RRT3_ARATH
ID RRT3_ARATH Reviewed; 481 AA.
AC Q6E279; F4ISA5; O81046; Q6E278; Q84WS1;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Rhamnogalacturonan I rhamnosyltransferase 4 {ECO:0000303|PubMed:30082766};
DE EC=2.4.1.351 {ECO:0000269|PubMed:30082766};
DE AltName: Full=O-fucosyltransferase 18 {ECO:0000305};
DE Short=O-FucT-18 {ECO:0000305};
DE AltName: Full=O-fucosyltransferase family protein {ECO:0000312|EMBL:ARJ31420.1};
GN Name=RRT3 {ECO:0000303|PubMed:30082766}; Synonyms=OFUT18 {ECO:0000305};
GN OrderedLocusNames=At2g03280 {ECO:0000312|Araport:AT2G03280};
GN ORFNames=T18E12.4 {ECO:0000312|EMBL:AAM15036.1},
GN T4M8.29 {ECO:0000312|EMBL:AAD17446.1};
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] (ISOFORM 1).
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 1).
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] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RX PubMed=16244158; DOI=10.1104/pp.105.063479;
RA Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT reveals numerous transcript variants.";
RL Plant Physiol. 139:1323-1337(2005).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6E279-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6E279-2; Sequence=VSP_059170;
CC -!- SIMILARITY: Belongs to the glycosyltransferase GT106 family.
CC {ECO:0000305|PubMed:30082766}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD17446.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM15036.1; 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; KY906056; ARJ31420.1; -; mRNA.
DR EMBL; AC005313; AAM15036.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC006284; AAD17446.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC05682.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05683.1; -; Genomic_DNA.
DR EMBL; BT002839; AAO22658.1; -; mRNA.
DR EMBL; AY600544; AAT68343.1; -; mRNA.
DR EMBL; AY924736; AAX23811.1; -; mRNA.
DR EMBL; AY600545; AAT68344.1; -; mRNA.
DR PIR; T02698; T02698.
DR RefSeq; NP_001030963.1; NM_001035886.3. [Q6E279-2]
DR RefSeq; NP_178427.2; NM_126379.4. [Q6E279-1]
DR AlphaFoldDB; Q6E279; -.
DR STRING; 3702.AT2G03280.2; -.
DR PRIDE; Q6E279; -.
DR ProteomicsDB; 236201; -. [Q6E279-1]
DR EnsemblPlants; AT2G03280.1; AT2G03280.1; AT2G03280. [Q6E279-1]
DR EnsemblPlants; AT2G03280.2; AT2G03280.2; AT2G03280. [Q6E279-2]
DR GeneID; 814857; -.
DR Gramene; AT2G03280.1; AT2G03280.1; AT2G03280. [Q6E279-1]
DR Gramene; AT2G03280.2; AT2G03280.2; AT2G03280. [Q6E279-2]
DR KEGG; ath:AT2G03280; -.
DR Araport; AT2G03280; -.
DR TAIR; locus:2056981; AT2G03280.
DR eggNOG; ENOG502QT8R; Eukaryota.
DR HOGENOM; CLU_018420_0_0_1; -.
DR OMA; CLCESAR; -.
DR OrthoDB; 580218at2759; -.
DR PhylomeDB; Q6E279; -.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q6E279; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q6E279; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
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 Alternative splicing; Carbohydrate metabolism;
KW Cell wall biogenesis/degradation; Fucose metabolism; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..481
FT /note="Rhamnogalacturonan I rhamnosyltransferase 4"
FT /id="PRO_0000442080"
FT TRANSMEM 33..55
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT BINDING 258..260
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 135
FT /note="T -> TRYMFVSHVNDPTRFVCSLKHSFVSSFY (in isoform 2)"
FT /id="VSP_059170"
FT CONFLICT 15
FT /note="R -> W (in Ref. 4; AAO22658)"
FT /evidence="ECO:0000305"
FT CONFLICT Q6E279-2:136
FT /note="R -> G (in Ref. 5; AAT68344)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 55631 MW; 6C43190B50E75F16 CRC64;
MSVVVGDRSE STLMRSDYKA PPSQAIPKAR LQVWFFRVCS CILVWTCLIQ LFWHSQIFTG
LTNHISRFSL PVQSVPLPPP LPPRNYTSNG ILLVSCNGGL NQMRAAICDM VTVARLLNLT
LVVPELDKKS FWADTSDFED IFDIKHFIDS LRDEVRIIRR LPKRYSKKYG FKLFEMPPVS
WSNDKYYLQQ VLPRFSKRKV IHFVRSDTRL ANNGLSLDLQ RLRCRVNFQG LRFTPRIEAL
GSKLVRILQQ RGSFVALHLR YEMDMLAFSG CTHGCTDEEA EELKKMRYAY PWWREKEIVS
EERRVQGLCP LTPEEAVLVL KALGFQKDTQ IYIAAGEIFG GAKRLALLKE SFPRIVKKEM
LLDPTELQQF QNHSSQMAAL DFIVSVASNT FIPTYYGNMA KVVEGHRRYL GFKKTILLDR
KRLVELLDLH NNKTLSWDQF AVAVKDAHQG RRMGEPTHRK VISVRPKEED YFYANPQECI
S
