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)

P50429

- ARSB_MOUSE

UniProt

P50429 - ARSB_MOUSE

Protein

Arylsulfatase B

Gene

Arsb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 3 (09 Jan 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 bindingi54 – 541CalciumBy similarity
    Metal bindingi55 – 551CalciumBy similarity
    Metal bindingi92 – 921Calcium; via 3-oxoalanineBy similarity
    Binding sitei146 – 1461SubstrateBy similarity
    Active sitei148 – 1481By similarity
    Binding sitei243 – 2431SubstrateBy similarity
    Metal bindingi301 – 3011CalciumBy similarity
    Metal bindingi302 – 3021CalciumBy similarity
    Binding sitei319 – 3191SubstrateBy similarity

    GO - Molecular functioni

    1. arylsulfatase activity Source: MGI
    2. metal ion binding Source: UniProtKB-KW
    3. N-acetylgalactosamine-4-sulfatase activity Source: UniProtKB-EC

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_198981. CS/DS degradation.
    REACT_198990. The activation of arylsulfatases.
    REACT_199008. Glycosphingolipid metabolism.
    SABIO-RKP50429.

    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
    Synonyms:As1, As1-s
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:88075. Arsb.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi apparatus Source: Ensembl
    2. lysosome Source: UniProtKB-SubCell
    3. mitochondrion Source: Ensembl
    4. rough endoplasmic reticulum Source: Ensembl

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4141Sequence AnalysisAdd
    BLAST
    Chaini42 – 534493Arylsulfatase BPRO_0000033423Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei92 – 9213-oxoalanine (Cys)By similarity
    Disulfide bondi118 ↔ 522By similarity
    Disulfide bondi122 ↔ 156By similarity
    Disulfide bondi182 ↔ 193By similarity
    Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi280 – 2801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi292 – 2921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi406 ↔ 448By similarity
    Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP50429.
    PaxDbiP50429.
    PRIDEiP50429.

    PTM databases

    PhosphoSiteiP50429.

    Expressioni

    Gene expression databases

    BgeeiP50429.
    CleanExiMM_ARSB.
    GenevestigatoriP50429.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP50429.
    SMRiP50429. Positions 43-534.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the sulfatase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3119.
    GeneTreeiENSGT00560000077076.
    HOGENOMiHOG000135354.
    HOVERGENiHBG004282.
    InParanoidiP50429.
    KOiK01135.
    OrthoDBiEOG7MKW5Q.
    PhylomeDBiP50429.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P50429-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGKLSPCTGR SRPGGPGPQL PLLLLLLQLL LLLLSPARAS GATQPPHVVF    50
    VLADDLGWND LGFHGSVIRT PHLDALAAGG VVLDNYYVQP LCTPSRSQLL 100
    TGRYQIHLGL QHYLIMTCQP SCVPLDEKLL PQLLKEAGYA THMVGKWHLG 150
    MYRKECLPTR RGFDTYFGYL LGSEDYYTHE ACAPIESLNG TRCALDLRDG 200
    EEPAKEYNNI YSTNIFTKRA TTVIANHPPE KPLFLYLAFQ SVHDPLQVPE 250
    EYMEPYGFIQ DKHRRIYAGM VSLMDEAVGN VTKALKSHGL WNNTVFIFST 300
    DNGGQTRSGG NNWPLRGRKG TLWEGGIRGT GFVASPLLKQ KGVKSRELMH 350
    ITDWLPTLVD LAGGSTNGTK PLDGFNMWKT ISEGHPSPRV ELLHNIDQDF 400
    FDGLPCPGKN MTPAKDDSFP LEHSAFNTSI HAGIRYKNWK LLTGHPGCGY 450
    WFPPPSQSNV SEIPPVGPPT KTLWLFDINQ DPEERHDVSR EHPHIVQNLL 500
    SRLQYYHEHS VPSHFPPLDP RCDPKSTGVW SPWM 534
    Length:534
    Mass (Da):59,647
    Last modified:January 9, 2007 - v3
    Checksum:i78DAB2D65C71E97D
    GO
    Isoform 2 (identifier: P50429-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         383-431: EGHPSPRVEL...EHSAFNTSIH → PVTGDHWHAE...PDCGRARWFL
         432-534: Missing.

    Show »
    Length:431
    Mass (Da):47,934
    Checksum:iE3C8BBE3E0B7C6D5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 601D → A in AAA37261. (PubMed:1572648)Curated
    Sequence conflicti352 – 3521T → S in BAE34455. (PubMed:16141072)Curated
    Sequence conflicti352 – 3521T → S in CAA63067. (PubMed:8710849)Curated
    Sequence conflicti467 – 4671G → D in CAI84992. (PubMed:19468303)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei383 – 43149EGHPS…NTSIH → PVTGDHWHAEGELGCSFRTA SAAEEEPTYKLREKKRRKSP DCGRARWFL in isoform 2. 1 PublicationVSP_007881Add
    BLAST
    Alternative sequencei432 – 534103Missing in isoform 2. 1 PublicationVSP_022249Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK083309 mRNA. Translation: BAC38859.1.
    AK154098 mRNA. Translation: BAE32375.1.
    AK158312 mRNA. Translation: BAE34455.1.
    AC131739 Genomic DNA. No translation available.
    AC136976 Genomic DNA. No translation available.
    M82877 mRNA. Translation: AAA37261.1.
    X92096 mRNA. Translation: CAA63067.1.
    BN000746 mRNA. Translation: CAI84992.1.
    CCDSiCCDS36749.1. [P50429-1]
    RefSeqiNP_033842.3. NM_009712.3.
    UniGeneiMm.300178.
    Mm.472255.

    Genome annotation databases

    EnsembliENSMUST00000091403; ENSMUSP00000088964; ENSMUSG00000042082.
    GeneIDi11881.
    KEGGimmu:11881.
    UCSCiuc007rlo.1. mouse. [P50429-1]
    uc011zcv.1. mouse. [P50429-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK083309 mRNA. Translation: BAC38859.1 .
    AK154098 mRNA. Translation: BAE32375.1 .
    AK158312 mRNA. Translation: BAE34455.1 .
    AC131739 Genomic DNA. No translation available.
    AC136976 Genomic DNA. No translation available.
    M82877 mRNA. Translation: AAA37261.1 .
    X92096 mRNA. Translation: CAA63067.1 .
    BN000746 mRNA. Translation: CAI84992.1 .
    CCDSi CCDS36749.1. [P50429-1 ]
    RefSeqi NP_033842.3. NM_009712.3.
    UniGenei Mm.300178.
    Mm.472255.

    3D structure databases

    ProteinModelPortali P50429.
    SMRi P50429. Positions 43-534.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei P50429.

    Proteomic databases

    MaxQBi P50429.
    PaxDbi P50429.
    PRIDEi P50429.

    Protocols and materials databases

    DNASUi 11881.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000091403 ; ENSMUSP00000088964 ; ENSMUSG00000042082 .
    GeneIDi 11881.
    KEGGi mmu:11881.
    UCSCi uc007rlo.1. mouse. [P50429-1 ]
    uc011zcv.1. mouse. [P50429-2 ]

    Organism-specific databases

    CTDi 411.
    MGIi MGI:88075. Arsb.

    Phylogenomic databases

    eggNOGi COG3119.
    GeneTreei ENSGT00560000077076.
    HOGENOMi HOG000135354.
    HOVERGENi HBG004282.
    InParanoidi P50429.
    KOi K01135.
    OrthoDBi EOG7MKW5Q.
    PhylomeDBi P50429.
    TreeFami TF314186.

    Enzyme and pathway databases

    Reactomei REACT_198981. CS/DS degradation.
    REACT_198990. The activation of arylsulfatases.
    REACT_199008. Glycosphingolipid metabolism.
    SABIO-RK P50429.

    Miscellaneous databases

    NextBioi 279911.
    PROi P50429.
    SOURCEi Search...

    Gene expression databases

    Bgeei P50429.
    CleanExi MM_ARSB.
    Genevestigatori P50429.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Inner ear and Thymus.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "The sulfatase gene family: cross-species PCR cloning using the MOPAC technique."
      Grompe M., Pieretti M., Caskey C.T., Ballabio A.
      Genomics 12:755-760(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-90 (ISOFORM 1).
    4. "Targeted disruption of the arylsulfatase B gene results in mice resembling the phenotype of mucopolysaccharidosis VI."
      Evers M., Saftig P., Schmidt P., Hafner A., McLoghlin D.B., Schmahl W., Hess B., von Figura K., Peters C.
      Proc. Natl. Acad. Sci. U.S.A. 93:8214-8219(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 137-388 (ISOFORM 1).
    5. "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_MOUSE
    AccessioniPrimary (citable) accession number: P50429
    Secondary accession number(s): Q32KJ1
    , Q3TYV7, Q3U4Q6, Q8C404
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 125 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3