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P50430 (ARSB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arylsulfatase B

Short name=ASB
EC=3.1.6.12
Alternative name(s):
N-acetylgalactosamine-4-sulfatase
Short name=G4S
Gene names
Name:Arsb
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Lysosome.

Involvement in disease

Defects in Arsb are the cause of mucopolysaccharidosis type VI (MPS-VI).

Sequence similarities

Belongs to the sulfatase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 528528Arylsulfatase B
PRO_0000192682

Sites

Active site1421 By similarity
Metal binding481Calcium By similarity
Metal binding491Calcium By similarity
Metal binding861Calcium; via 3-oxoalanine By similarity
Metal binding2951Calcium By similarity
Metal binding2961Calcium By similarity
Binding site1401Substrate By similarity
Binding site2371Substrate By similarity
Binding site3131Substrate By similarity

Amino acid modifications

Modified residue8613-oxoalanine (Cys) By similarity
Glycosylation1831N-linked (GlcNAc...) Potential
Glycosylation2741N-linked (GlcNAc...) Potential
Glycosylation2861N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential
Glycosylation4211N-linked (GlcNAc...) Potential
Glycosylation4531N-linked (GlcNAc...) Potential
Disulfide bond112 ↔ 516 By similarity
Disulfide bond116 ↔ 150 By similarity
Disulfide bond176 ↔ 187 By similarity
Disulfide bond400 ↔ 442 By similarity

Experimental info

Sequence conflict56 – 572GF → IR in AABR03012149. Ref.1
Sequence conflict133 – 1342YA → SS in AABR03012149. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P50430 [UniParc].

Last modified June 12, 2007. Version 2.
Checksum: 1F02425E858E5A00

FASTA52858,959
        10         20         30         40         50         60 
MGELSGCTGG SRAGGPGPRL PLLLLLLLWP ARASDAAPPP HVVFVLADDL GWNDLGFHGS 

        70         80         90        100        110        120 
VIRTPHLDAL AAGGVVLDNY YVQPLCTPSR SQLLTGRYQI HMGLQHYLIM TCQPNCVPLD 

       130        140        150        160        170        180 
EKLLPQLLKD AGYATHMVGK WHLGMYRKEC LPTRRGFDTY FGYLLGSEDY YTHEACAPIE 

       190        200        210        220        230        240 
CLNGTRCALD LRDGEEPAKE YTDIYSTNIF TKRATTLIAN HPPEKPLFLY LAFQSVHDPL 

       250        260        270        280        290        300 
QVPEEYMEPY DFIQDKHRRI YAGMVSLLDE AVGNVTKALK SRGLWNNTVL IFSTDNGGQT 

       310        320        330        340        350        360 
RSGGNNWPLR GRKGTLWEGG IRGAGFVASP LLKQKGVKSR ELMHITDWLP TLVNLAGGST 

       370        380        390        400        410        420 
HGTKPLDGFD VWETISEGSP SPRVELLLNI DPDFFDGLPC PGKNTTPEKN DSFPLEHSAF 

       430        440        450        460        470        480 
NTSIHAGIRY KNWKLLTGYP GCGYWFPPPS QSNISEVPSV DSPTKTLWLF DINRDPEERH 

       490        500        510        520 
DVSREHPHIV QNLLSRLQYY HEHSVPSYFP PLDPRCDPKG TGVWSPWM 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"Mucopolysaccharidosis type VI in rats: isolation of cDNAs encoding arylsulfatase B, chromosomal localization of the gene, and identification of the mutation."
Kunieda T.
Genomics 29:582-587(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-55.
Strain: Sprague-Dawley.
Tissue: Liver.
[3]"Sulfatases and sulfatase modifying factors: an exclusive and promiscuous relationship."
Sardiello M., Annunziata I., Roma G., Ballabio A.
Hum. Mol. Genet. 14:3203-3217(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03012149 Genomic DNA. No translation available.
AABR03015281 Genomic DNA. No translation available.
AABR03016930 Genomic DNA. No translation available.
AABR03021723 Genomic DNA. No translation available.
D49434 mRNA. Translation: BAA08412.1.
BN000736 mRNA. Translation: CAI84982.1.
PIRI54210.
RefSeqNP_254278.1. NM_033443.1.
UniGeneRn.94004.

3D structure databases

ProteinModelPortalP50430.
SMRP50430. Positions 39-528.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP50430. 1 interaction.

Proteomic databases

PaxDbP50430.
PRIDEP50430.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000014860; ENSRNOP00000014860; ENSRNOG00000011150.
GeneID25227.
KEGGrno:25227.
UCSCRGD:2158. rat.

Organism-specific databases

CTD411.
RGD2158. Arsb.

Phylogenomic databases

eggNOGCOG3119.
GeneTreeENSGT00560000077076.
HOGENOMHOG000135354.
HOVERGENHBG004282.
InParanoidP50430.
KOK01135.
OMAPPEKXNG.
OrthoDBEOG7MKW5Q.
PhylomeDBP50430.
TreeFamTF314186.

Gene expression databases

ArrayExpressP50430.
GenevestigatorP50430.

Family and domain databases

Gene3D3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMSSF53649. SSF53649. 1 hit.
PROSITEPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio605779.
PROP50430.

Entry information

Entry nameARSB_RAT
AccessionPrimary (citable) accession number: P50430
Secondary accession number(s): Q32KK1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families