ARAD2_ARATH
ID ARAD2_ARATH Reviewed; 443 AA.
AC Q9FLA5;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable arabinosyltransferase ARAD2;
DE EC=2.4.2.-;
DE AltName: Full=Arabinan alpha-1,5-arabinosyltransferase;
DE AltName: Full=L-Arabinosyltransferase;
DE AltName: Full=Protein ARABINAN DEFICIENT 2;
GN Name=ARAD2; OrderedLocusNames=At5g44930; ORFNames=K21C13.11;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 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 [6]
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. Cell
CC wall pectic arabinans are involved in thigmomorphogenesis response of
CC inflorescence stems to mechanical stress. {ECO:0000269|PubMed:22270560,
CC ECO:0000269|PubMed:23695504}.
CC -!- SUBUNIT: Homodimer and heterodimer with ARAD1.
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 -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
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DR EMBL; KJ138648; AHL38588.1; -; mRNA.
DR EMBL; AB010693; BAB10875.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95176.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95177.1; -; Genomic_DNA.
DR EMBL; AY048259; AAK82521.1; -; mRNA.
DR EMBL; BT002634; AAO11550.1; -; mRNA.
DR RefSeq; NP_199306.1; NM_123861.3.
DR RefSeq; NP_851132.1; NM_180801.2.
DR AlphaFoldDB; Q9FLA5; -.
DR BioGRID; 19772; 3.
DR IntAct; Q9FLA5; 1.
DR STRING; 3702.AT5G44930.1; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR PaxDb; Q9FLA5; -.
DR PRIDE; Q9FLA5; -.
DR ProteomicsDB; 244456; -.
DR EnsemblPlants; AT5G44930.1; AT5G44930.1; AT5G44930.
DR EnsemblPlants; AT5G44930.2; AT5G44930.2; AT5G44930.
DR GeneID; 834523; -.
DR Gramene; AT5G44930.1; AT5G44930.1; AT5G44930.
DR Gramene; AT5G44930.2; AT5G44930.2; AT5G44930.
DR KEGG; ath:AT5G44930; -.
DR Araport; AT5G44930; -.
DR TAIR; locus:2155302; AT5G44930.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_033763_1_1_1; -.
DR InParanoid; Q9FLA5; -.
DR OMA; RYFDYTH; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; Q9FLA5; -.
DR PRO; PR:Q9FLA5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLA5; baseline and differential.
DR Genevisible; Q9FLA5; AT.
DR GO; GO:0005794; C:Golgi apparatus; 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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0035884; P:arabinan biosynthetic process; IMP:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; 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..443
FT /note="Probable arabinosyltransferase ARAD2"
FT /id="PRO_0000429126"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..443
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 443 AA; 50997 MW; B85FF6F53095D98D CRC64;
MNPKIRKPNN SSSKKVTVSV LSVFLVFVFV NTFFYPSFYS DSGSIRRNLV DSRESFHFPG
NFRKTKVYMY ELPTNFTYGV IEQHGGEKSD DVTGLKYPGH QHMHEWYLYS DLTRPEVKRV
GSPIVRVFDP AEADLFYVSA FSSLSLIVDS GRPGFGYSDE EMQESLVSWL ESQEWWRRNN
GRDHVIVAGD PNALKRVMDR VKNAVLLVTD FDRLRADQGS LVKDVIIPYS HRIDAYEGEL
GVKQRTNLLF FMGNRYRKDG GKVRDLLFKL LEKEEDVVIK RGTQSRENMR AVKQGMHTSK
FCLHLAGDTS SACRLFDAIA SLCVPVIVSD GIELPFEDVI DYRKFSIFLR RDAALKPGFV
VKKLRKVKPG KILKYQKVMK EVRRYFDYTH LNGSVNEIWR QVTKKIPLIK LMINREKRMI
KRDGSDPQCS CLCSNQTGII HGV
