XTH24_ARATH
ID XTH24_ARATH Reviewed; 269 AA.
AC P24806; O64956; Q39148; Q39149; Q41904; Q8LDQ0;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase protein 24;
DE Short=At-XTH24;
DE Short=XTH-24;
DE EC=2.4.1.207;
DE AltName: Full=Endo-xyloglucan transferase;
DE AltName: Full=Meristem protein 5;
DE Short=MERI-5 protein;
DE Short=MERI5 protein;
DE AltName: Full=Xyloglucan endo-1,4-beta-D-glucanase;
DE Flags: Precursor;
GN Name=XTH24; Synonyms=MERI-5, MERI5B, SEN4; OrderedLocusNames=At4g30270;
GN ORFNames=F9N11.120;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=1840916; DOI=10.2307/3869211;
RA Medford J.I., Elmer J.S., Klee H.J.;
RT "Molecular cloning and characterization of genes expressed in shoot apical
RT meristems.";
RL Plant Cell 3:359-370(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Kamimai T., Tomita E., Nishitani K.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-132.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-120.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=9617812; DOI=10.1023/a:1005958300951;
RA Park J.-H., Oh S.A., Kim Y.H., Woo H.R., Nam H.G.;
RT "Differential expression of senescence-associated mRNAs during leaf
RT senescence induced by different senescence-inducing factors in
RT Arabidopsis.";
RL Plant Mol. Biol. 37:445-454(1998).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 104-269.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7632911; DOI=10.1007/bf00020389;
RA Arrowsmith D.A., De Silva J.;
RT "Characterisation of two tomato fruit-expressed cDNAs encoding xyloglucan
RT endo-transglycosylase.";
RL Plant Mol. Biol. 28:391-403(1995).
RN [10]
RP ENZYME ACTIVITY, AND GLYCOSYLATION.
RX PubMed=10406121; DOI=10.1046/j.1365-313x.1999.00459.x;
RA Campbell P., Braam J.;
RT "In vitro activities of four xyloglucan endotransglycosylases from
RT Arabidopsis.";
RL Plant J. 18:371-382(1999).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=11673616; DOI=10.1093/pcp/pce154;
RA Yokoyama R., Nishitani K.;
RT "A comprehensive expression analysis of all members of a gene family
RT encoding cell-wall enzymes allowed us to predict cis-regulatory regions
RT involved in cell-wall construction in specific organs of Arabidopsis.";
RL Plant Cell Physiol. 42:1025-1033(2001).
RN [12]
RP INDUCTION.
RX PubMed=11889033; DOI=10.1093/emboj/21.6.1267;
RA Kim G.-T., Shoda K., Tsuge T., Cho K.-H., Uchimiya H., Yokoyama R.,
RA Nishitani K., Tsukaya H.;
RT "The ANGUSTIFOLIA gene of Arabidopsis, a plant CtBP gene, regulates leaf-
RT cell expansion, the arrangement of cortical microtubules in leaf cells and
RT expression of a gene involved in cell-wall formation.";
RL EMBO J. 21:1267-1279(2002).
RN [13]
RP NOMENCLATURE.
RX PubMed=12514239; DOI=10.1093/pcp/pcf171;
RA Rose J.K.C., Braam J., Fry S.C., Nishitani K.;
RT "The XTH family of enzymes involved in xyloglucan endotransglucosylation
RT and endohydrolysis: current perspectives and a new unifying nomenclature.";
RL Plant Cell Physiol. 43:1421-1435(2002).
CC -!- FUNCTION: Catalyzes xyloglucan endohydrolysis (XEH) and/or
CC endotransglycosylation (XET). Cleaves and religates xyloglucan
CC polymers, an essential constituent of the primary cell wall, and
CC thereby participates in cell wall construction of growing tissues. May
CC be required during development to modify the walls of cells under
CC mechanical stress.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and
CC transfers the xyloglucanyl segment on to O-4 of the non-reducing
CC terminal glucose residue of an acceptor, which can be a xyloglucan or
CC an oligosaccharide of xyloglucan.; EC=2.4.1.207;
CC Evidence={ECO:0000269|PubMed:10406121};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC extracellular space, apoplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed. Predominantly expressed in stems.
CC Expressed in shoot apical meristems, also found in seedlings and
CC meristems. {ECO:0000269|PubMed:11673616, ECO:0000269|PubMed:1840916}.
CC -!- INDUCTION: May be transcriptionally regulated by ANGUSTIFOLIA.
CC {ECO:0000269|PubMed:11889033}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000250}.
CC -!- PTM: N-glycosylated; essential for its enzymatic activity.
CC {ECO:0000269|PubMed:10406121}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA32828.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA79012.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M63166; AAA32828.1; ALT_FRAME; Genomic_DNA.
DR EMBL; D63508; BAA09783.1; -; mRNA.
DR EMBL; AL109796; CAB52471.1; -; Genomic_DNA.
DR EMBL; AL161576; CAB81020.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85745.1; -; Genomic_DNA.
DR EMBL; AY035156; AAK59660.1; -; mRNA.
DR EMBL; AY063027; AAL34201.1; -; mRNA.
DR EMBL; AY085867; AAM63080.1; -; mRNA.
DR EMBL; Z17602; CAA79012.1; ALT_FRAME; mRNA.
DR EMBL; AF035384; AAC39467.1; -; mRNA.
DR EMBL; X82683; CAA58001.1; -; Genomic_DNA.
DR PIR; S61555; S61555.
DR PIR; T51754; T51754.
DR RefSeq; NP_194756.1; NM_119173.4.
DR AlphaFoldDB; P24806; -.
DR SMR; P24806; -.
DR BioGRID; 14437; 1.
DR STRING; 3702.AT4G30270.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR iPTMnet; P24806; -.
DR PaxDb; P24806; -.
DR PRIDE; P24806; -.
DR ProteomicsDB; 242455; -.
DR EnsemblPlants; AT4G30270.1; AT4G30270.1; AT4G30270.
DR GeneID; 829150; -.
DR Gramene; AT4G30270.1; AT4G30270.1; AT4G30270.
DR KEGG; ath:AT4G30270; -.
DR Araport; AT4G30270; -.
DR TAIR; locus:2128936; AT4G30270.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR HOGENOM; CLU_048041_0_0_1; -.
DR InParanoid; P24806; -.
DR OMA; NSNWYTQ; -.
DR OrthoDB; 1209387at2759; -.
DR PhylomeDB; P24806; -.
DR BRENDA; 2.4.1.207; 399.
DR PRO; PR:P24806; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P24806; baseline and differential.
DR Genevisible; P24806; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; ISS:UniProtKB.
DR GO; GO:0016762; F:xyloglucan:xyloglucosyl transferase activity; IDA:TAIR.
DR GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
DR GO; GO:0009828; P:plant-type cell wall loosening; TAS:TAIR.
DR GO; GO:0071669; P:plant-type cell wall organization or biogenesis; IMP:TAIR.
DR GO; GO:0010411; P:xyloglucan metabolic process; IEA:InterPro.
DR CDD; cd02176; GH16_XET; 1.
DR InterPro; IPR044791; Beta-glucanase/XTH.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR008263; GH16_AS.
DR InterPro; IPR010713; XET_C.
DR InterPro; IPR016455; XTH.
DR PANTHER; PTHR31062; PTHR31062; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF06955; XET_C; 1.
DR PIRSF; PIRSF005604; XET; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS01034; GH16_1; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW Apoplast; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..269
FT /note="Xyloglucan endotransglucosylase/hydrolase protein
FT 24"
FT /id="PRO_0000011824"
FT DOMAIN 22..212
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 102
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 115..117
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 125..127
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 191..192
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 196
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 256
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 100
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:10406121"
FT DISULFID 251..265
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CONFLICT 65
FT /note="L -> F (in Ref. 6; AAM63080)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..94
FT /note="GS -> DR (in Ref. 8; AAC39467)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="A -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 30756 MW; 648F042BC7ADED86 CRC64;
MSPFKIFFFT TLLVAAFSVS AADFNTDVNV AWGNGRGKIL NNGQLLTLSL DKSSGSGFQS
KTEYLFGKID MQIKLVPGNS AGTVTTFYLK SEGSTWDEID FEFLGNMSGD PYTLHTNVYT
QGKGDKEQQF HLWFDPTANF HTYSILWNPQ RIILTVDDTP IREFKNYESL GVLFPKNKPM
RMYASLWNAD DWATRGGLVK TDWSKAPFMA SYRNIKIDSK PNSNWYTQEM DSTSQARLKW
VQKNYMIYNY CTDHRRFPQG APKECTTSS
