XTH33_ARATH
ID XTH33_ARATH Reviewed; 310 AA.
AC Q8LC45; Q9XIJ7;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase protein 33 {ECO:0000303|PubMed:12514239};
DE Short=At-XTH33 {ECO:0000303|PubMed:12514239};
DE Short=XTH-33 {ECO:0000303|PubMed:12514239};
DE EC=2.4.1.207 {ECO:0000250|UniProtKB:Q38857};
DE Flags: Precursor;
GN Name=XTH33 {ECO:0000303|PubMed:12514239};
GN OrderedLocusNames=At1g10550 {ECO:0000312|Araport:AT1G10550};
GN ORFNames=T10O24.17 {ECO:0000312|EMBL:AAD39577.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
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 [4]
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 [5]
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 [6]
RP TISSUE SPECIFICITY, AND REGULATION BY ATX1 AND ATX2.
RC STRAIN=cv. Columbia;
RX PubMed=18375658; DOI=10.1105/tpc.107.056614;
RA Saleh A., Alvarez-Venegas R., Yilmaz M., Le O., Hou G., Sadder M.,
RA Al-Abdallat A., Xia Y., Lu G., Ladunga I., Avramova Z.;
RT "The highly similar Arabidopsis homologs of trithorax ATX1 and ATX2 encode
RT proteins with divergent biochemical functions.";
RL Plant Cell 20:568-579(2008).
RN [7]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 90-LEU--ALA-109.
RC STRAIN=cv. Columbia;
RX PubMed=19154201; DOI=10.1111/j.1365-313x.2009.03798.x;
RA Ndamukong I., Chetram A., Saleh A., Avramova Z.;
RT "Wall-modifying genes regulated by the Arabidopsis homolog of trithorax,
RT ATX1: repression of the XTH33 gene as a test case.";
RL Plant J. 58:541-553(2009).
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). {ECO:0000250|UniProtKB:Q38857}.
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:0000250|UniProtKB:Q38857};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC extracellular space, apoplast {ECO:0000305}. Cell membrane
CC {ECO:0000269|PubMed:19154201}; Single-pass membrane protein
CC {ECO:0000269|PubMed:19154201}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in vegetative tissues
CC (roots, stems and seedlings) (PubMed:19154201). Predominantly expressed
CC in green siliques (PubMed:11673616). Expressed in flowers
CC (PubMed:18375658). {ECO:0000269|PubMed:11673616,
CC ECO:0000269|PubMed:18375658, ECO:0000269|PubMed:19154201}.
CC -!- DEVELOPMENTAL STAGE: Transiently expressed in flowers.
CC {ECO:0000269|PubMed:19154201}.
CC -!- INDUCTION: Regulated by ATX1 and ATX2 by epigenetic histone H3
CC methylation. {ECO:0000269|PubMed:18375658}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM63851.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC007067; AAD39577.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28593.1; -; Genomic_DNA.
DR EMBL; AY086802; AAM63851.1; ALT_INIT; mRNA.
DR PIR; A86239; A86239.
DR RefSeq; NP_172525.1; NM_100930.4.
DR AlphaFoldDB; Q8LC45; -.
DR SMR; Q8LC45; -.
DR STRING; 3702.AT1G10550.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; Q8LC45; -.
DR PRIDE; Q8LC45; -.
DR ProteomicsDB; 242491; -.
DR EnsemblPlants; AT1G10550.1; AT1G10550.1; AT1G10550.
DR GeneID; 837596; -.
DR Gramene; AT1G10550.1; AT1G10550.1; AT1G10550.
DR KEGG; ath:AT1G10550; -.
DR Araport; AT1G10550; -.
DR TAIR; locus:2194554; AT1G10550.
DR eggNOG; ENOG502QQMG; Eukaryota.
DR HOGENOM; CLU_048041_1_1_1; -.
DR InParanoid; Q8LC45; -.
DR OMA; RGPVYKP; -.
DR OrthoDB; 1209387at2759; -.
DR PhylomeDB; Q8LC45; -.
DR BioCyc; ARA:AT1G10550-MON; -.
DR PRO; PR:Q8LC45; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LC45; baseline and differential.
DR Genevisible; Q8LC45; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA: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; IEA:UniProtKB-EC.
DR GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
DR GO; GO:0009831; P:plant-type cell wall modification involved in multidimensional cell growth; 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 1: Evidence at protein level;
KW Apoplast; Cell membrane; Cell wall; Cell wall biogenesis/degradation;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Reference proteome; Secreted; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..310
FT /note="Probable xyloglucan endotransglucosylase/hydrolase
FT protein 33"
FT /id="PRO_0000011833"
FT TRANSMEM 90..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 22..233
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 118
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 122
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 122
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 135..137
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 145..149
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 212..213
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 217
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 301
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 120
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 296..309
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT MUTAGEN 90..109
FT /note="Missing: Abnormal subcellular cytoplasmic
FT localization organized as discrete aggregated bodies."
FT /evidence="ECO:0000269|PubMed:19154201"
FT CONFLICT 21
FT /note="S -> A (in Ref. 3; AAM63851)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="K -> N (in Ref. 3; AAM63851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 34644 MW; F3228D8CB96EF89D CRC64;
MKIMWETAVV FCLCSLSLVS SHSRKFTTPN VTRLTDQFSK IAIENGFSRR FGAHNIQVNG
SLAKLTLDKS SGAGLVSKNK YHYGFFSARL KLPAGFASGV VVAFYLSNAE TYPKSHDEID
IELLGRSRRD DWTIQTNVYA NGSTRTGREE KFYFWFDPTQ AFHDYTLIWN SHHTVFLVDN
IPVRQFPNRG AFTSAYPSKP MSLYVTVWDG SEWATKGGKY PVNYKYAPFV VSVADVELSG
CSVNNGSSTG SGPCTKSGGS ISSLDPVDGQ DFATLSKNQI NAMDWARRKL MFYSYCSDKP
RYKVMPAECN
