HPAT1_ARATH
ID HPAT1_ARATH Reviewed; 366 AA.
AC Q8W4E6;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Hydroxyproline O-arabinosyltransferase 1 {ECO:0000303|PubMed:24036508};
DE EC=2.4.2.58 {ECO:0000269|PubMed:24036508};
GN Name=HPAT1 {ECO:0000303|PubMed:24036508};
GN OrderedLocusNames=At5g25265 {ECO:0000312|Araport:AT5G25265};
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 {ECO:0000312|EMBL:AAL32685.1};
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].
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 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 HPAT2 and HPAT3 to
CC arabinosylation of EXT3 (PubMed:24036508).
CC {ECO:0000269|PubMed:24036508, 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 (PubMed:24036508). Short-
CC root-hair phenotype (PubMed:25944827). Hpat1 hpat2 double mutants have
CC longer hypocotyls, are early flowering and show early senescence in
CC leaves associated with a decrease in chlorophyll content
CC (PubMed:24036508). Hpat1 hpat3 double mutants have an impaired growth
CC of pollen tubes, thereby causing a transmisson defect through the male
CC gametophyte (PubMed:24036508). Hpat1 hpat2 hpat3 triple mutants fail to
CC produce detectable levels of Hyp-arabinosides, have low fertility and
CC shorter pollen tubes (PubMed:26577059). {ECO:0000269|PubMed:24036508,
CC ECO:0000269|PubMed:25944827, ECO:0000269|PubMed:26577059}.
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DR EMBL; AC006259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93419.1; -; Genomic_DNA.
DR EMBL; AY062607; AAL32685.1; -; mRNA.
DR EMBL; BT008447; AAP37806.1; -; mRNA.
DR EMBL; AK230260; BAF02062.1; -; mRNA.
DR RefSeq; NP_680219.1; NM_147914.4.
DR AlphaFoldDB; Q8W4E6; -.
DR STRING; 3702.AT5G25265.1; -.
DR SwissPalm; Q8W4E6; -.
DR PaxDb; Q8W4E6; -.
DR PRIDE; Q8W4E6; -.
DR ProteomicsDB; 232171; -.
DR EnsemblPlants; AT5G25265.1; AT5G25265.1; AT5G25265.
DR GeneID; 832598; -.
DR Gramene; AT5G25265.1; AT5G25265.1; AT5G25265.
DR KEGG; ath:AT5G25265; -.
DR Araport; AT5G25265; -.
DR TAIR; locus:504955105; AT5G25265.
DR eggNOG; ENOG502QQNK; Eukaryota.
DR HOGENOM; CLU_065254_0_0_1; -.
DR InParanoid; Q8W4E6; -.
DR OMA; KFFPEHE; -.
DR OrthoDB; 897130at2759; -.
DR PhylomeDB; Q8W4E6; -.
DR BioCyc; ARA:AT5G25265-MON; -.
DR BioCyc; MetaCyc:AT5G25265-MON; -.
DR PRO; PR:Q8W4E6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W4E6; baseline and differential.
DR GO; GO:0005801; C:cis-Golgi network; IDA:TAIR.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005797; C:Golgi medial cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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..366
FT /note="Hydroxyproline O-arabinosyltransferase 1"
FT /id="PRO_0000437954"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 366 AA; 40973 MW; 9482ED959B68123C CRC64;
MGCGGTLFYP LLITLSVALI TYNIIISANA PLKQGFPGRS SSSDISIDPV IELPRGGGSR
NNDGKRIRLF HTAVTASDSV YNTWQCRVMY YWFKKIQASA GPGSEMGGFT RILHSGKPDQ
YMDEIPTFVA QPLPSGMDQG YVVLNRPWAF VQWLQQTDIK EDYILMSEPD HIIVKPIPNL
AKDGLGAAFP FFYIEPKKYE KVLRKYYPEV RGPVTNIDPI GNSPVIVGKD ALKKIAPTWM
NVSLAMKKDP EADKAFGWVL EMYAYAVSSA LHGVSNILHK DFMIQPPWDI EVGDKYIIHY
TYGCDYDMKG KLTYGKIGEW RFDKRSYDSK PPPRNLTMPP PGVSQSVVTL VKMINEATAN
IPNWGS
