RRA2_ARATH
ID RRA2_ARATH Reviewed; 428 AA.
AC Q9C9Q5; Q8LCK7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Arabinosyltransferase RRA2 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000305};
DE AltName: Full=Protein REDUCED RESIDUAL ARABINOSE 1 {ECO:0000303|PubMed:17401635};
GN Name=RRA2 {ECO:0000303|PubMed:17401635};
GN OrderedLocusNames=At1g75110 {ECO:0000312|Araport:AT1G75110};
GN ORFNames=F9E10.4 {ECO:0000312|EMBL:AAG51917.1};
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 [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].
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17401635; DOI=10.1007/s11103-007-9162-y;
RA Egelund J., Obel N., Ulvskov P., Geshi N., Pauly M., Bacic A.,
RA Petersen B.L.;
RT "Molecular characterization of two Arabidopsis thaliana glycosyltransferase
RT mutants, rra1 and rra2, which have a reduced residual arabinose content in
RT a polymer tightly associated with the cellulosic wall residue.";
RL Plant Mol. Biol. 64:439-451(2007).
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).
CC -!- FUNCTION: Plays a role in the arabinosylation of cell wall components
CC (PubMed:17401635). Involved in the arabinosylation of extensin proteins
CC in root hair cells. Extensins are structural glycoproteins present in
CC cell walls and its arabinosylation is important for root hair cell
CC development (PubMed:21680836). {ECO:0000269|PubMed:17401635,
CC ECO:0000269|PubMed:21680836}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:21680836}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:21680836}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette and cauline leaves,
CC stems, flowers and siliques. {ECO:0000269|PubMed:17401635}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250|UniProtKB:Q9JI93}.
CC -!- DISRUPTION PHENOTYPE: Reduced arabinose content in the insoluble cell
CC wall fraction of meristematic region (PubMed:17401635). Reduced root
CC hair length and content of arabinosylated extensins in root cell walls
CC (PubMed:21680836). {ECO:0000269|PubMed:17401635,
CC ECO:0000269|PubMed:21680836}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 77 family.
CC {ECO:0000305}.
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DR EMBL; KJ138932; AHL38872.1; -; mRNA.
DR EMBL; AC013258; AAG51917.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35673.1; -; Genomic_DNA.
DR EMBL; AY039531; AAK62587.1; -; mRNA.
DR EMBL; AY102148; AAM26715.1; -; mRNA.
DR EMBL; AY086542; AAM63606.1; -; mRNA.
DR PIR; B96781; B96781.
DR RefSeq; NP_565102.1; NM_106167.3.
DR AlphaFoldDB; Q9C9Q5; -.
DR IntAct; Q9C9Q5; 1.
DR STRING; 3702.AT1G75110.1; -.
DR CAZy; GT77; Glycosyltransferase Family 77.
DR PaxDb; Q9C9Q5; -.
DR PRIDE; Q9C9Q5; -.
DR ProteomicsDB; 228210; -.
DR EnsemblPlants; AT1G75110.1; AT1G75110.1; AT1G75110.
DR GeneID; 843848; -.
DR Gramene; AT1G75110.1; AT1G75110.1; AT1G75110.
DR KEGG; ath:AT1G75110; -.
DR Araport; AT1G75110; -.
DR TAIR; locus:2037248; AT1G75110.
DR eggNOG; ENOG502QRD4; Eukaryota.
DR HOGENOM; CLU_037805_0_0_1; -.
DR InParanoid; Q9C9Q5; -.
DR OMA; FCESKEV; -.
DR OrthoDB; 996187at2759; -.
DR PhylomeDB; Q9C9Q5; -.
DR PRO; PR:Q9C9Q5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9Q5; baseline and differential.
DR Genevisible; Q9C9Q5; AT.
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: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 RRA2"
FT /id="PRO_0000434538"
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 250..252
FT /note="DXD motif"
FT /evidence="ECO:0000305"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 2
FT /note="A -> S (in Ref. 5; AAM63606)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="F -> L (in Ref. 5; AAM63606)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="I -> L (in Ref. 5; AAM63606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 48169 MW; D67FFFC470477086 CRC64;
MAGRRDRIQQ LRGSRIAIAI FVGILIGCVC SVLFPNGFFN SGSSLIANEE RISKSTSTDG
LASCESSERV KMLKSDFSII SVKNAELRKQ VRELTEKVRL AEQETENARK QVLVLGSEIK
AGPFGTVKSL RTNPTVVPDE SVNPRLAKLL EKVAVNKEII VVLANSNVKP MLELQIASVK
RVGIQNYLIV ALDDSMESFC ESKEVVFYKR DPDKAVDMVG KSGGNHAVSG LKFRVLREFL
QLGYSVLLSD VDIVFLQNPF SHLHRDSDVE SMSDGHDNNT AYGFNDVFDE PSMGWARYAH
TMRIWVFNSG FFYLRPTIPS IDLLDRVADT LSKSEAWDQA VFNEQLFYPS HPGYTGLHAS
KRVMDMYEFM NSKVLFKTVR KNQELKKLKP VIVHLNYHPD KLERMHAVVE FYVNGKQDAL
DSFPDGSD
