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P51689

- ARSD_HUMAN

UniProt

P51689 - ARSD_HUMAN

Protein

Arylsulfatase D

Gene

ARSD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (04 Nov 2008)
      Previous versions | rss
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    Functioni

    Cofactori

    Binds 1 calcium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi49 – 491CalciumBy similarity
    Metal bindingi50 – 501CalciumBy similarity
    Metal bindingi89 – 891Calcium; via 3-oxoalanineBy similarity
    Binding sitei148 – 1481SubstrateBy similarity
    Active sitei150 – 1501By similarity
    Binding sitei304 – 3041SubstrateBy similarity
    Metal bindingi356 – 3561CalciumBy similarity
    Metal bindingi357 – 3571CalciumBy similarity
    Binding sitei381 – 3811SubstrateBy similarity

    GO - Molecular functioni

    1. arylsulfatase activity Source: ProtInc
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. glycosphingolipid metabolic process Source: Reactome
    3. post-translational protein modification Source: Reactome
    4. small molecule metabolic process Source: Reactome
    5. sphingolipid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_116105. Glycosphingolipid metabolism.
    REACT_121036. The activation of arylsulfatases.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arylsulfatase D (EC:3.1.6.-)
    Short name:
    ASD
    Gene namesi
    Name:ARSD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:717. ARSD.

    Subcellular locationi

    Lysosome Curated

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25008.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3333Sequence AnalysisAdd
    BLAST
    Chaini34 – 593560Arylsulfatase DPRO_0000033424Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
    Modified residuei89 – 8913-oxoalanine (Cys)By similarity
    Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi347 – 3471N-linked (GlcNAc...)1 Publication

    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

    Glycoprotein

    Proteomic databases

    MaxQBiP51689.
    PaxDbiP51689.
    PRIDEiP51689.

    Expressioni

    Tissue specificityi

    Expressed in the pancreas, kidney, liver, lung, placenta, brain and heart.

    Gene expression databases

    ArrayExpressiP51689.
    BgeeiP51689.
    CleanExiHS_ARSD.
    GenevestigatoriP51689.

    Organism-specific databases

    HPAiHPA004694.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000370546.

    Structurei

    3D structure databases

    ProteinModelPortaliP51689.
    SMRiP51689. Positions 38-586.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the sulfatase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3119.
    HOGENOMiHOG000135352.
    HOVERGENiHBG004283.
    InParanoidiP51689.
    KOiK12374.
    OMAiCLFFISW.
    OrthoDBiEOG7QZG9J.
    PhylomeDBiP51689.
    TreeFamiTF314186.

    Family and domain databases

    Gene3Di3.40.720.10. 2 hits.
    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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P51689-1) [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

    MRSAARRGRA APAARDSLPV LLFLCLLLKT CEPKTANAFK PNILLIMADD    50
    LGTGDLGCYG NNTLRTPNID QLAEEGVRLT QHLAAAPLCT PSRAAFLTGR 100
    HSFRSGMDAS NGYRALQWNA GSGGLPENET TFARILQQHG YATGLIGKWH 150
    QGVNCASRGD HCHHPLNHGF DYFYGMPFTL TNDCDPGRPP EVDAALRAQL 200
    WGYTQFLALG ILTLAAGQTC GFFSVSARAV TGMAGVGCLF FISWYSSFGF 250
    VRRWNCILMR NHDVTEQPMV LEKTASLMLK EAVSYIERHK HGPFLLFLSL 300
    LHVHIPLVTT SAFLGKSQHG LYGDNVEEMD WLIGKVLNAI EDNGLKNSTF 350
    TYFTSDHGGH LEARDGHSQL GGWNGIYKGG KGMGGWEGGI RVPGIFHWPG 400
    VLPAGRVIGE PTSLMDVFPT VVQLVGGEVP QDRVIDGHSL VPLLQGAEAR 450
    SAHEFLFHYC GQHLHAARWH QKDSGSVWKV HYTTPQFHPE GAGACYGRGV 500
    CPCSGEGVTH HRPPLLFDLS RDPSEARPLT PDSEPLYHAV IARVGAAVSE 550
    HRQTLSPVPQ QFSMSNILWK PWLQPCCGHF PFCSCHEDGD GTP 593
    Length:593
    Mass (Da):64,860
    Last modified:November 4, 2008 - v2
    Checksum:i982B29D0FCEF9D34
    GO
    Isoform 2 (identifier: P51689-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         334-382: GKVLNAIEDN...WNGIYKGGKG → ASDFMSSSEV...PVRLQILKRA
         383-593: Missing.

    Show »
    Length:382
    Mass (Da):42,315
    Checksum:iC9A8FFBE567654DD
    GO
    Isoform 3 (identifier: P51689-3) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    The sequence of this isoform differs from the canonical sequence as follows:
         504-593: Missing.

    Show »
    Length:503
    Mass (Da):54,934
    Checksum:iCC4F3F8C7D201877
    GO

    Sequence cautioni

    The sequence CAA58555.1 differs from that shown. Reason: Frameshift at several positions.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti224 – 2241S → C.1 Publication
    Corresponds to variant rs211653 [ dbSNP | Ensembl ].
    VAR_052508
    Natural varianti500 – 5001V → I.
    Corresponds to variant rs2229557 [ dbSNP | Ensembl ].
    VAR_052509
    Natural varianti564 – 5641M → T.
    Corresponds to variant rs2228431 [ dbSNP | Ensembl ].
    VAR_052510

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei334 – 38249GKVLN…KGGKG → ASDFMSSSEVTESEAIKLMF RTMQRRCLPSMAFKKPWRGP VRLQILKRA in isoform 2. 1 PublicationVSP_015798Add
    BLAST
    Alternative sequencei383 – 593211Missing in isoform 2. 1 PublicationVSP_015799Add
    BLAST
    Alternative sequencei504 – 59390Missing in isoform 3. 1 PublicationVSP_035667Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83572 mRNA. Translation: CAA58555.1. Frameshift.
    AF160499 mRNA. Translation: AAF22253.1.
    AC005295 Genomic DNA. No translation available.
    BC020229 mRNA. No translation available.
    CCDSiCCDS35196.1. [P51689-1]
    PIRiI37186.
    RefSeqiNP_001660.2. NM_001669.3. [P51689-1]
    UniGeneiHs.528631.

    Genome annotation databases

    EnsembliENST00000381154; ENSP00000370546; ENSG00000006756. [P51689-1]
    GeneIDi414.
    KEGGihsa:414.
    UCSCiuc004cqy.3. human. [P51689-1]

    Polymorphism databases

    DMDMi212276422.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83572 mRNA. Translation: CAA58555.1 . Frameshift.
    AF160499 mRNA. Translation: AAF22253.1 .
    AC005295 Genomic DNA. No translation available.
    BC020229 mRNA. No translation available.
    CCDSi CCDS35196.1. [P51689-1 ]
    PIRi I37186.
    RefSeqi NP_001660.2. NM_001669.3. [P51689-1 ]
    UniGenei Hs.528631.

    3D structure databases

    ProteinModelPortali P51689.
    SMRi P51689. Positions 38-586.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000370546.

    Polymorphism databases

    DMDMi 212276422.

    Proteomic databases

    MaxQBi P51689.
    PaxDbi P51689.
    PRIDEi P51689.

    Protocols and materials databases

    DNASUi 414.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381154 ; ENSP00000370546 ; ENSG00000006756 . [P51689-1 ]
    GeneIDi 414.
    KEGGi hsa:414.
    UCSCi uc004cqy.3. human. [P51689-1 ]

    Organism-specific databases

    CTDi 414.
    GeneCardsi GC0XM002818.
    HGNCi HGNC:717. ARSD.
    HPAi HPA004694.
    MIMi 300002. gene.
    neXtProti NX_P51689.
    PharmGKBi PA25008.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3119.
    HOGENOMi HOG000135352.
    HOVERGENi HBG004283.
    InParanoidi P51689.
    KOi K12374.
    OMAi CLFFISW.
    OrthoDBi EOG7QZG9J.
    PhylomeDBi P51689.
    TreeFami TF314186.

    Enzyme and pathway databases

    Reactomei REACT_116105. Glycosphingolipid metabolism.
    REACT_121036. The activation of arylsulfatases.

    Miscellaneous databases

    ChiTaRSi ARSD. human.
    GenomeRNAii 414.
    NextBioi 1749.
    PROi P51689.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51689.
    Bgeei P51689.
    CleanExi HS_ARSD.
    Genevestigatori P51689.

    Family and domain databases

    Gene3Di 3.40.720.10. 2 hits.
    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. "A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy."
      Franco B., Meroni G., Parenti G., Levilliers J., Bernard L., Gebbia M., Cox L., Maroteaux P., Sheffield L., Rappold G.A., Andria G., Petit C., Ballabio A.
      Cell 81:15-25(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Kidney.
    2. "Arylsulfatase D gene in Xp22.3 encodes two protein isoforms."
      Urbitsch P., Salzer M.J., Hirschmann P., Vogt P.H.
      DNA Cell Biol. 19:765-773(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT CYS-224.
      Tissue: Testis.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Colon.
    5. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-347.
      Tissue: Liver.

    Entry informationi

    Entry nameiARSD_HUMAN
    AccessioniPrimary (citable) accession number: P51689
    Secondary accession number(s): Q9UHJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3