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Q9SCU8 (BGA14_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 90. 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:
Beta-galactosidase 14

Short name=Lactase 14
EC=3.2.1.23
Gene names
Name:BGAL14
Ordered Locus Names:At4g38590
ORF Names:F20M13.150
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length887 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.

Subcellular location

Secretedextracellular spaceapoplast Potential.

Sequence similarities

Belongs to the glycosyl hydrolase 35 family.

Contains 1 SUEL-type lectin domain.

Sequence caution

The sequence AEE86951.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB80523.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentApoplast
Secreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentapoplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-galactosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

carbohydrate 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: Q9SCU8-1)

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

Signal peptide1 – 3131 Potential
Chain32 – 887856Beta-galactosidase 14
PRO_5000065887

Regions

Domain752 – 83887SUEL-type lectin

Sites

Active site1971Proton donor Potential
Active site2681Nucleophile Potential

Amino acid modifications

Glycosylation2691N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation3951N-linked (GlcNAc...) Potential
Glycosylation7851N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict571L → F in CAB64750. Ref.1
Sequence conflict701H → D in CAB64750. Ref.1
Sequence conflict2861V → A in CAB64750. Ref.1
Sequence conflict6271K → E in CAB64750. Ref.1
Sequence conflict6531A → G in CAB64750. Ref.1

Sequences

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

Last modified July 10, 2007. Version 2.
Checksum: 58486CB4B949508D

FASTA887101,222
        10         20         30         40         50         60 
MSKSSRIRMK SRTRYLIAIL LVISLCSKAS SHDDEKKKKG VTYDGTSLII NGKRELLFSG 

        70         80         90        100        110        120 
SVHYPRSTPH MWPSIIDKAR IGGLNTIQTY VFWNVHEPEQ GKYDFKGRFD LVKFIKLIHE 

       130        140        150        160        170        180 
KGLYVTLRLG PFIQAEWNHG GLPYWLREVP DVYFRTNNEP FKEHTERYVR KILGMMKEEK 

       190        200        210        220        230        240 
LFASQGGPII LGQIENEYNA VQLAYKENGE KYIKWAANLV ESMNLGIPWV MCKQNDAPGN 

       250        260        270        280        290        300 
LINACNGRHC GDTFPGPNRH DKPSLWTENW TTQFRVFGDP PTQRTVEDIA FSVARYFSKN 

       310        320        330        340        350        360 
GSHVNYYMYH GGTNFGRTSA HFVTTRYYDD APLDEFGLEK APKYGHLKHV HRALRLCKKA 

       370        380        390        400        410        420 
LFWGQLRAQT LGPDTEVRYY EQPGTKVCAA FLSNNNTRDT NTIKFKGQDY VLPSRSISIL 

       430        440        450        460        470        480 
PDCKTVVYNT AQIVAQHSWR DFVKSEKTSK GLKFEMFSEN IPSLLDGDSL IPGELYYLTK 

       490        500        510        520        530        540 
DKTDYAWYTT SVKIDEDDFP DQKGLKTILR VASLGHALIV YVNGEYAGKA HGRHEMKSFE 

       550        560        570        580        590        600 
FAKPVNFKTG DNRISILGVL TGLPDSGSYM EHRFAGPRAI SIIGLKSGTR DLTENNEWGH 

       610        620        630        640        650        660 
LAGLEGEKKE VYTEEGSKKV KWEKDGKRKP LTWYKTYFET PEGVNAVAIR MKAMGKGLIW 

       670        680        690        700        710        720 
VNGIGVGRYW MSFLSPLGEP TQTEYHIPRS FMKGEKKKNM LVILEEEPGV KLESIDFVLV 

       730        740        750        760        770        780 
NRDTICSNVG EDYPVSVKSW KREGPKIVSR SKDMRLKAVM RCPPEKQMVE VQFASFGDPT 

       790        800        810        820        830        840 
GTCGNFTMGK CSASKSKEVV EKECLGRNYC SIVVARETFG DKGCPEIVKT LAVQVKCEKK 

       850        860        870        880 
EGKQDEKKKK EDKDEEEEDD EDDDEEEEEE DKENKDTKDM ENKNQDM 

« Hide

References

« Hide 'large scale' references
[1]"The beta-galactosidases are encoding by a multigene family in Arabidopsis thaliana."
Gy I., Kreis M., Lecharny A.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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] [Europe PMC] [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]"Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 35."
Ahn Y.O., Zheng M., Bevan D.R., Esen A., Shiu S.-H., Benson J., Peng H.-P., Miller J.T., Cheng C.-L., Poulton J.E., Shih M.-C.
Phytochemistry 68:1510-1520(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ270310 mRNA. Translation: CAB64750.1.
AL035540 Genomic DNA. Translation: CAB37515.1. Sequence problems.
AL161593 Genomic DNA. Translation: CAB80523.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE86951.1. Sequence problems.
PIRT05687.
RefSeqNP_195571.2. NM_120020.3.
UniGeneAt.70242.

3D structure databases

ProteinModelPortalQ9SCU8.
SMRQ9SCU8. Positions 41-709.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH35. Glycoside Hydrolase Family 35.

Proteomic databases

PaxDbQ9SCU8.
PRIDEQ9SCU8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G38590.1; AT4G38590.1; AT4G38590.
GeneID830016.
KEGGath:AT4G38590.

Organism-specific databases

GeneFarm517. 90.
TAIRAT4G38590.

Phylogenomic databases

eggNOGCOG1874.
HOGENOMHOG000239919.
InParanoidQ9SCU8.
PhylomeDBQ9SCU8.

Enzyme and pathway databases

BioCycARA:GQT-2802-MONOMER.

Gene expression databases

GenevestigatorQ9SCU8.

Family and domain databases

Gene3D2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProIPR008979. Galactose-bd-like.
IPR006104. Glyco_hydro_2_N.
IPR019801. Glyco_hydro_35_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001944. Glycoside_Hdrlase_35.
IPR017853. Glycoside_hydrolase_SF.
IPR000922. Lectin_gal-bd_dom.
[Graphical view]
PANTHERPTHR23421. PTHR23421. 1 hit.
PfamPF02140. Gal_Lectin. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
PF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PRINTSPR00742. GLHYDRLASE35.
SUPFAMSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
PS50228. SUEL_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGA14_ARATH
AccessionPrimary (citable) accession number: Q9SCU8
Secondary accession number(s): F4JUE4, Q9SZN8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 10, 2007
Last modified: June 11, 2014
This is version 90 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