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Protein

Arylsulfatase B

Gene

Arsb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation (PubMed:24311516). In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels (PubMed:24311516). Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium (By similarity).By similarity1 Publication

Catalytic activityi

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

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Enzyme regulationi

Inhibited by ethanol.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi48 – 481CalciumBy similarity
Metal bindingi49 – 491CalciumBy similarity
Metal bindingi86 – 861Calcium; via 3-oxoalanineBy similarity
Binding sitei140 – 1401SubstrateBy similarity
Active sitei142 – 1421By similarity
Binding sitei237 – 2371SubstrateBy similarity
Metal bindingi295 – 2951CalciumBy similarity
Metal bindingi296 – 2961CalciumBy similarity
Binding sitei313 – 3131SubstrateBy similarity

GO - Molecular functioni

  1. arylsulfatase activity Source: RGD
  2. metal ion binding Source: UniProtKB-KW
  3. N-acetylgalactosamine-4-sulfatase activity Source: UniProtKB
  4. sulfuric ester hydrolase activity Source: RGD

GO - Biological processi

  1. autophagy Source: RGD
  2. central nervous system development Source: RGD
  3. colon epithelial cell migration Source: UniProtKB
  4. positive regulation of neuron projection development Source: UniProtKB
  5. regulation of epithelial cell migration Source: UniProtKB
  6. response to estrogen Source: RGD
  7. response to methylmercury Source: RGD
  8. response to nutrient Source: RGD
  9. response to pH Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_198577. CS/DS degradation.
REACT_198581. The activation of arylsulfatases.
REACT_198596. Glycosphingolipid metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Arylsulfatase B (EC:3.1.6.12)
Short name:
ASB
Alternative name(s):
N-acetylgalactosamine-4-sulfatase
Short name:
G4S
Gene namesi
Name:Arsb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi2158. Arsb.

Subcellular locationi

Lysosome. Cell surface 1 Publication

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. extracellular vesicular exosome Source: Ensembl
  3. Golgi apparatus Source: RGD
  4. lysosome Source: RGD
  5. mitochondrion Source: RGD
  6. rough endoplasmic reticulum Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

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

Keywords - Diseasei

Mucopolysaccharidosis

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 528528Arylsulfatase BPRO_0000192682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei86 – 8613-oxoalanine (Cys)By similarity
Disulfide bondi112 ↔ 516By similarity
Disulfide bondi116 ↔ 150By similarity
Disulfide bondi176 ↔ 187By similarity
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi286 – 2861N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi400 ↔ 442By similarity
Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi421 – 4211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi453 – 4531N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP50430.
PRIDEiP50430.

Expressioni

Gene expression databases

ExpressionAtlasiP50430. baseline and differential.
GenevestigatoriP50430.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi247268. 1 interaction.
IntActiP50430. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP50430.
SMRiP50430. Positions 39-528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135354.
HOVERGENiHBG004282.
InParanoidiP50430.
KOiK01135.
OMAiWELIHIS.
OrthoDBiEOG7MKW5Q.
PhylomeDBiP50430.
TreeFamiTF314186.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50430-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGELSGCTGG SRAGGPGPRL PLLLLLLLWP ARASDAAPPP HVVFVLADDL
60 70 80 90 100
GWNDLGFHGS VIRTPHLDAL AAGGVVLDNY YVQPLCTPSR SQLLTGRYQI
110 120 130 140 150
HMGLQHYLIM TCQPNCVPLD EKLLPQLLKD AGYATHMVGK WHLGMYRKEC
160 170 180 190 200
LPTRRGFDTY FGYLLGSEDY YTHEACAPIE CLNGTRCALD LRDGEEPAKE
210 220 230 240 250
YTDIYSTNIF TKRATTLIAN HPPEKPLFLY LAFQSVHDPL QVPEEYMEPY
260 270 280 290 300
DFIQDKHRRI YAGMVSLLDE AVGNVTKALK SRGLWNNTVL IFSTDNGGQT
310 320 330 340 350
RSGGNNWPLR GRKGTLWEGG IRGAGFVASP LLKQKGVKSR ELMHITDWLP
360 370 380 390 400
TLVNLAGGST HGTKPLDGFD VWETISEGSP SPRVELLLNI DPDFFDGLPC
410 420 430 440 450
PGKNTTPEKN DSFPLEHSAF NTSIHAGIRY KNWKLLTGYP GCGYWFPPPS
460 470 480 490 500
QSNISEVPSV DSPTKTLWLF DINRDPEERH DVSREHPHIV QNLLSRLQYY
510 520
HEHSVPSYFP PLDPRCDPKG TGVWSPWM
Length:528
Mass (Da):58,959
Last modified:June 12, 2007 - v2
Checksum:i1F02425E858E5A00
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 572GF → IR in AABR03012149. (PubMed:15057822)Curated
Sequence conflicti133 – 1342YA → SS in AABR03012149. (PubMed:15057822)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI54210.
RefSeqiNP_254278.1. NM_033443.1.
UniGeneiRn.94004.

Genome annotation databases

EnsembliENSRNOT00000014860; ENSRNOP00000014860; ENSRNOG00000011150.
GeneIDi25227.
KEGGirno:25227.
UCSCiRGD:2158. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI54210.
RefSeqiNP_254278.1. NM_033443.1.
UniGeneiRn.94004.

3D structure databases

ProteinModelPortaliP50430.
SMRiP50430. Positions 39-528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247268. 1 interaction.
IntActiP50430. 1 interaction.

Proteomic databases

PaxDbiP50430.
PRIDEiP50430.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014860; ENSRNOP00000014860; ENSRNOG00000011150.
GeneIDi25227.
KEGGirno:25227.
UCSCiRGD:2158. rat.

Organism-specific databases

CTDi411.
RGDi2158. Arsb.

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135354.
HOVERGENiHBG004282.
InParanoidiP50430.
KOiK01135.
OMAiWELIHIS.
OrthoDBiEOG7MKW5Q.
PhylomeDBiP50430.
TreeFamiTF314186.

Enzyme and pathway databases

ReactomeiREACT_198577. CS/DS degradation.
REACT_198581. The activation of arylsulfatases.
REACT_198596. Glycosphingolipid metabolism.

Miscellaneous databases

NextBioi605779.
PROiP50430.

Gene expression databases

ExpressionAtlasiP50430. baseline and differential.
GenevestigatoriP50430.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
  4. "Cell-surface arylsulfatase A and B on sinusoidal endothelial cells, hepatocytes, and Kupffer cells in mammalian livers."
    Mitsunaga-Nakatsubo K., Kusunoki S., Kawakami H., Akasaka K., Akimoto Y.
    Med. Mol. Morphol. 42:63-69(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Arylsulfatase B modulates neurite outgrowth via astrocyte chondroitin-4-sulfate: dysregulation by ethanol."
    Zhang X., Bhattacharyya S., Kusumo H., Goodlett C.R., Tobacman J.K., Guizzetti M.
    Glia 62:259-271(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.

Entry informationi

Entry nameiARSB_RAT
AccessioniPrimary (citable) accession number: P50430
Secondary accession number(s): Q32KK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 12, 2007
Last modified: February 4, 2015
This is version 106 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.