HPAT3_ARATH
ID HPAT3_ARATH Reviewed; 358 AA.
AC Q9FY51;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Hydroxyproline O-arabinosyltransferase 3 {ECO:0000303|PubMed:24036508};
DE EC=2.4.2.58 {ECO:0000269|PubMed:24036508};
GN Name=HPAT3 {ECO:0000303|PubMed:24036508};
GN OrderedLocusNames=At5g13500 {ECO:0000312|Araport:AT5G13500};
GN ORFNames=T6I14.30 {ECO:0000312|EMBL:CAC05427.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24036508; DOI=10.1038/nchembio.1351;
RA Ogawa-Ohnishi M., Matsushita W., Matsubayashi Y.;
RT "Identification of three hydroxyproline O-arabinosyltransferases in
RT Arabidopsis thaliana.";
RL Nat. Chem. Biol. 9:726-730(2013).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=25944827; DOI=10.1104/pp.114.255521;
RA Velasquez S.M., Marzol E., Borassi C., Pol-Fachin L., Ricardi M.M.,
RA Mangano S., Juarez S.P., Salter J.D., Dorosz J.G., Marcus S.E., Knox J.P.,
RA Dinneny J.R., Iusem N.D., Verli H., Estevez J.M.;
RT "Low sugar is not always good: impact of specific o-glycan defects on tip
RT growth in Arabidopsis.";
RL Plant Physiol. 168:808-813(2015).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26577059; DOI=10.1111/tpj.13079;
RA MacAlister C.A., Ortiz-Ramirez C., Becker J.D., Feijo J.A., Lippman Z.B.;
RT "Hydroxyproline O-arabinosyltransferase mutants oppositely alter tip growth
RT in Arabidopsis thaliana and Physcomitrella patens.";
RL Plant J. 85:193-208(2016).
CC -!- FUNCTION: Glycosyltransferase involved in the O-arabinosylation of
CC several proteins including extensins and small signaling peptides
CC (PubMed:24036508, PubMed:26577059). Catalyzes the transfer of the
CC initial L-arabinose to the hydroxyl group of Hyp residues
CC (PubMed:24036508). Contributes redundantly with HPAT1 and HPAT2 to
CC arabinosylation of EXT3, but main contributor to arabinosylation of CLE
CC peptides (PubMed:24036508). {ECO:0000269|PubMed:24036508,
CC ECO:0000269|PubMed:26577059}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=trans-4-hydroxy-L-prolyl-[protein] + UDP-beta-L-
CC arabinofuranose = H(+) + O-(beta-L-arabinofuranosyl)-trans-4-hydroxy-
CC L-prolyl-[protein] + UDP; Xref=Rhea:RHEA:49472, Rhea:RHEA-COMP:12408,
CC Rhea:RHEA-COMP:12409, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:61463, ChEBI:CHEBI:61965, ChEBI:CHEBI:131610;
CC EC=2.4.2.58; Evidence={ECO:0000269|PubMed:24036508};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:24036508}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:24036508}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but reduced level of
CC arabinosylation of EXT3 (PubMed:24036508). Short-root-hair phenotype
CC (PubMed:25944827). Hpat1 hpat3 double mutants have an impaired growth
CC of pollen tubes, thereby causing a transmisson defect through the male
CC gametophyte (PubMed:24036508, PubMed:26577059). Hpat1 hpat2 hpat3
CC triple mutants fail to produce detectable levels of Hyp-arabinosides,
CC have low fertility and shorter pollen tubes (PubMed:26577059).
CC {ECO:0000269|PubMed:24036508, ECO:0000269|PubMed:25944827,
CC ECO:0000269|PubMed:26577059}.
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DR EMBL; AL391710; CAC05427.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91903.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91904.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91905.1; -; Genomic_DNA.
DR EMBL; AY081351; AAL91240.1; -; mRNA.
DR EMBL; BT000256; AAN15575.1; -; mRNA.
DR EMBL; AY088436; AAM65972.1; -; mRNA.
DR RefSeq; NP_196854.1; NM_121353.4.
DR RefSeq; NP_850813.1; NM_180482.2.
DR RefSeq; NP_974777.1; NM_203048.2.
DR AlphaFoldDB; Q9FY51; -.
DR STRING; 3702.AT5G13500.1; -.
DR PaxDb; Q9FY51; -.
DR PRIDE; Q9FY51; -.
DR ProteomicsDB; 232087; -.
DR EnsemblPlants; AT5G13500.1; AT5G13500.1; AT5G13500.
DR EnsemblPlants; AT5G13500.2; AT5G13500.2; AT5G13500.
DR EnsemblPlants; AT5G13500.3; AT5G13500.3; AT5G13500.
DR GeneID; 831194; -.
DR Gramene; AT5G13500.1; AT5G13500.1; AT5G13500.
DR Gramene; AT5G13500.2; AT5G13500.2; AT5G13500.
DR Gramene; AT5G13500.3; AT5G13500.3; AT5G13500.
DR KEGG; ath:AT5G13500; -.
DR Araport; AT5G13500; -.
DR TAIR; locus:2185046; AT5G13500.
DR eggNOG; ENOG502QQNK; Eukaryota.
DR HOGENOM; CLU_065254_0_0_1; -.
DR InParanoid; Q9FY51; -.
DR OMA; TMIIHYG; -.
DR OrthoDB; 897130at2759; -.
DR PhylomeDB; Q9FY51; -.
DR BioCyc; ARA:AT5G13500-MON; -.
DR PRO; PR:Q9FY51; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FY51; baseline and differential.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
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:1990585; F:hydroxyproline O-arabinosyltransferase activity; IDA:TAIR.
DR GO; GO:0102562; F:hydroxyproline O-arbinofuranose transferase activity; IEA:RHEA.
DR InterPro; IPR044845; HPAT/SRGT1-like.
DR PANTHER; PTHR31485; PTHR31485; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..358
FT /note="Hydroxyproline O-arabinosyltransferase 3"
FT /id="PRO_0000437956"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 358 AA; 40333 MW; D9E307AC6F226379 CRC64;
MGKASGLLLF LLGFGFFVVT YNLLTLIVHN RSGVSNSDGS PLLDPVVQMP LNIRKAKSSP
APFHVALTAT DAPYNKWQCR IMYYWYKQKK ALPGSDMGGF TRILHSGNSD NLMDEIPTFV
VDPLPPGLDR GYVVLNRPWA FVQWLERATI KEDYVLMAEP DHVFVNPLPN LAVGGFPAAF
PFFYITPEKY ENIVRKYYPA EMGPVTNIDP IGNSPVIISK ESLEKIAPTW MNVSLTMKND
PETDKAFGWV LEMYGYAIAS AIHGVRHILR KDFMLQPPWD LSTKGKFIIH YTYGCDYNMK
GELTYGKIGE WRFDKRSHLR GPPPRNMSLP PPGVPESVVT LVKMVNEATA TIPNWDTL
