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Q5R5N6

- BGLR_PONAB

UniProt

Q5R5N6 - BGLR_PONAB

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Protein

Beta-glucuronidase

Gene

GUSB

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Plays an important role in the degradation of dermatan and keratan sulfates.By similarity

Catalytic activityi

A beta-D-glucuronoside + H2O = D-glucuronate + an alcohol.

Enzyme regulationi

Inhibited by L-aspartic acid.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei451 – 4511Proton donorBy similarity

GO - Molecular functioni

  1. beta-glucuronidase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucuronidase (EC:3.2.1.31)
Gene namesi
Name:GUSB
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Lysosome By similarity

GO - Cellular componenti

  1. lysosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222By similarityAdd
BLAST
Chaini23 – 651629Beta-glucuronidasePRO_0000231039Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi272 – 2721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi420 – 4201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5R5N6.
SMRiQ5R5N6. Positions 22-632.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG004843.
InParanoidiQ5R5N6.
KOiK01195.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR023232. Glyco_hydro_2_AS.
IPR023230. Glyco_hydro_2_CS.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR006103. Glyco_hydro_2_TIM.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
PRINTSiPR00132. GLHYDRLASE2.
SUPFAMiSSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5R5N6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARGSAVAWA AFGPLLWGCA LGLQGGMLYP QESRSRERKE LDGLWSFRAD
60 70 80 90 100
FSDNRRRGFE EQWYRRPLRE SGPTLDMPVP SSFNDISQDW RLRHFVGWVW
110 120 130 140 150
YEREVILPER WTQDLHTRVV LRIGSAHSYA IVWVNGVDTL EHEGGYLPFE
160 170 180 190 200
ADISNLVQVG PLPSRLRITI AINNTLTPTT LPPGTIQYMN DTSKYPKGYF
210 220 230 240 250
VQNTYFDFFN YAGLQRSVLL YTTPTTYIDD ITVTTGVEQD SGLVNYQISV
260 270 280 290 300
KGSNLFELEA RLLDAENKVV ANGTGTQGQL KVPGASLWWP YLMHERPAYL
310 320 330 340 350
YSLEVRLTAQ TSLGPVSDFY SLPVGIRTVA VTESQFLING KPFYFHGVNK
360 370 380 390 400
HEDADIRGKG FDWPLLVKDF NLLRWLGANA FRTSHYPYAE EVLQMCDRHG
410 420 430 440 450
IVVIDECPGV GLALPQFFNN VSLHHHMRVM EEVVRRDKNH PAVVMWSVAN
460 470 480 490 500
EPASHLESAG YYLKMVIAHT KALDPSRPVT FVSNSNYAAD KGAPYVDVIC
510 520 530 540 550
LNSYYSWYHD YGHLELIQLQ LATQFENWYK KYQKPIIQSE YGAETIAGFH
560 570 580 590 600
QDPPLMFTEE YQKSLLEQYH LGLDQKRRKY VVGELIWNFA DFMTEQSLTR
610 620 630 640 650
VLGNKKGIFT RQRQPKSAAF LLRERYWKIA NETRYPHSVA KSQCLENSPF

T
Length:651
Mass (Da):74,772
Last modified:April 4, 2006 - v2
Checksum:iA3170629BE393917
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41G → R in CAH92009. 1 PublicationCurated
Sequence conflicti69 – 691R → Q in CAH92930. 1 PublicationCurated
Sequence conflicti370 – 3701F → I in CAH92009. 1 PublicationCurated
Sequence conflicti406 – 4061E → G in CAH92930. 1 PublicationCurated
Sequence conflicti460 – 4601G → D in CAH92009. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR859852 mRNA. Translation: CAH92009.1.
CR860821 mRNA. Translation: CAH92930.1.
RefSeqiNP_001126724.1. NM_001133252.1.
NP_001128846.1. NM_001135374.1.
UniGeneiPab.18644.
Pab.8068.

Genome annotation databases

GeneIDi100173726.
100189763.
KEGGipon:100173726.
pon:100189763.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR859852 mRNA. Translation: CAH92009.1 .
CR860821 mRNA. Translation: CAH92930.1 .
RefSeqi NP_001126724.1. NM_001133252.1.
NP_001128846.1. NM_001135374.1.
UniGenei Pab.18644.
Pab.8068.

3D structure databases

ProteinModelPortali Q5R5N6.
SMRi Q5R5N6. Positions 22-632.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100173726.
100189763.
KEGGi pon:100173726.
pon:100189763.

Organism-specific databases

CTDi 2990.

Phylogenomic databases

HOVERGENi HBG004843.
InParanoidi Q5R5N6.
KOi K01195.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR008979. Galactose-bd-like.
IPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR023232. Glyco_hydro_2_AS.
IPR023230. Glyco_hydro_2_CS.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR006103. Glyco_hydro_2_TIM.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view ]
PRINTSi PR00132. GLHYDRLASE2.
SUPFAMi SSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEi PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex and Kidney.

Entry informationi

Entry nameiBGLR_PONAB
AccessioniPrimary (citable) accession number: Q5R5N6
Secondary accession number(s): Q5R8A1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: October 29, 2014
This is version 52 of the entry and version 2 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