Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P50430

- ARSB_RAT

UniProt

P50430 - ARSB_RAT

Protein

Arylsulfatase B

Gene

Arsb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (12 Jun 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 1 calcium ion per subunit.By similarity

    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-EC
    4. sulfuric ester hydrolase activity Source: RGD

    GO - Biological processi

    1. autophagy Source: RGD
    2. central nervous system development Source: RGD
    3. response to estrogen Source: RGD
    4. response to methylmercury Source: RGD
    5. response to nutrient Source: RGD
    6. response to pH Source: RGD

    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

    GO - Cellular componenti

    1. Golgi apparatus Source: RGD
    2. lysosome Source: RGD
    3. mitochondrion Source: RGD
    4. rough endoplasmic reticulum Source: RGD

    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

    ArrayExpressiP50430.
    GenevestigatoriP50430.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    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.
    GeneTreeiENSGT00560000077076.
    HOGENOMiHOG000135354.
    HOVERGENiHBG004282.
    InParanoidiP50430.
    KOiK01135.
    OMAiPPEKXNG.
    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

    MGELSGCTGG SRAGGPGPRL PLLLLLLLWP ARASDAAPPP HVVFVLADDL    50
    GWNDLGFHGS VIRTPHLDAL AAGGVVLDNY YVQPLCTPSR SQLLTGRYQI 100
    HMGLQHYLIM TCQPNCVPLD EKLLPQLLKD AGYATHMVGK WHLGMYRKEC 150
    LPTRRGFDTY FGYLLGSEDY YTHEACAPIE CLNGTRCALD LRDGEEPAKE 200
    YTDIYSTNIF TKRATTLIAN HPPEKPLFLY LAFQSVHDPL QVPEEYMEPY 250
    DFIQDKHRRI YAGMVSLLDE AVGNVTKALK SRGLWNNTVL IFSTDNGGQT 300
    RSGGNNWPLR GRKGTLWEGG IRGAGFVASP LLKQKGVKSR ELMHITDWLP 350
    TLVNLAGGST HGTKPLDGFD VWETISEGSP SPRVELLLNI DPDFFDGLPC 400
    PGKNTTPEKN DSFPLEHSAF NTSIHAGIRY KNWKLLTGYP GCGYWFPPPS 450
    QSNISEVPSV DSPTKTLWLF DINRDPEERH DVSREHPHIV QNLLSRLQYY 500
    HEHSVPSYFP PLDPRCDPKG TGVWSPWM 528
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi I54210.
    RefSeqi NP_254278.1. NM_033443.1.
    UniGenei Rn.94004.

    3D structure databases

    ProteinModelPortali P50430.
    SMRi P50430. Positions 39-528.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P50430. 1 interaction.

    Proteomic databases

    PaxDbi P50430.
    PRIDEi P50430.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000014860 ; ENSRNOP00000014860 ; ENSRNOG00000011150 .
    GeneIDi 25227.
    KEGGi rno:25227.
    UCSCi RGD:2158. rat.

    Organism-specific databases

    CTDi 411.
    RGDi 2158. Arsb.

    Phylogenomic databases

    eggNOGi COG3119.
    GeneTreei ENSGT00560000077076.
    HOGENOMi HOG000135354.
    HOVERGENi HBG004282.
    InParanoidi P50430.
    KOi K01135.
    OMAi PPEKXNG.
    OrthoDBi EOG7MKW5Q.
    PhylomeDBi P50430.
    TreeFami TF314186.

    Enzyme and pathway databases

    Reactomei REACT_198577. CS/DS degradation.
    REACT_198581. The activation of arylsulfatases.
    REACT_198596. Glycosphingolipid metabolism.

    Miscellaneous databases

    NextBioi 605779.
    PROi P50430.

    Gene expression databases

    ArrayExpressi P50430.
    Genevestigatori P50430.

    Family and domain databases

    Gene3Di 3.40.720.10. 1 hit.
    InterProi IPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR000917. Sulfatase.
    IPR024607. Sulfatase_CS.
    [Graphical view ]
    Pfami PF00884. Sulfatase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53649. SSF53649. 1 hit.
    PROSITEi PS00523. SULFATASE_1. 1 hit.
    PS00149. SULFATASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 102 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