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A7XDQ9 (B3GTK_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 35. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable beta-1,3-galactosyltransferase 20

EC=2.4.1.-
Gene names
Name:B3GALT20
Ordered Locus Names:At4g21060
ORF Names:T13K14.220
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length684 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal glycosyl residue By similarity.

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein Probable.

Tissue specificity

Expressed in stems and at lower levels in cauline leaves and siliques. Ref.1

Sequence similarities

Belongs to the glycosyltransferase 31 family.

Contains 1 galectin domain.

Sequence caution

The sequence CAB45901.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB79106.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandManganese
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processprotein glycosylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiongalactosyltransferase activity

Inferred from electronic annotation. Source: InterPro

sugar binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: A7XDQ9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 684684Probable beta-1,3-galactosyltransferase 20
PRO_0000359430

Regions

Transmembrane23 – 4321Helical; Signal-anchor for type II membrane protein; Potential
Domain191 – 405215Galectin

Amino acid modifications

Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation1271N-linked (GlcNAc...) Potential
Glycosylation1621N-linked (GlcNAc...) Potential
Glycosylation5241N-linked (GlcNAc...) Potential
Glycosylation6321N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: C877E82BDC30326A

FASTA68477,912
        10         20         30         40         50         60 
MKRVKSESFR GVYSSRRFKL SHFLLAIAGF YLVFLAFKFP HFIEMVAMLS GDTGLDGALS 

        70         80         90        100        110        120 
DTSLDVSLSG SLRNDMLNRK LEDEDHQSGP STTQKVSPEE KINGSKQIQP LLFRYGRISG 

       130        140        150        160        170        180 
EVMRRRNRTI HMSPFERMAD EAWILGSKAW EDVDKFEVDK INESASIFEG KVESCPSQIS 

       190        200        210        220        230        240 
MNGDDLNKAN RIMLLPCGLA AGSSITILGT PQYAHKESVP QRSRLTRSYG MVLVSQFMVE 

       250        260        270        280        290        300 
LQGLKTGDGE YPPKILHLNP RIKGDWNHRP VIEHNTCYRM QWGVAQRCDG TPSKKDADVL 

       310        320        330        340        350        360 
VDGFRRCEKW TQNDIIDMVD SKESKTTSWF KRFIGREQKP EVTWSFPFAE GKVFVLTLRA 

       370        380        390        400        410        420 
GIDGFHINVG GRHVSSFPYR PGFTIEDATG LAVTGDVDIH SIHATSLSTS HPSFSPQKAI 

       430        440        450        460        470        480 
EFSSEWKAPP LPGTPFRLFM GVLSATNHFS ERMAVRKTWM QHPSIKSSDV VARFFVALNP 

       490        500        510        520        530        540 
RKEVNAMLKK EAEYFGDIVI LPFMDRYELV VLKTIAICEF GVQNVTAPYI MKCDDDTFIR 

       550        560        570        580        590        600 
VESILKQIDG VSPEKSLYMG NLNLRHRPLR TGKWTVTWEE WPEAVYPPYA NGPGYIISSN 

       610        620        630        640        650        660 
IAKYIVSQNS RHKLRLFKME DVSMGLWVEQ FNASMQPVEY SHSWKFCQYG CTLNYYTAHY 

       670        680 
QSPSQMMCLW DNLLKGRPQC CNFR 

« Hide

References

« Hide 'large scale' references
[1]"A unique beta-1,3-galactosyltransferase is indispensable for the biosynthesis of N-glycans containing Lewis a structures in Arabidopsis thaliana."
Strasser R., Bondili J.S., Vavra U., Schoberer J., Svoboda B., Gloessl J., Leonard R., Stadlmann J., Altmann F., Steinkellner H., Mach L.
Plant Cell 19:2278-2292(2007) [PubMed: 17630273] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: cv. Columbia.
Tissue: Leaf.
[2]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Identification of a novel group of putative Arabidopsis thaliana beta-(1,3)-galactosyltransferases."
Qu Y., Egelund J., Gilson P.R., Houghton F., Gleeson P.A., Schultz C.J., Bacic A.
Plant Mol. Biol. 68:43-59(2008) [PubMed: 18548197] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF428438 mRNA. Translation: ABR58857.1.
AL080282 Genomic DNA. Translation: CAB45901.1. Sequence problems.
AL161554 Genomic DNA. Translation: CAB79106.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84393.1.
IPIIPI00938828.
PIRT10648.
UniGeneAt.32667.

3D structure databases

ProteinModelPortalA7XDQ9.
ModBaseSearch...

Protein family/group databases

CAZyGT31. Glycosyltransferase Family 31.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G21060.2; AT4G21060.2; AT4G21060.
GenomeReviewsGene locus AT4G21060 in contig CT486007_GR.

Organism-specific databases

TAIRAt4g21060.

Phylogenomic databases

eggNOGKOG2287.
GeneTreeEPGT00050000005432.
HOGENOMHBG318248.
PhylomeDBA7XDQ9.

Gene expression databases

GenevestigatorA7XDQ9.

Family and domain databases

InterProIPR008985. ConA-like_lec_gl.
IPR013320. ConA-like_subgrp.
IPR001079. Galectin_CRD.
IPR002659. Glyco_trans_31.
[Graphical view]
Gene3DG3DSA:2.60.120.200. ConA_like_subgrp. 2 hits.
PANTHERPTHR11214. Glyco_trans_31. 1 hit.
PfamPF00337. Gal-bind_lectin. 1 hit.
PF01762. Galactosyl_T. 1 hit.
[Graphical view]
SMARTSM00908. Gal-bind_lectin. 1 hit.
SM00276. GLECT. 1 hit.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
PROSITEPS51304. GALECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB3GTK_ARATH
AccessionPrimary (citable) accession number: A7XDQ9
Secondary accession number(s): Q9SUA8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: October 23, 2007
Last modified: December 14, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families