HPAT2_ARATH
ID HPAT2_ARATH Reviewed; 358 AA.
AC Q494Q2; Q9SIR7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Hydroxyproline O-arabinosyltransferase 2 {ECO:0000303|PubMed:24036508};
DE EC=2.4.2.58 {ECO:0000269|PubMed:24036508};
GN Name=HPAT2 {ECO:0000303|PubMed:24036508};
GN OrderedLocusNames=At2g25260 {ECO:0000312|Araport:AT2G25260};
GN ORFNames=T22F11.15 {ECO:0000312|EMBL:AAD23665.1};
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 {ECO:0000312|EMBL:AAZ23916.1};
RN [1]
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 [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 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 [5]
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 [6]
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 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 hpat2 hpat3 triple mutants fail to produce
CC detectable levels of Hyp-arabinosides, have low fertility and shorter
CC pollen tubes (PubMed:26577059). {ECO:0000269|PubMed:24036508,
CC ECO:0000269|PubMed:25944827, ECO:0000269|PubMed:26577059}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD23665.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007070; AAD23665.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07677.1; -; Genomic_DNA.
DR EMBL; BT023724; AAZ23916.1; -; mRNA.
DR PIR; C84646; C84646.
DR RefSeq; NP_180098.3; NM_128083.4.
DR AlphaFoldDB; Q494Q2; -.
DR STRING; 3702.AT2G25260.1; -.
DR PaxDb; Q494Q2; -.
DR PRIDE; Q494Q2; -.
DR ProteomicsDB; 232172; -.
DR EnsemblPlants; AT2G25260.1; AT2G25260.1; AT2G25260.
DR GeneID; 817064; -.
DR Gramene; AT2G25260.1; AT2G25260.1; AT2G25260.
DR KEGG; ath:AT2G25260; -.
DR Araport; AT2G25260; -.
DR TAIR; locus:2059573; AT2G25260.
DR eggNOG; ENOG502QQNK; Eukaryota.
DR HOGENOM; CLU_065254_0_0_1; -.
DR InParanoid; Q494Q2; -.
DR OMA; FPILMTL; -.
DR OrthoDB; 897130at2759; -.
DR PhylomeDB; Q494Q2; -.
DR BioCyc; ARA:AT2G25260-MON; -.
DR PRO; PR:Q494Q2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q494Q2; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 2"
FT /id="PRO_0000437955"
FT TRANSMEM 7..26
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 358 AA; 40972 MW; 5896BC313B08B721 CRC64;
MGFRGKYFFP ILMTLSLFLI IRYNYIVSDD PPLRQELPGR RSASSGDDIT YTVKTPSKKT
KRLFHTAVTA TDSVYSTWQC RVMYYWYNRF RDEPGSDMGG YTRILHSGRP DGLMDEIPTF
VADPLPSGVD KGYVVLNRPW AFVQWLQQAH IEEDYILMAE PDHIIVKPIP NLARGNLAAA
FPFFYIEPKK YESVLRKFFP KENGPISRID PIGNSPVIVT KNALMKIAPT WMNVSLAMKN
DPQTDKAFGW VLEMYAYAVS SALHGVSNIL HKDFMIQPPW DTETKKTFII HYTYGCDFDM
KGKMMVGKIG EWRFDKRSYG DKPPPRNLTL PPRGVPESVV TLVTMINEAT ANIPNWES
