Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9SCV0 (BGA12_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. 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 12

Short name=Lactase 12
EC=3.2.1.23
Gene names
Name:BGAL12
Ordered Locus Names:At4g26140
ORF Names:F20B18.250
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length728 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.

Tissue specificity

Ubiquitous, with higher expression levels in roots and siliques. Ref.5

Sequence similarities

Belongs to the glycosyl hydrolase 35 family.

Sequence caution

The sequence CAB39679.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB79469.1 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

cell wall

Inferred from direct assay PubMed 19767039. Source: TAIR

   Molecular_functionbeta-galactosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9SCV0-1)

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.
Isoform 2 (identifier: Q9SCV0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     418-419: Missing.
     624-638: STFDSPTGNEPLALD → VRETEESMNHDHQQS
     639-728: Missing.
Note: May be due to a competing acceptor splice site and to an intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 728701Beta-galactosidase 12
PRO_5000065885

Sites

Active site1851Proton donor Potential
Active site2541Nucleophile Potential

Amino acid modifications

Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation3801N-linked (GlcNAc...) Potential
Glycosylation4501N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence418 – 4192Missing in isoform 2.
VSP_026465
Alternative sequence624 – 63815STFDS…PLALD → VRETEESMNHDHQQS in isoform 2.
VSP_026466
Alternative sequence639 – 72890Missing in isoform 2.
VSP_026467

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 75EB099914A7BA65

FASTA72881,533
        10         20         30         40         50         60 
MGLNFREKAW ILLGILCCSS LICSVKAIVT YDRKAVIING QRRILLSGSI HYPRSTPEMW 

        70         80         90        100        110        120 
PDLIQKAKDG GLDVIQTYVF WNGHEPSPGQ YYFEDRYDLV KFIKVVQQAG LYVHLRIGPY 

       130        140        150        160        170        180 
VCAEWNFGGF PVWLKYVPGM VFRTDNEPFK AAMQKFTEKI VRMMKEEKLF ETQGGPIILS 

       190        200        210        220        230        240 
QIENEYGPIE WEIGAPGKAY TKWVAEMAQG LSTGVPWIMC KQDDAPNSII NTCNGFYCEN 

       250        260        270        280        290        300 
FKPNSDNKPK MWTENWTGWF TEFGGAVPYR PAEDIALSVA RFIQNGGSFI NYYMYHGGTN 

       310        320        330        340        350        360 
FDRTAGEFIA TSYDYDAPLD EYGLPREPKY SHLKRLHKVI KLCEPALVSA DPTVTSLGDK 

       370        380        390        400        410        420 
QEAHVFKSKS SCAAFLSNYN TSSAARVLFG GSTYDLPPWS VSILPDCKTE YYNTAKVQVR 

       430        440        450        460        470        480 
TSSIHMKMVP TNTPFSWGSY NEEIPSANDN GTFSQDGLVE QISITRDKTD YFWYLTDITI 

       490        500        510        520        530        540 
SPDEKFLTGE DPLLTIGSAG HALHVFVNGQ LAGTAYGSLE KPKLTFSQKI KLHAGVNKLA 

       550        560        570        580        590        600 
LLSTAAGLPN VGVHYETWNT GVLGPVTLNG VNSGTWDMTK WKWSYKIGTK GEALSVHTLA 

       610        620        630        640        650        660 
GSSTVEWKEG SLVAKKQPLT WYKSTFDSPT GNEPLALDMN TMGKGQMWIN GQNIGRHWPA 

       670        680        690        700        710        720 
YTARGKCERC SYAGTFTEKK CLSNCGEASQ RWYHVPRSWL KPTNNLVIVL EEWGGEPNGI 


SLVKRTAK 

« Hide

Isoform 2 [UniParc].

Checksum: 11F0DC8FDB69283D
Show »

FASTA63671,357

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] (ISOFORM 1).
[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]"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] (ISOFORM 2).
Strain: cv. Columbia.
[5]"Apoplastic glycosidases active against xyloglucan oligosaccharides of Arabidopsis thaliana."
Iglesias N., Abelenda J.A., Rodino M., Sampedro J., Revilla G., Zarra I.
Plant Cell Physiol. 47:55-63(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ270308 mRNA. Translation: CAB64748.1.
AL049483 Genomic DNA. Translation: CAB39679.1. Sequence problems.
AL161564 Genomic DNA. Translation: CAB79469.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85162.1.
CP002687 Genomic DNA. Translation: AEE85163.1.
AY099612 mRNA. Translation: AAM20463.1.
BT000267 mRNA. Translation: AAN15586.1.
PIRT04269.
RefSeqNP_194344.2. NM_118747.2.
NP_849553.1. NM_179222.1.
UniGeneAt.2962.

3D structure databases

ProteinModelPortalQ9SCV0.
SMRQ9SCV0. Positions 29-443, 470-514.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH35. Glycoside Hydrolase Family 35.

Proteomic databases

PaxDbQ9SCV0.
PRIDEQ9SCV0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G26140.1; AT4G26140.1; AT4G26140. [Q9SCV0-1]
GeneID828720.
KEGGath:AT4G26140.

Organism-specific databases

GeneFarm514. 90.
TAIRAT4G26140.

Phylogenomic databases

eggNOGCOG1874.
HOGENOMHOG000239919.
InParanoidQ9SCV0.
OMANSIINTC.
PhylomeDBQ9SCV0.
ProtClustDBCLSN2687368.

Enzyme and pathway databases

BioCycARA:AT4G26140-MONOMER.
ARA:GQT-2664-MONOMER.

Gene expression databases

GenevestigatorQ9SCV0.

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.
[Graphical view]
PANTHERPTHR23421. PTHR23421. 1 hit.
PfamPF02837. Glyco_hydro_2_N. 1 hit.
PF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PRINTSPR00742. GLHYDRLASE35.
SUPFAMSSF49785. SSF49785. 3 hits.
SSF51445. SSF51445. 1 hit.
PROSITEPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGA12_ARATH
AccessionPrimary (citable) accession number: Q9SCV0
Secondary accession number(s): Q8LPL0, Q9SZI5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 88 of the entry and version 1 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