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Q38908 (XTH30_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable xyloglucan endotransglucosylase/hydrolase protein 30

Short name=At-XTH30
Short name=XTH-30
EC=2.4.1.207
Gene names
Name:XTH30
Synonyms:XTR4
Ordered Locus Names:At1g32170
ORF Names:F3C3.5
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues By similarity.

Catalytic activity

Breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.

Subcellular location

Secretedcell wall Probable. Secretedextracellular spaceapoplast Probable.

Tissue specificity

Predominantly expressed in green siliques. Ref.6

Post-translational modification

Contains at least one intrachain disulfide bond essential for its enzymatic activity By similarity.

Miscellaneous

In contrast to group 1 and group 2 endotransglucosylase/hydrolase proteins, it may not contain the ligase activity, and may catalyze endohydrolysis xyloglucan polymers only.

Sequence similarities

Belongs to the glycosyl hydrolase 16 family. XTH group 3 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 343320Probable xyloglucan endotransglucosylase/hydrolase protein 30
PRO_0000011830

Sites

Active site1091Nucleophile By similarity
Active site1131Proton donor By similarity

Amino acid modifications

Glycosylation1321N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2021S → F in AAM67311. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q38908 [UniParc].

Last modified November 28, 2003. Version 2.
Checksum: B4DD6A9CE8451CD2

FASTA34339,888
        10         20         30         40         50         60 
MSKSSYNHIF ILILCLCLRS SSAFTNLNTL SFEESLSPLF GDANLVRSPD DLSVRLLLDR 

        70         80         90        100        110        120 
YTGSGFISSN MYQHGFYSSM IKLPADYTAG VVVAFYTSNG DVFEKTHDEL DIEFLGNIKG 

       130        140        150        160        170        180 
KPWRFQTNLY GNGSTHRGRE ERYRLWFDPS KEFHRYSILW TPHKIIFWVD DVPIREVIRN 

       190        200        210        220        230        240 
DAMGADYPAK PMALYATIWD ASDWATSGGK YKANYKFAPF VAEFKSFSLD GCSVDPIQEV 

       250        260        270        280        290        300 
PMDCSDSVDF LESQDYSSIN SHQRAAMRRF RQRFMYYSYC YDTLRYPEPL PECVIVPAEK 

       310        320        330        340 
DRFKETGRLK FGGTEARERR RNRRQQRRPE IEIESDPDDR KLL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The Arabidopsis XET-related gene family: environmental and hormonal regulation of expression."
Xu W., Campbell P., Vargheese A.K., Braam J.
Plant J. 9:879-889(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-343.
Strain: cv. Columbia.
[6]"A comprehensive expression analysis of all members of a gene family encoding cell-wall enzymes allowed us to predict cis-regulatory regions involved in cell-wall construction in specific organs of Arabidopsis."
Yokoyama R., Nishitani K.
Plant Cell Physiol. 42:1025-1033(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"The XTH family of enzymes involved in xyloglucan endotransglucosylation and endohydrolysis: current perspectives and a new unifying nomenclature."
Rose J.K.C., Braam J., Fry S.C., Nishitani K.
Plant Cell Physiol. 43:1421-1435(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC084165 Genomic DNA. Translation: AAG23439.1.
CP002684 Genomic DNA. Translation: AEE31443.1.
AY062698 mRNA. Translation: AAL32776.1.
AY086104 mRNA. Translation: AAM67311.1.
U43486 mRNA. Translation: AAB18365.1.
PIRB86446.
S71223.
RefSeqNP_174496.1. NM_102950.3.
UniGeneAt.10186.

3D structure databases

ProteinModelPortalQ38908.
SMRQ38908. Positions 25-293.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH16. Glycoside Hydrolase Family 16.

Proteomic databases

PaxDbQ38908.
PRIDEQ38908.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G32170.1; AT1G32170.1; AT1G32170.
GeneID840109.
KEGGath:AT1G32170.

Organism-specific databases

TAIRAT1G32170.

Phylogenomic databases

eggNOGCOG2273.
HOGENOMHOG000236368.
InParanoidQ38908.
KOK08235.
OMADASTWAT.
PhylomeDBQ38908.
ProtClustDBCLSN2913586.

Enzyme and pathway databases

BioCycARA:AT1G32170-MONOMER.

Gene expression databases

GenevestigatorQ38908.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
IPR016455. XET.
IPR010713. XET_C.
[Graphical view]
PfamPF00722. Glyco_hydro_16. 1 hit.
PF06955. XET_C. 1 hit.
[Graphical view]
PIRSFPIRSF005604. XET. 1 hit.
SUPFAMSSF49899. SSF49899. 1 hit.
ProtoNetSearch...

Entry information

Entry nameXTH30_ARATH
AccessionPrimary (citable) accession number: Q38908
Secondary accession number(s): Q8LDA9, Q9FVR2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 28, 2003
Last modified: February 19, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names