RRT4_ARATH
ID RRT4_ARATH Reviewed; 499 AA.
AC Q6NQ51; Q9LMF6; Q9XI85;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 3 {ECO:0000305};
DE Short=O-FucT-3 {ECO:0000305};
DE AltName: Full=O-fucosyltransferase family protein {ECO:0000305};
GN Name=RRT4 {ECO:0000303|PubMed:30082766}; Synonyms=OFUT3 {ECO:0000305};
GN OrderedLocusNames=At1g14020 {ECO:0000312|Araport:AT1G14020};
GN ORFNames=F16A14.24 {ECO:0000312|EMBL:AAF79406.1},
GN F7A19.11 {ECO:0000312|EMBL:AAD39288.1};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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=AAD39288.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF79406.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=The Arabidopsis GT Collection;
CC URL="http://gt.jbei.org/arabidopsis.html";
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DR EMBL; AC007576; AAD39288.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC068197; AAF79406.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29099.1; -; Genomic_DNA.
DR EMBL; BT010612; AAQ89634.1; -; mRNA.
DR EMBL; AK229836; BAF01665.1; -; mRNA.
DR EMBL; AK229994; BAF01818.1; -; mRNA.
DR PIR; E86273; E86273.
DR RefSeq; NP_172855.2; NM_101268.3.
DR AlphaFoldDB; Q6NQ51; -.
DR IntAct; Q6NQ51; 89.
DR STRING; 3702.AT1G14020.1; -.
DR iPTMnet; Q6NQ51; -.
DR PaxDb; Q6NQ51; -.
DR PRIDE; Q6NQ51; -.
DR ProteomicsDB; 236202; -.
DR EnsemblPlants; AT1G14020.1; AT1G14020.1; AT1G14020.
DR GeneID; 837963; -.
DR Gramene; AT1G14020.1; AT1G14020.1; AT1G14020.
DR KEGG; ath:AT1G14020; -.
DR Araport; AT1G14020; -.
DR TAIR; locus:2014869; AT1G14020.
DR eggNOG; ENOG502QT8R; Eukaryota.
DR HOGENOM; CLU_018420_0_0_1; -.
DR InParanoid; Q6NQ51; -.
DR OMA; WFVRVCS; -.
DR OrthoDB; 580218at2759; -.
DR PhylomeDB; Q6NQ51; -.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q6NQ51; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NQ51; 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..499
FT /note="Rhamnogalacturonan I rhamnosyltransferase 1"
FT /id="PRO_0000442066"
FT TRANSMEM 31..50
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT BINDING 261..263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 499 AA; 57571 MW; 246CFD271E474D8C CRC64;
MEVRSESNIT QARSDKLPLP PAVPKPRVQV WFVRVCSSIL VWTCLVQLFA AGELWHSRIF
TGLTNQISRF SAPVEPVPLP PPLPPPRNYT SNGILLVSCN GGLNQMRSAI CDMVTVARLL
NLTLVVPELD KTSFWADPSG FEDIFDVRHF IDSLRDEVRI LRRLPKRFSR KYGYQMFEMP
PVSWSDEKYY LKQVLPLFSK HKVVHFNRTD TRLANNGLPL SLQWLRCRVN FQGLKFTPQL
EALGSKLVRI LQQRGPFVAL HLRYEMDMLA FSGCTHGCTE EEAEELKKMR YTYPWWREKE
IVSEERRAQG LCPLTPEEVA LVLKALGFEK NTQIYIAAGE IYGSEHRLSV LREAFPRIVK
KEMLLESAEL QQFQNHSSQM AALDFMVSVA SNTFIPTYDG NMAKVVEGHR RYLGYKKTIL
LDRKRLVELL DLHHNKTLTW DQFAVAVKEA HERRAGAPTH RRVISDKPKE EDYFYANPQE
CLCEGTNCHD LFGHRNLTH
