XTH27_ARATH
ID XTH27_ARATH Reviewed; 333 AA.
AC Q8LDS2; B9DI46; O04906; Q9SEB1;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase protein 27;
DE Short=At-XTH27;
DE Short=XTH-27;
DE EC=2.4.1.207;
DE Flags: Precursor;
GN Name=XTH27; Synonyms=EXGT-A3; OrderedLocusNames=At2g01850;
GN ORFNames=T23K3.4;
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.
RC STRAIN=cv. Columbia;
RX PubMed=10557219; DOI=10.1104/pp.121.3.715;
RA Akamatsu T., Hanzawa Y., Ohtake Y., Takahashi T., Nishitani K., Komeda Y.;
RT "Expression of endoxyloglucan transferase genes in acaulis mutants of
RT Arabidopsis.";
RL Plant Physiol. 121:715-721(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Okamoto S., Kamimai T., 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=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 [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 97-333.
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [8]
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).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. No-0;
RX PubMed=15860011; DOI=10.1111/j.1365-313x.2005.02395.x;
RA Matsui A., Yokoyama R., Seki M., Ito T., Shinozaki K., Takahashi T.,
RA Komeda Y., Nishitani K.;
RT "AtXTH27 plays an essential role in cell wall modification during the
RT development of tracheary elements.";
RL Plant J. 42:525-534(2005).
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 (By
CC similarity). Required for cell wall modification during the development
CC of tracheary elements. {ECO:0000250, ECO:0000269|PubMed:15860011}.
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 -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC extracellular space, apoplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in 7 day old seedlings, roots,
CC hypocotyls, rosette leaves, internodes between nodes bearing axillary
CC shoots, nodes bearing flowers, flower buds, anthers and siliques.
CC {ECO:0000269|PubMed:10557219, ECO:0000269|PubMed:15860011}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in the immature tracheary elements of
CC rosette leaves. Expressed in differentiating vasculature of the root,
CC the hypocotyls, and the flower filaments, as well as in the anthers and
CC the inner subepidermal layer of mature siliques.
CC {ECO:0000269|PubMed:15860011}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: In xth27-1 and xth27-2, short-shaped tracheary
CC elements in tertiary veins, reduced number of tertiary veins in the
CC first leaf, and yellow lesion-mimic spots in mature rosette leaves.
CC {ECO:0000269|PubMed:15860011}.
CC -!- MISCELLANEOUS: In contrast to group 1 and group 2
CC endotransglucosylase/hydrolase proteins, it may not contain the ligase
CC activity, and may catalyze endohydrolysis xyloglucan polymers only.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 3
CC subfamily. {ECO:0000305}.
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DR EMBL; AF163821; AAD45125.1; -; Genomic_DNA.
DR EMBL; D63509; BAA20289.1; -; mRNA.
DR EMBL; AC007069; AAD21783.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05508.1; -; Genomic_DNA.
DR EMBL; AY059910; AAL24392.1; -; mRNA.
DR EMBL; BT008820; AAP68259.1; -; mRNA.
DR EMBL; AY085835; AAM63050.1; -; mRNA.
DR EMBL; AK317757; BAH20413.1; -; mRNA.
DR PIR; H84429; H84429.
DR RefSeq; NP_178294.1; NM_126246.4.
DR AlphaFoldDB; Q8LDS2; -.
DR SMR; Q8LDS2; -.
DR STRING; 3702.AT2G01850.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; Q8LDS2; -.
DR PRIDE; Q8LDS2; -.
DR ProteomicsDB; 242579; -.
DR EnsemblPlants; AT2G01850.1; AT2G01850.1; AT2G01850.
DR GeneID; 814716; -.
DR Gramene; AT2G01850.1; AT2G01850.1; AT2G01850.
DR KEGG; ath:AT2G01850; -.
DR Araport; AT2G01850; -.
DR TAIR; locus:2059728; AT2G01850.
DR eggNOG; ENOG502QVQI; Eukaryota.
DR HOGENOM; CLU_048041_1_2_1; -.
DR InParanoid; Q8LDS2; -.
DR OMA; WIVFYID; -.
DR OrthoDB; 1209387at2759; -.
DR PhylomeDB; Q8LDS2; -.
DR BioCyc; ARA:AT2G01850-MON; -.
DR PRO; PR:Q8LDS2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8LDS2; baseline and differential.
DR Genevisible; Q8LDS2; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0010087; P:phloem or xylem histogenesis; 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; 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; PS51762; GH16_2; 1.
PE 2: Evidence at transcript level;
KW Apoplast; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..333
FT /note="Probable xyloglucan endotransglucosylase/hydrolase
FT protein 27"
FT /id="PRO_0000011827"
FT DOMAIN 21..223
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 311..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 112
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 135..139
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 202..203
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 207
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 282
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 110
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 277..290
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CONFLICT 181
FT /note="E -> Q (in Ref. 1; AAD45125)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="M -> I (in Ref. 6; AAM63050)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="E -> K (in Ref. 6; AAM63050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 38415 MW; E5B9861A9E5989D9 CRC64;
METLSRLLVF MSLFSGLVSG FALQNLPITS FEESYTQLFG DKNLFVHQDG KSVRLTLDER
TGSGFVSNDY YLHGFFSASI KLPSDYTAGV VVAFYMSNGD MYEKNHDEID FEFLGNIREK
EWRVQTNIYG NGSTHSGREE RYNLWFDPTE DFHQYSILWS DSHIIFFVDN VPIREVKRTA
EMGGHFPSKP MSLYTTIWDG SKWATNGGKY GVNYKYAPYI ARFSDLVLHG CPVDPIEQFP
RCDEGAAEDM RAAQEITPSQ RSKMDVFRRR LMTYSYCYDR ARYNVALSEC VVNPAEAQRL
RVYDPVRFGG IPRRHRNGKH RSKRSRVDGT ESI
