RRA1_ARATH
ID RRA1_ARATH Reviewed; 402 AA.
AC Q9C9Q6; Q84R12;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Arabinosyltransferase RRA1 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000305};
DE AltName: Full=Protein REDUCED RESIDUAL ARABINOSE 1 {ECO:0000303|PubMed:17401635};
GN Name=RRA1 {ECO:0000303|PubMed:17401635};
GN OrderedLocusNames=At1g75120 {ECO:0000312|Araport:AT1G75120};
GN ORFNames=F9E10.3 {ECO:0000312|EMBL:AAG51930.1};
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].
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 GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, 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 [8]
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 leaf meristem and at points of cauline
CC leaf attachments on the primary stem. Expressed at low levels in
CC 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; KJ138931; AHL38871.1; -; mRNA.
DR EMBL; AC013258; AAG51930.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35674.1; -; Genomic_DNA.
DR EMBL; BT006179; AAP04162.1; -; mRNA.
DR EMBL; AK228598; BAF00513.1; -; mRNA.
DR EMBL; BT026432; ABH04539.1; -; mRNA.
DR PIR; C96781; C96781.
DR RefSeq; NP_177648.1; NM_106168.3.
DR AlphaFoldDB; Q9C9Q6; -.
DR STRING; 3702.AT1G75120.1; -.
DR CAZy; GT77; Glycosyltransferase Family 77.
DR PaxDb; Q9C9Q6; -.
DR PRIDE; Q9C9Q6; -.
DR ProteomicsDB; 228209; -.
DR EnsemblPlants; AT1G75120.1; AT1G75120.1; AT1G75120.
DR GeneID; 843849; -.
DR Gramene; AT1G75120.1; AT1G75120.1; AT1G75120.
DR KEGG; ath:AT1G75120; -.
DR Araport; AT1G75120; -.
DR TAIR; locus:2037273; AT1G75120.
DR eggNOG; ENOG502QRD4; Eukaryota.
DR HOGENOM; CLU_037805_0_0_1; -.
DR InParanoid; Q9C9Q6; -.
DR OMA; NRTAYGY; -.
DR OrthoDB; 996187at2759; -.
DR PhylomeDB; Q9C9Q6; -.
DR PRO; PR:Q9C9Q6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9Q6; baseline and differential.
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 Gene3D; 3.90.550.10; -; 1.
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..402
FT /note="Arabinosyltransferase RRA1"
FT /id="PRO_0000434537"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..402
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 225..227
FT /note="DXD motif"
FT /evidence="ECO:0000305"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 168
FT /note="D -> Y (in Ref. 4; AAP04162 and 5; BAF00513)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 45475 MW; 20B223E8AA23F377 CRC64;
MAVRKEKVQP FRECGIAIAV LVGIFIGCVC TILIPNDFVN FRSSKVASAS CESPERVKMF
KAEFAIISEK NGELRKQVSD LTEKVRLAEQ KEVIKAGPFG TVTGLQTNPT VAPDESANPR
LAKLLEKVAV NKEIIVVLAN NNVKPMLEVQ IASVKRVGIQ NYLVVPLDDS LESFCKSNEV
AYYKRDPDNA IDVVGKSRRS SDVSGLKFRV LREFLQLGYG VLLSDVDIVF LQNPFGHLYR
DSDVESMSDG HDNNTAYGFN DVFDDPTMTR SRTVYTNRIW VFNSGFFYLR PTLPSIELLD
RVTDTLSKSG GWDQAVFNQH LFYPSHPGYT GLYASKRVMD VYEFMNSRVL FKTVRKDEEM
KKLKPVIIHM NYHSDKLERM QAAVEFYVNG KQDALDRFRD GS
