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Q9TRY9

- BGAL_CANFA

UniProt

Q9TRY9 - BGAL_CANFA

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Protein

Beta-galactosidase

Gene

GLB1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei189 – 1891Proton donorSequence Analysis
Active sitei269 – 2691NucleophileSequence Analysis

GO - Molecular functioni

  1. beta-galactosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_182226. Glycosphingolipid metabolism.
REACT_182384. Keratan sulfate degradation.
REACT_220733. HS-GAG degradation.
REACT_222277. Sialic acid metabolism.

Protein family/group databases

CAZyiGH35. Glycoside Hydrolase Family 35.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactosidase (EC:3.2.1.23)
Alternative name(s):
Acid beta-galactosidase
Short name:
Lactase
Gene namesi
Name:GLB1
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. Golgi apparatus Source: Ensembl
  3. lysosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Propeptidei25 – 295By similarityPRO_0000012181
Chaini30 – 668639Beta-galactosidasePRO_0000012182Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi248 – 2481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi465 – 4651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi499 – 4991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi546 – 5461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi556 – 5561N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9TRY9.
PRIDEiQ9TRY9.

Structurei

3D structure databases

ProteinModelPortaliQ9TRY9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 35 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1874.
HOGENOMiHOG000221607.
HOVERGENiHBG004841.
InParanoidiQ9TRY9.
KOiK12309.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR026283. B-gal_1-like.
IPR008979. Galactose-bd-like.
IPR019801. Glyco_hydro_35_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001944. Glycoside_Hdrlase_35.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR23421. PTHR23421. 1 hit.
PfamiPF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PIRSFiPIRSF006336. B-gal. 1 hit.
PRINTSiPR00742. GLHYDRLASE35.
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9TRY9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARPAAVRVL WALLLPLLLG SARGLRNASQ RTFTIDYSHN RFLKDGQPFR
60 70 80 90 100
YISGSIHYSR VPRFYWKDRL LKMKMAGLNA IQTYVPWNFH EPQPGQYQFS
110 120 130 140 150
GEQDVEYFIK LAHELGLLVI LRPGPYICAE WDMGGLPAWL LLKESIILRS
160 170 180 190 200
SDPDYLAAVD KWLGVLLPKM KPLLYQNGGP IITMQVENEY GSYFTCDYDY
210 220 230 240 250
LRFLQKLFHH HLGNDVLLFT TDGANEKFLQ CGALQGLYAT VDFGPGANIT
260 270 280 290 300
AAFQIQRKSE PKGPLVNSEF YTGWLDHWGQ PHSTVRTEVV ASSLHDILAH
310 320 330 340 350
GANVNLYMFI GGTNFAYWNG ANMPYQAQPT SYDYDAPLSE AGDLTEKYFA
360 370 380 390 400
LREVIRKFEK VPEGFIPPST PKFAYGKVAL KKLKTVEEAL NVLCPPGPIN
410 420 430 440 450
SLYPLTFIQV KQYFGFVMYR TTLPQDCSDP TPLSSPLSGV HDRAYVSVDG
460 470 480 490 500
VPQGVMERSN VITLNITGKA GATLDLLVEN MGRVNYGRYI NDFKGLISNL
510 520 530 540 550
TLGSSILTNW MIFPLNTEDA VRSHLGGWHG PNNGRHDKTF AHRSSNYTLP
560 570 580 590 600
AFYMGNFSIP SGIPDLPQDT FIQFPGWTKG QVWINGFNLG RYWPARGPQM
610 620 630 640 650
TLFVPRHILV TSTPNTIMVL ELEHAPCGDS GPEVCTVEFV DRPVIGAPPT
660
PGHPPPDLSH RDLRLDYV
Length:668
Mass (Da):74,992
Last modified:May 2, 2006 - v3
Checksum:i56B4A4AC7357221E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601R → H(PubMed:8725782)Curated
Sequence conflicti227 – 2271K → L(PubMed:8725782)Curated
Sequence conflicti342 – 3421G → A(PubMed:8725782)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti280 – 2801Q → P.
Natural varianti442 – 4421D → V.
Natural varianti444 – 4441A → V.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ196436 mRNA. Translation: ABA43388.1.
AF056084 mRNA. Translation: AAC12775.1.
RefSeqiNP_001032730.1. NM_001037641.1.
UniGeneiCfa.22721.

Genome annotation databases

GeneIDi403873.
KEGGicfa:403873.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ196436 mRNA. Translation: ABA43388.1 .
AF056084 mRNA. Translation: AAC12775.1 .
RefSeqi NP_001032730.1. NM_001037641.1.
UniGenei Cfa.22721.

3D structure databases

ProteinModelPortali Q9TRY9.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH35. Glycoside Hydrolase Family 35.

Proteomic databases

PaxDbi Q9TRY9.
PRIDEi Q9TRY9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 403873.
KEGGi cfa:403873.

Organism-specific databases

CTDi 2720.

Phylogenomic databases

eggNOGi COG1874.
HOGENOMi HOG000221607.
HOVERGENi HBG004841.
InParanoidi Q9TRY9.
KOi K12309.

Enzyme and pathway databases

Reactomei REACT_182226. Glycosphingolipid metabolism.
REACT_182384. Keratan sulfate degradation.
REACT_220733. HS-GAG degradation.
REACT_222277. Sialic acid metabolism.

Miscellaneous databases

NextBioi 20817366.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR026283. B-gal_1-like.
IPR008979. Galactose-bd-like.
IPR019801. Glyco_hydro_35_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001944. Glycoside_Hdrlase_35.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR23421. PTHR23421. 1 hit.
Pfami PF01301. Glyco_hydro_35. 1 hit.
[Graphical view ]
PIRSFi PIRSF006336. B-gal. 1 hit.
PRINTSi PR00742. GLHYDRLASE35.
SUPFAMi SSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEi PS01182. GLYCOSYL_HYDROL_F35. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The entire coding region of the canine lysosomal beta-galactosidase (GLB1) gene."
    Kreutzer R., Mueller G., Leeb T., Moritz A., Baumgaertner W.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skin.
  2. "A partial sequence of canine lysosomal beta-galactosidase (GLB1)."
    Smith B.F., Georgeson M., Baker H.J.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-668.
    Strain: Beagle.
    Tissue: Brain.
  3. "Comparison of the canine and human acid beta-galactosidase gene."
    Ahern-Rindell A.J., Kretz K.A., O'Brien J.S.
    Am. J. Med. Genet. 63:340-345(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-668.
    Tissue: Kidney, Muscle, Pancreas and Testis.

Entry informationi

Entry nameiBGAL_CANFA
AccessioniPrimary (citable) accession number: Q9TRY9
Secondary accession number(s): O62800, Q3HTI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: May 2, 2006
Last modified: October 29, 2014
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3