Reviewed,
UniProtKB/Swiss-Prot P51690 (ARSE_HUMAN)
Last modified
November 3, 2009.
Version 79.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Arylsulfatase E Short name=ASE EC=3.1.6.- | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Complete proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 589 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | May be essential for the correct composition of cartilage and bone matrix during development. Has no activity toward steroid sulfates. |
| Cofactor | Binds 1 calcium ion per subunit By similarity. |
| Enzyme regulation | Inhibited by millimolar concentrations of warfarin. |
| Subcellular location | |
| Tissue specificity | Expressed in the pancreas, liver and kidney. |
| Post-translational modification | N-glycosylated. Ref.4 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. |
| Involvement in disease | Defects in ARSE are the cause of chondrodysplasia punctata X-linked recessive type 1 (CDPX1) [MIM:302950]. CDP is a clinically and genetically heterogeneous disorder characterized by punctiform calcification of the bones. CDPX1 is a congenital defect of bone and cartilage development characterized by aberrant bone mineralization, severe underdevelopment of nasal cartilage, and distal phalangeal hypoplasia. This disease can also be induced by inhibition with the drug warfarin. Ref.1 Ref.5 Ref.6 |
| Sequence similarities | Belongs to the sulfatase family. |
| Biophysicochemical properties | pH dependence: Optimum pH is 7. Temperature dependence: Almost completely inactivated after 10 minutes at 50 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Golgi apparatus |
| Disease | Disease mutation |
| Domain | Signal |
| Ligand | Calcium Metal-binding |
| Molecular function | Hydrolase |
| PTM | Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | metabolic process Inferred from electronic annotation. Source: InterPro skeletal system development Ref.1Traceable author statement. Source: ProtInc |
| Cellular component | Golgi stack Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | arylsulfatase activity Traceable author statement. Source: ProtInc calcium ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 31 | 31 | Potential | ||||||
| Chain | 32 – 589 | 558 | Arylsulfatase E | PRO_0000033425 | |||||
Sites | |||||||||
| Active site | 147 | 1 | By similarity | ||||||
| Metal binding | 46 | 1 | Calcium By similarity | ||||||
| Metal binding | 47 | 1 | Calcium By similarity | ||||||
| Metal binding | 86 | 1 | Calcium; via 3-oxoalanine By similarity | ||||||
| Metal binding | 353 | 1 | Calcium By similarity | ||||||
| Metal binding | 354 | 1 | Calcium By similarity | ||||||
| Binding site | 145 | 1 | Substrate By similarity | ||||||
| Binding site | 301 | 1 | Substrate By similarity | ||||||
| Binding site | 378 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 86 | 1 | 3-oxoalanine (Cys) By similarity | ||||||
| Glycosylation | 58 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 125 | 1 | N-linked (GlcNAc...) Ref.4 | ||||||
| Glycosylation | 258 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 344 | 1 | N-linked (GlcNAc...) Potential | ||||||
Natural variations | |||||||||
| Natural variant | 12 | 1 | R → S in CDPX1. Ref.1 | VAR_007307 | |||||
| Natural variant | 80 | 1 | I → N in CDPX1. Ref.6 | VAR_023570 | |||||
| Natural variant | 111 | 1 | R → P in CDPX1. Ref.1 | VAR_007308 | |||||
| Natural variant | 117 | 1 | G → R in CDPX1. Ref.1 | VAR_007309 | |||||
| Natural variant | 137 | 1 | G → V in CDPX1. Ref.1 | VAR_007310 | |||||
| Natural variant | 183 | 1 | R → H: dbSNP rs34412194. | VAR_037974 | |||||
| Natural variant | 245 | 1 | G → R in CDPX1. Ref.1 | VAR_007311 | |||||
| Natural variant | 424 | 1 | G → S: dbSNP rs35143646. Ref.2 | VAR_037975 | |||||
| Natural variant | 481 | 1 | T → M in CDPX1. Ref.6 | VAR_023571 | |||||
| Natural variant | 492 | 1 | C → Y in CDPX1. Ref.5 | VAR_007312 | |||||
| Natural variant | 578 | 1 | P → S in CDPX1. dbSNP rs28935474. Ref.6 | VAR_023572 | |||||
Experimental info | |||||||||
| Sequence conflict | 168 | 1 | D → E in CAA58556. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 7720070] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS CDPX1 SER-12; PRO-111; ARG-117; VAL-137 AND ARG-245. Tissue: Kidney. |
| [2] | Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-424. Tissue: Kidney proximal tubule and Pancreas. |
| [3] | "Biochemical characterization of arylsulfatase E and functional analysis of mutations found in patients with X-linked chondrodysplasia punctata." Daniele A., Parenti G., D'Addio M., Andria G., Ballabio A., Meroni G. Am. J. Hum. Genet. 62:562-572(1998) [PubMed: 9497243] [Abstract] Cited for: CHARACTERIZATION. |
| [4] | "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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125, MASS SPECTROMETRY. Tissue: Liver. |
| [5] | "X-linked recessive chondrodysplasia punctata due to a new point mutation of the ARSE gene." Parenti G., Buttitta P., Meroni G., Franco B., Bernard L., Rizzolo M.G., Brunetti-Pierri N., Ballabio A., Andria G. Am. J. Med. Genet. 73:139-143(1997) [PubMed: 9409863] [Abstract] Cited for: VARIANT CDPX1 TYR-492. |
| [6] | "X-linked recessive chondrodysplasia punctata: spectrum of arylsulfatase E gene mutations and expanded clinical variability." Brunetti-Pierri N., Andreucci M.V., Tuzzi R., Vega G.R., Gray G., McKeown C., Ballabio A., Andria G., Meroni G., Parenti G. Am. J. Med. Genet. A 117:164-168(2003) [PubMed: 12567415] [Abstract] Cited for: VARIANTS CDPX1 ASN-80; MET-481 AND SER-578. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| X83573 mRNA. Translation: CAA58556.1. AK223183 mRNA. Translation: BAD96903.1. AK223199 mRNA. Translation: BAD96919.1. | |
| IPI | IPI00020005. |
| PIR | I37187. |
| RefSeq | NP_000038.2. |
| UniGene | Hs.386975 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1P49 based on UniProtKB P08842. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P51690. 4 interactions. |
| STRING | P51690. |
Proteomic databases | |
| PRIDE | P51690. |
Genome annotation databases | |
| Ensembl | ENST00000381134; ENSP00000370526; ENSG00000157399; Homo sapiens. [Genome view] ENST00000438544; ENSP00000406528; ENSG00000157399; Homo sapiens. [Genome view] |
| GeneID | 415. |
| KEGG | hsa:415. |
| UCSC | uc004crc.2. human. |
Organism-specific databases | |
| CTD | 415. |
| GeneCards | GC0XM002846. |
| HGNC | HGNC:719. ARSE. |
| MIM | 300180. gene. 302950. phenotype. |
| Orphanet | 79345. Chondrodysplasia punctata, brachytelephalangic. 176. Chondrodysplasia punctata, nonrhizomelic type. |
| PharmGKB | PA25010. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | P51690. |
| OMA | AQHSDHE. |
Gene expression databases | |
| ArrayExpress | P51690. |
| Bgee | P51690. |
| CleanEx | HS_ARSE. |
| Genevestigator | P51690. |
| GermOnline | ENSG00000157399. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR017849. Alkaline_Pase-like_a/b/a. IPR000917. Sulfatase. [Graphical view] |
| Gene3D | G3DSA:3.40.720.10. Alk_phosphtse. 1 hit. |
| Pfam | PF00884. Sulfatase. 1 hit. [Graphical view] |
| PROSITE | PS00523. SULFATASE_1. 1 hit. PS00149. SULFATASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 1755. |
| SOURCE | Search... |
Entry information
| Entry name | ARSE_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P51690 Secondary accession number(s): Q53FT2, Q53FU8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome X Human chromosome X: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


