Reviewed, UniProtKB/Swiss-Prot Q94A05 (B3GTA_ARATH)

Names and origin

Protein names

Recommended name:
    Probable beta-1,3-galactosyltransferase 10
    EC=2.4.1.-

Gene names

Name:	B3GALT10
Ordered Locus Names:	At4g32120
ORF Names:	F10N7.70

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Sequence similarities	Belongs to the glycosyltransferase 31 family.
Sequence caution	The sequence CAA16577.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB79930.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Ligand	Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid glycosylation Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	galactosyltransferase activity Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 345	345	Probable beta-1,3-galactosyltransferase 10		PRO_0000359420
Regions
	Transmembrane	28 – 44	17	Signal-anchor for type II membrane protein Potential
Amino acid modifications
	Glycosylation	23	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	1	1	M → V in BAC42946. Ref.2
	Sequence conflict	1	1	M → V in BAD43409. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q94A05-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 3336BA48963155D4	FASTA	345	39,272
	10 20 30 40 50 60 MESLPTTVSG KSDRRGRFSK SQNTSKPSLI LAFFSCLAWL YVAGRLWQDA QYRAALNTVL 70 80 90 100 110 120 KMNYDQRPKV LTVEDKLVVL GCKDLERRIV ETEMELAQAK SQGYLKKQKS VSSSGKKMLA 130 140 150 160 170 180 VIGVYTGFGS HLKRNKFRGS WMPRDDALKK LEERGVVIRF VIGRSANRGD SLDRKIDEEN 190 200 210 220 230 240 RATKDFLILE NHEEAQEELP KKVKFFYSAA VQNWDAEFYV KVDDNVDLDL EGMIALLESR 250 260 270 280 290 300 RSQDGAYIGC MKSGDVITEE GSQWYEPEWW KFGDDKSYFR HATGSLVILS KNLAQYVNIN 310 320 330 340 SGLLKTYAFD DTTIGSWMIG VQATYIDDNR LCCSSTRQEK VCSMA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. , 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.
[2]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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. , 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL021636 Genomic DNA. Translation: CAA16577.1. Sequence problems. AL161580 Genomic DNA. Translation: CAB79930.1. Sequence problems. AK118332 mRNA. Translation: BAC42946.1. Different initiation. AY050775 mRNA. Translation: AAK92710.1. AY113951 mRNA. Translation: AAM44999.1. AK175646 mRNA. Translation: BAD43409.1. Different initiation.
IPI	IPI00533528.
PIR	T04633.
RefSeq	NP_194939.1.
UniGene	At.25086
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT31. Glycosyltransferase Family 31.
Proteomic databases
PRIDE	Q94A05.
Genome annotation databases
GeneID	829344.
GenomeReviews	Gene locus AT4G32120 in contig CT486007_GR.
KEGG	ath:AT4G32120.
NMPDR	fig|3702.1.peg.21231.
Organism-specific databases
TAIR	At4g32120.
Phylogenomic databases
OMA	Q94A05. EAEMDLT.
Family and domain databases
InterPro	IPR002659. Glyco_trans_31. [Graphical view]
PANTHER	PTHR11214. Glyco_trans_31. 1 hit.
Pfam	PF01762. Galactosyl_T. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

B3GTA_ARATH

Accession

Primary (citable) accession number: Q94A05
Secondary accession number(s): O49380, Q8GXB0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)