBL:ARJ31449.1};
GN Name=RRT1 {ECO:0000303|PubMed:30082766}; Synonyms=OFUT34 {ECO:0000305};
GN OrderedLocusNames=At5g15740 {ECO:0000312|Araport:AT5G15740};
GN ORFNames=F14F8.120 {ECO:0000312|EMBL:CAC01773.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) 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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
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 (PubMed:30082766).
CC Transfers the rhamnose residue from UDP-beta-L-rhamnose to RG-I
CC oligosaccharides (PubMed:30082766). Prefers RG-I oligosaccharides with
CC a degree of polymerization of 5 or larger than 5 (PubMed:30082766).
CC Does not act on oligosaccharides with a degree of polymerization of 4
CC or smaller than 4 (PubMed:30082766). Does not require metal ions for
CC its activity (PubMed:30082766). {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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:30082766};
CC -!- PATHWAY: Glycan metabolism; pectin biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:30082766}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in siliques (PubMed:30082766).
CC Expressed in stems and flowers (PubMed:30082766). Expressed at low
CC levels in roots and rosette leaves (PubMed:30082766).
CC {ECO:0000269|PubMed:30082766}.
CC -!- DEVELOPMENTAL STAGE: During seed coat development, expressed from
CC linear cotyledon to mature green stages, with a peak at the bent
CC cotyledon stage. {ECO:0000269|PubMed:30082766}.
CC -!- DISRUPTION PHENOTYPE: Reduced volume of the seed coat mucilage due to
CC reduced levels of rhamnogalacturonan I (RG-I) in the seed coat
CC mucilage. {ECO:0000269|PubMed:30082766}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase GT106 family.
CC {ECO:0000305|PubMed:30082766}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01773.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=The Arabidopsis GT Collection;
CC URL="http://gt.jbei.org/arabidopsis.html";
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DR EMBL; KY906085; ARJ31449.1; -; mRNA.
DR EMBL; AL391144; CAC01773.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED92200.1; -; Genomic_DNA.
DR EMBL; BT023458; AAY56449.1; -; mRNA.
DR EMBL; AK227710; BAE99696.1; -; mRNA.
DR PIR; T51403; T51403.
DR RefSeq; NP_197078.2; NM_121579.4.
DR AlphaFoldDB; Q4V398; -.
DR STRING; 3702.AT5G15740.1; -.
DR PaxDb; Q4V398; -.
DR PRIDE; Q4V398; -.
DR ProteomicsDB; 236199; -.
DR EnsemblPlants; AT5G15740.1; AT5G15740.1; AT5G15740.
DR GeneID; 831430; -.
DR Gramene; AT5G15740.1; AT5G15740.1; AT5G15740.
DR KEGG; ath:AT5G15740; -.
DR Araport; AT5G15740; -.
DR TAIR; locus:2143181; AT5G15740.
DR eggNOG; ENOG502QRT0; Eukaryota.
DR HOGENOM; CLU_018420_0_0_1; -.
DR InParanoid; Q4V398; -.
DR OMA; WDVFSST; -.
DR OrthoDB; 477315at2759; -.
DR PhylomeDB; Q4V398; -.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q4V398; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q4V398; 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:0008194; F:UDP-glycosyltransferase activity; IDA:TAIR.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045489; P:pectin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0010395; P:rhamnogalacturonan I metabolic process; IDA:TAIR.
DR GO; GO:0010214; P:seed coat development; IMP:TAIR.
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..508
FT /note="Rhamnogalacturonan I rhamnosyltransferase 1"
FT /id="PRO_0000442096"
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 508 AA; 59041 MW; D3964044E8948431 CRC64;
MCKMEKFLYH RKLWEMNVKL LGESKVEKLK NSFVSRPRMS LWMIRAVTVL LLWSCFVHLM
ALGEMWGPRL FKGWPSCFNH HQLSTAAEMT SLPTKIALPP KRVYVNNGYL MVSCNGGLNQ
MRAAICDMVT VARYMNVTLI VPELDKTSFW NDPSEFKDIF DVDHFISSLR DEVRILKELP
PRLKKRVELG VYHEMPPISW SNMSYYQNQI LPLVKKHKVL HLNRTDTRLA NNGLPVEVQK
LRCRVNFNGL KFTPQIEELG RRVVKILREK GPFLVLHLRY EMDMLAFSGC SHGCNPEEEE
ELTRMRYAYP WWKEKVINSE LKRKDGLCPL TPEETALTLT ALGIDRNVQI YIAAGEIYGG
QRRMKALTDA FPNVVRKETL LESSDLDFCR NHSSQMAALD YLVALESDIF VPTNDGNMAR
VVEGHRRFLG FKKTIQLNRR FLVKLIDEYT EGLLSWDVFS STVKAFHSTR MGSPKRRLVI
PNRPKEEDYF YANPQECLQL LDEPLRVI
