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)

P54793

- ARSF_HUMAN

UniProt

P54793 - ARSF_HUMAN

Protein

Arylsulfatase F

Gene

ARSF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 4 (22 Sep 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Cofactori

    Binds 1 calcium ion per subunit.By similarity

    Enzyme regulationi

    Not inhibited by DHEAS or warfarin.

    pH dependencei

    Optimum pH is 8.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi38 – 381CalciumBy similarity
    Metal bindingi39 – 391CalciumBy similarity
    Metal bindingi78 – 781Calcium; via 3-oxoalanineBy similarity
    Binding sitei137 – 1371SubstrateBy similarity
    Active sitei139 – 1391By similarity
    Binding sitei293 – 2931SubstrateBy similarity
    Metal bindingi345 – 3451CalciumBy similarity
    Metal bindingi346 – 3461CalciumBy similarity
    Binding sitei370 – 3701SubstrateBy 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 F (EC:3.1.6.-)
    Short name:
    ASF
    Gene namesi
    Name:ARSF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:721. ARSF.

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25012.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 590568Arylsulfatase FPRO_0000033427Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi50 – 501N-linked (GlcNAc...)Sequence Analysis
    Modified residuei78 – 7813-oxoalanine (Cys)By similarity
    Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi336 – 3361N-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

    Glycoprotein

    Proteomic databases

    PaxDbiP54793.
    PRIDEiP54793.

    PTM databases

    PhosphoSiteiP54793.

    Expressioni

    Gene expression databases

    BgeeiP54793.
    CleanExiHS_ARSF.
    GenevestigatoriP54793.

    Organism-specific databases

    HPAiHPA000549.

    Interactioni

    Protein-protein interaction databases

    BioGridi106909. 1 interaction.
    IntActiP54793. 1 interaction.
    STRINGi9606.ENSP00000352319.

    Structurei

    3D structure databases

    ProteinModelPortaliP54793.
    SMRiP54793. Positions 29-161, 225-550.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the sulfatase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3119.
    HOGENOMiHOG000135352.
    HOVERGENiHBG004283.
    InParanoidiP54793.
    KOiK12374.
    OMAiFIGTSKH.
    OrthoDBiEOG7QZG9J.
    PhylomeDBiP54793.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P54793-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRPRRPLVFM SLVCALLNTC QAHRVHDDKP NIVLIMVDDL GIGDLGCYGN    50
    DTMRTPHIDR LAREGVRLTQ HISAASLCSP SRSAFLTGRY PIRSGMVSSG 100
    NRRVIQNLAV PAGLPLNETT LAALLKKQGY STGLIGKWHQ GLNCDSRSDQ 150
    CHHPYNYGFD YYYGMPFTLV DSCWPDPSRN TELAFESQLW LCVQLVAIAI 200
    LTLTFGKLSG WVSVPWLLIF SMILFIFLLG YAWFSSHTSP LYWDCLLMRG 250
    HEITEQPMKA ERAGSIMVKE AISFLERHSK ETFLLFFSFL HVHTPLPTTD 300
    DFTGTSKHGL YGDNVEEMDS MVGKILDAID DFGLRNNTLV YFTSDHGGHL 350
    EARRGHAQLG GWNGIYKGGK GMGGWEGGIR VPGIVRWPGK VPAGRLIKEP 400
    TSLMDILPTV ASVSGGSLPQ DRVIDGRDLM PLLQGNVRHS EHEFLFHYCG 450
    SYLHAVRWIP KDDSGSVWKA HYVTPVFQPP ASGGCYVTSL CRCFGEQVTY 500
    HNPPLLFDLS RDPSESTPLT PATEPLHDFV IKKVANALKE HQETIVPVTY 550
    QLSELNQGRT WLKPCCGVFP FCLCDKEEEV SQPRGPNEKR 590
    Length:590
    Mass (Da):65,940
    Last modified:September 22, 2009 - v4
    Checksum:iEA9B7289040AE79A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 2910CQAHRVHDDK → WPGHTGCMTTR in CAA66462. (PubMed:9192838)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti527 – 5271H → Y.2 Publications
    Corresponds to variant rs1052638 [ dbSNP | Ensembl ].
    VAR_058846

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97868 mRNA. Translation: CAA66462.1.
    AC112653 Genomic DNA. No translation available.
    BC022389 mRNA. Translation: AAH22389.1.
    CCDSiCCDS14123.1.
    PIRiA56217.
    RefSeqiNP_001188467.1. NM_001201538.1.
    NP_001188468.1. NM_001201539.1.
    NP_004033.2. NM_004042.4.
    UniGeneiHs.101674.

    Genome annotation databases

    EnsembliENST00000359361; ENSP00000352319; ENSG00000062096.
    ENST00000381127; ENSP00000370519; ENSG00000062096.
    GeneIDi416.
    KEGGihsa:416.
    UCSCiuc004cre.2. human.

    Polymorphism databases

    DMDMi259016386.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97868 mRNA. Translation: CAA66462.1 .
    AC112653 Genomic DNA. No translation available.
    BC022389 mRNA. Translation: AAH22389.1 .
    CCDSi CCDS14123.1.
    PIRi A56217.
    RefSeqi NP_001188467.1. NM_001201538.1.
    NP_001188468.1. NM_001201539.1.
    NP_004033.2. NM_004042.4.
    UniGenei Hs.101674.

    3D structure databases

    ProteinModelPortali P54793.
    SMRi P54793. Positions 29-161, 225-550.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106909. 1 interaction.
    IntActi P54793. 1 interaction.
    STRINGi 9606.ENSP00000352319.

    PTM databases

    PhosphoSitei P54793.

    Polymorphism databases

    DMDMi 259016386.

    Proteomic databases

    PaxDbi P54793.
    PRIDEi P54793.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359361 ; ENSP00000352319 ; ENSG00000062096 .
    ENST00000381127 ; ENSP00000370519 ; ENSG00000062096 .
    GeneIDi 416.
    KEGGi hsa:416.
    UCSCi uc004cre.2. human.

    Organism-specific databases

    CTDi 416.
    GeneCardsi GC0XP002978.
    H-InvDB HIX0016636.
    HGNCi HGNC:721. ARSF.
    HPAi HPA000549.
    MIMi 300003. gene.
    neXtProti NX_P54793.
    PharmGKBi PA25012.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3119.
    HOGENOMi HOG000135352.
    HOVERGENi HBG004283.
    InParanoidi P54793.
    KOi K12374.
    OMAi FIGTSKH.
    OrthoDBi EOG7QZG9J.
    PhylomeDBi P54793.
    TreeFami TF314186.

    Enzyme and pathway databases

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

    Miscellaneous databases

    GenomeRNAii 416.
    NextBioi 1759.
    PROi P54793.
    SOURCEi Search...

    Gene expression databases

    Bgeei P54793.
    CleanExi HS_ARSF.
    Genevestigatori P54793.

    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. "Identification by shotgun sequencing, genomic organization, and functional analysis of a fourth arylsulfatase gene (ARSF) from the Xp22.3 region."
      Puca A.A., Zollo M., Repetto M., Andolfi G., Guffanti A., Simon G., Ballabio A., Franco B.
      Genomics 42:192-199(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TYR-527.
      Tissue: Fetal brain.
    2. "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].
    3. "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], VARIANT TYR-527.
      Tissue: Kidney.
    4. "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] OF 369-422.
      Tissue: Kidney.

    Entry informationi

    Entry nameiARSF_HUMAN
    AccessioniPrimary (citable) accession number: P54793
    Secondary accession number(s): Q8TCC5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 116 of the entry and version 4 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