RRA3_ARATH
ID RRA3_ARATH Reviewed; 428 AA.
AC Q9LN62;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Arabinosyltransferase RRA3 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000305};
DE AltName: Full=Protein REDUCED RESIDUAL ARABINOSE 3 {ECO:0000303|PubMed:21680836};
GN Name=RRA3 {ECO:0000303|PubMed:21680836};
GN OrderedLocusNames=At1g19360 {ECO:0000312|Araport:AT1G19360};
GN ORFNames=F18O14.8 {ECO:0000312|EMBL:AAF79453.1};
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 NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21680836; DOI=10.1126/science.1206657;
RA Velasquez S.M., Ricardi M.M., Dorosz J.G., Fernandez P.V., Nadra A.D.,
RA Pol-Fachin L., Egelund J., Gille S., Harholt J., Ciancia M., Verli H.,
RA Pauly M., Bacic A., Olsen C.E., Ulvskov P., Petersen B.L., Somerville C.,
RA Iusem N.D., Estevez J.M.;
RT "O-glycosylated cell wall proteins are essential in root hair growth.";
RL Science 332:1401-1403(2011).
RN [8]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=25944827; DOI=10.1104/pp.114.255521;
RA Velasquez S.M., Marzol E., Borassi C., Pol-Fachin L., Ricardi M.M.,
RA Mangano S., Juarez S.P., Salter J.D., Dorosz J.G., Marcus S.E., Knox J.P.,
RA Dinneny J.R., Iusem N.D., Verli H., Estevez J.M.;
RT "Low sugar is not always good: impact of specific o-glycan defects on tip
RT growth in Arabidopsis.";
RL Plant Physiol. 168:808-813(2015).
CC -!- FUNCTION: Plays a role in the arabinosylation of cell wall components.
CC Involved in the arabinosylation of extensin proteins in root hair cells
CC (PubMed:21680836). Extensins are structural glycoproteins present in
CC cell walls and its arabinosylation is important for root hair cell
CC development and root hair tip growth (PubMed:21680836,
CC PubMed:25944827). {ECO:0000269|PubMed:21680836,
CC ECO:0000269|PubMed:25944827}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:21680836}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:21680836}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250|UniProtKB:Q9JI93}.
CC -!- DISRUPTION PHENOTYPE: Reduced root hair length and content of
CC arabinosylated extensins in root cell walls.
CC {ECO:0000269|PubMed:21680836}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 77 family.
CC {ECO:0000305}.
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DR EMBL; KJ138999; AHL38939.1; -; mRNA.
DR EMBL; AC025808; AAF79453.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29839.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59303.1; -; Genomic_DNA.
DR EMBL; BT025990; ABG25079.1; -; mRNA.
DR EMBL; AK229032; BAF00917.1; -; mRNA.
DR EMBL; AY088117; AAM65662.1; -; mRNA.
DR RefSeq; NP_001321670.1; NM_001332391.1.
DR RefSeq; NP_564082.1; NM_101793.4.
DR AlphaFoldDB; Q9LN62; -.
DR STRING; 3702.AT1G19360.1; -.
DR CAZy; GT77; Glycosyltransferase Family 77.
DR iPTMnet; Q9LN62; -.
DR SwissPalm; Q9LN62; -.
DR PaxDb; Q9LN62; -.
DR PRIDE; Q9LN62; -.
DR ProteomicsDB; 228200; -.
DR EnsemblPlants; AT1G19360.1; AT1G19360.1; AT1G19360.
DR EnsemblPlants; AT1G19360.2; AT1G19360.2; AT1G19360.
DR GeneID; 838519; -.
DR Gramene; AT1G19360.1; AT1G19360.1; AT1G19360.
DR Gramene; AT1G19360.2; AT1G19360.2; AT1G19360.
DR KEGG; ath:AT1G19360; -.
DR Araport; AT1G19360; -.
DR TAIR; locus:2016487; AT1G19360.
DR eggNOG; ENOG502QRD4; Eukaryota.
DR HOGENOM; CLU_037805_0_0_1; -.
DR InParanoid; Q9LN62; -.
DR OMA; DHAHEQF; -.
DR OrthoDB; 996187at2759; -.
DR PhylomeDB; Q9LN62; -.
DR PRO; PR:Q9LN62; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LN62; baseline and differential.
DR Genevisible; Q9LN62; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:TAIR.
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:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0080147; P:root hair cell development; IMP:TAIR.
DR InterPro; IPR005069; Nucl-diP-sugar_transferase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR044290; RRA1/2/3.
DR PANTHER; PTHR46581; PTHR46581; 1.
DR Pfam; PF03407; Nucleotid_trans; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..428
FT /note="Arabinosyltransferase RRA3"
FT /id="PRO_0000434539"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..428
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 249..251
FT /note="DXD motif"
FT /evidence="ECO:0000305"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 428 AA; 48251 MW; 143DDB43473F0353 CRC64;
MAGRRDRSQQ LRGSRIAIAI LIGIFIGCVC AVLFPYGFFN SSSSLKASEH LSKSSNQVGS
SACESPERVK MLKSDFVTLS EKNAELKKQV RELTEKLRLA EQGSDNARKQ VLALGTQIKA
GPFGTVKSLR TNPTILPDES INPRLAKILE EIAVDKEVIV ALANANVKAM LEVQIASIKR
VGITNYLVVA LDDYIENLCK ENDVAYYKRD PDKDVDTVGK TGGNHAVSGL KFRVLREFLQ
LGYGVLLSDV DIVFLQNPFS HLYRDSDVES MSDGHDNHTA YGFNDVFDEP AMGWARYAHT
MRIWVFNSGF FYLRPTIPSI ELLDRVADRL SKAKVWDQAV FNEELFYPSH PEYTALHASK
RVMDMYEFMN SKVLFKTVRK NHELKKKVKP VIVHVNYHPD KLNRMQAVVE FYVNGKQDAL
DSFPDGSE
