ARAD1_ARATH
ID ARAD1_ARATH Reviewed; 447 AA.
AC Q6DBG8; O82181;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable arabinosyltransferase ARAD1;
DE EC=2.4.2.-;
DE AltName: Full=Arabinan alpha-1,5-arabinosyltransferase;
DE AltName: Full=L-Arabinosyltransferase;
DE AltName: Full=Protein ARABINAN DEFICIENT 1;
GN Name=ARAD1; OrderedLocusNames=At2g35100; ORFNames=T4C15;
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;
RA Lao J., Oikawa A., Bromley J.R., Smith-Moritz A.M., Chiu T.-Y.,
RA Christiansen K.M., Hansen S.F., Suttangkakul A., Ebert B., Yang F.,
RA Vega-Sanchez M.E., Stonebloom S., Morrison S., McInerney P., Hadi M.,
RA Adams P.D., Ronald P.C., Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for high-throughput
RT functional genomics.";
RL Submitted (JAN-2014) 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].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) 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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16377743; DOI=10.1104/pp.105.072744;
RA Harholt J., Jensen J.K., Sorensen S.O., Orfila C., Pauly M., Scheller H.V.;
RT "ARABINAN DEFICIENT 1 is a putative arabinosyltransferase involved in
RT biosynthesis of pectic arabinan in Arabidopsis.";
RL Plant Physiol. 140:49-58(2006).
RN [7]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=22270560; DOI=10.1007/s00425-012-1592-3;
RA Harholt J., Jensen J.K., Verhertbruggen Y., Sogaard C., Bernard S.,
RA Nafisi M., Poulsen C.P., Geshi N., Sakuragi Y., Driouich A., Knox J.P.,
RA Scheller H.V.;
RT "ARAD proteins associated with pectic Arabinan biosynthesis form complexes
RT when transiently overexpressed in planta.";
RL Planta 236:115-128(2012).
RN [8]
RP FUNCTION.
RX PubMed=23695504; DOI=10.1093/pcp/pct074;
RA Verhertbruggen Y., Marcus S.E., Chen J., Knox J.P.;
RT "Cell wall pectic arabinans influence the mechanical properties of
RT Arabidopsis thaliana inflorescence stems and their response to mechanical
RT stress.";
RL Plant Cell Physiol. 54:1278-1288(2013).
CC -!- FUNCTION: Probable arabinosyl transferase responsible for the
CC polymerization of arabinose into the arabinan of arabinogalactan. May
CC function as inverting enzyme using UDP-beta-L-arabinopyranoside. May be
CC important for arabinan side chains of rhamnogalacturonan I (RG-I), a
CC major component of pectins. Cell wall pectic arabinans are involved in
CC thigmomorphogenesis response of inflorescence stems to mechanical
CC stress. {ECO:0000269|PubMed:16377743, ECO:0000269|PubMed:22270560,
CC ECO:0000269|PubMed:23695504}.
CC -!- SUBUNIT: Homodimer and heterodimer with ARAD2.
CC {ECO:0000269|PubMed:22270560}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:22270560}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in root vasculature, cotyledons, leaves,
CC stems, vascular tissue of sepals, petals and stamens, pollen grains,
CC mature siliques and abscission region of seeds.
CC {ECO:0000269|PubMed:16377743}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have strong reduction of arabinose
CC content in leaves and stems due to a decreased content of pectic
CC arabinan. {ECO:0000269|PubMed:16377743}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC61825.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KJ138874; AHL38814.1; -; mRNA.
DR EMBL; AC004667; AAC61825.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09064.1; -; Genomic_DNA.
DR EMBL; BT015054; AAT71926.1; -; mRNA.
DR EMBL; BT015854; AAU94417.1; -; mRNA.
DR EMBL; AK228986; BAF00874.1; -; mRNA.
DR PIR; F84764; F84764.
DR RefSeq; NP_850241.1; NM_179910.3.
DR AlphaFoldDB; Q6DBG8; -.
DR BioGRID; 3422; 2.
DR STRING; 3702.AT2G35100.1; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR PaxDb; Q6DBG8; -.
DR PRIDE; Q6DBG8; -.
DR ProteomicsDB; 246953; -.
DR EnsemblPlants; AT2G35100.1; AT2G35100.1; AT2G35100.
DR GeneID; 818076; -.
DR Gramene; AT2G35100.1; AT2G35100.1; AT2G35100.
DR KEGG; ath:AT2G35100; -.
DR Araport; AT2G35100; -.
DR TAIR; locus:2063494; AT2G35100.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_033763_1_1_1; -.
DR InParanoid; Q6DBG8; -.
DR OMA; LERQPYW; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; Q6DBG8; -.
DR PRO; PR:Q6DBG8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q6DBG8; baseline and differential.
DR Genevisible; Q6DBG8; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; IDA:TAIR.
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; ISS:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045489; P:pectin biosynthetic process; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR040911; Exostosin_GT47.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR Pfam; PF03016; Exostosin; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..447
FT /note="Probable arabinosyltransferase ARAD1"
FT /id="PRO_0000429125"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..447
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 32..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 447 AA; 50782 MW; BD81FEB4E56C338A CRC64;
MARKSSLLKR AAIAVVSVIA IYVILNASVS RSLPSSSDLP RQLIREDDDD EGRAPIQPRV
RVYMYNLPKR FTYGLIEQHS IARGGIKKPV GDVTTLKYPG HQHMHEWYLF SDLNQPEVDR
SGSPIVRVSD PADADLFYVP VFSSLSLIVN AGRPVEAGSG YSDEKMQEGL VEWLEGQEWW
RRNAGRDHVI PAGDPNALYR ILDRVKNAVL LVSDFGRLRP DQGSFVKDVV IPYSHRVNLF
NGEIGVEDRN TLLFFMGNRY RKDGGKVRDL LFQVLEKEDD VTIKHGTQSR ENRRAATKGM
HTSKFCLNPA GDTPSACRLF DSIVSLCVPL IVSDSIELPF EDVIDYRKFS IFVEANAALQ
PGFLVQMLRK IKTKKILEYQ REMKSVRRYF DYDNPNGAVK EIWRQVSHKL PLIKLMSNRD
RRLVLRNLTE PNCSCLCTNQ TGLITSI
