PAGR_ARATH
ID PAGR_ARATH Reviewed; 557 AA.
AC Q9LIN9; Q8LAU4;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein PECTIC ARABINOGALACTAN SYNTHESIS-RELATED {ECO:0000303|PubMed:27091363, ECO:0000312|EMBL:ARJ31430.1};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=O-fucosyltransferase 26 {ECO:0000305};
DE Short=O-FucT-26 {ECO:0000305};
DE AltName: Full=O-fucosyltransferase family protein {ECO:0000305};
GN Name=PAGR {ECO:0000303|PubMed:27091363, ECO:0000312|EMBL:ARJ31430.1};
GN Synonyms=OFUT26 {ECO:0000305};
GN OrderedLocusNames=At3g26370 {ECO:0000312|Araport:AT3G26370};
GN ORFNames=F20C19.9 {ECO:0000312|EMBL:BAB02197.1};
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;
RA Zeng W., Gluza P., Heazlewood J.;
RT "Arabidopsis glycosyltransferases: an update.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 216-557.
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 GENE FAMILY, AND REVIEW.
RX PubMed=22629278; DOI=10.3389/fpls.2012.00059;
RA Hansen S.F., Harholt J., Oikawa A., Scheller H.V.;
RT "Plant glycosyltransferases beyond CAZy: a perspective on DUF families.";
RL Front. Plant Sci. 3:59-59(2012).
RN [7]
RP GENE FAMILY.
RX PubMed=22916179; DOI=10.1371/journal.pone.0042914;
RA Neumetzler L., Humphrey T., Lumba S., Snyder S., Yeats T.H., Usadel B.,
RA Vasilevski A., Patel J., Rose J.K., Persson S., Bonetta D.;
RT "The FRIABLE1 gene product affects cell adhesion in Arabidopsis.";
RL PLoS ONE 7:E42914-E42914(2012).
RN [8]
RP GENE FAMILY.
RX PubMed=23272088; DOI=10.1371/journal.pone.0051129;
RA Voxeur A., Andre A., Breton C., Lerouge P.;
RT "Identification of putative rhamnogalacturonan-II specific
RT glycosyltransferases in Arabidopsis using a combination of bioinformatics
RT approaches.";
RL PLoS ONE 7:E51129-E51129(2012).
RN [9]
RP GENE FAMILY.
RX PubMed=22966747; DOI=10.1111/tpj.12019;
RA Wang Y., Mortimer J.C., Davis J., Dupree P., Keegstra K.;
RT "Identification of an additional protein involved in mannan biosynthesis.";
RL Plant J. 73:105-117(2013).
RN [10]
RP WEB RESOURCE.
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 [11]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27091363; DOI=10.1186/s12870-016-0780-x;
RA Stonebloom S., Ebert B., Xiong G., Pattathil S., Birdseye D., Lao J.,
RA Pauly M., Hahn M.G., Heazlewood J.L., Scheller H.V.;
RT "A DUF-246 family glycosyltransferase-like gene affects male fertility and
RT the biosynthesis of pectic arabinogalactans.";
RL BMC Plant Biol. 16:90-90(2016).
CC -!- FUNCTION: Glycosyltransferase involved in the biosynthesis of pectic
CC type-II arabinogalactans. {ECO:0000269|PubMed:27091363}.
CC -!- PATHWAY: Glycan metabolism; pectin biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:27091363}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed with the highest expression in
CC reproductive tissues and roots. {ECO:0000269|PubMed:27091363}.
CC -!- DISRUPTION PHENOTYPE: Homozygote mutants are non viable. Heterozygote
CC mutants display affected pollen germination.
CC {ECO:0000269|PubMed:27091363}.
CC -!- MISCELLANEOUS: Overexpression of PAGR positively affects the
CC biosynthesis of type-II arabinogalactans.
CC {ECO:0000269|PubMed:27091363}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase GT106 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=The Arabidopsis GT Collection;
CC URL="http://gt.jbei.org/arabidopsis.html";
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DR EMBL; KY906066; ARJ31430.1; -; mRNA.
DR EMBL; AP001298; BAB02197.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77150.1; -; Genomic_DNA.
DR EMBL; AK226720; BAE98825.1; -; mRNA.
DR EMBL; AY087604; AAM67369.1; -; mRNA.
DR RefSeq; NP_566791.2; NM_113544.5.
DR AlphaFoldDB; Q9LIN9; -.
DR IntAct; Q9LIN9; 83.
DR STRING; 3702.AT3G26370.1; -.
DR iPTMnet; Q9LIN9; -.
DR PaxDb; Q9LIN9; -.
DR PRIDE; Q9LIN9; -.
DR ProteomicsDB; 248632; -.
DR EnsemblPlants; AT3G26370.1; AT3G26370.1; AT3G26370.
DR GeneID; 822241; -.
DR Gramene; AT3G26370.1; AT3G26370.1; AT3G26370.
DR KEGG; ath:AT3G26370; -.
DR Araport; AT3G26370; -.
DR TAIR; locus:2079281; AT3G26370.
DR eggNOG; ENOG502QU4K; Eukaryota.
DR HOGENOM; CLU_018420_8_2_1; -.
DR InParanoid; Q9LIN9; -.
DR OMA; YSPKRAM; -.
DR OrthoDB; 476257at2759; -.
DR PhylomeDB; Q9LIN9; -.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q9LIN9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIN9; baseline and differential.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005797; C:Golgi medial cisterna; HDA: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:0052325; P:cell wall pectin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11299; O-FucT_plant; 1.
DR InterPro; IPR024709; FucosylTrfase_pln.
DR InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR Pfam; PF10250; O-FucT; 1.
DR PIRSF; PIRSF009360; UCP009360; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Fucose metabolism; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..557
FT /note="Protein PECTIC ARABINOGALACTAN SYNTHESIS-RELATED"
FT /id="PRO_0000442088"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 80..100
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT TOPO_DOM 101..557
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 336..338
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 557 AA; 63367 MW; 1B5AF482E9C04217 CRC64;
MAELRHSSSL GSRSSSSPLR AAGDEDSSSP HVHDHSPNGG DDEDGRPRHP SRDRDRPIWF
HSLFPFFGDD PRVSPQKNKI SLLLILILAI ASLISVYGII NHLNAPYLCK KDGIVLNCPH
VKESPSPWEN PLSATTSWKP CAERRIGGIS DLPPENETNG YVFIHAEGGL NQQRIAICNA
VAVAKIMNAT LILPVLKQDQ IWKDTTKFED IFDVDHFIDY LKDDVRIVRD IPDWFTDKAE
LFSSIRRTVK NIPKYAAAQF YIDNVLPRIK EKKIMALKPF VDRLGYDNVP QEINRLRCRV
NYHALKFLPE IEQMADSLVS RMRNRTGNPN PYMALHLRFE KGMVGLSFCD FVGTREEKVK
MAEYRQKEWP RRFKNGSHLW QLALQKRKEG RCPLEPGEVA VILRAMGYPK ETQIYVASGQ
VYGGQNRMAP LRNMFPNLVT KEDLAGKEEL TTFRKHVTSL AALDFLVCLK SDVFVMTHGG
NFAKLIIGAR RYMGHRQKSI KPDKGLMSKS FGDPYMGWAT FVEDVVVTHQ TRTGLPEETF
PNYDLWENPL TPCMCKA
