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P50428 (ARSA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arylsulfatase A

Short name=ASA
EC=3.1.6.8
Alternative name(s):
Cerebroside-sulfatase
Gene names
Name:Arsa
Synonyms:As2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length506 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Hydrolyzes cerebroside sulfate.

Catalytic activity

A cerebroside 3-sulfate + H2O = a cerebroside + sulfate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Homodimer at neutral pH and homooctamer at acidic pH. Exists both as a single chain of 58 kDa (component A) or as a chain of 50 kDa (component B) linked by disulfide bond(s) to a 7 kDa chain (component C). Interacts with SUMF1 By similarity.

Subcellular location

Lysosome.

Post-translational modification

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.

Sequence similarities

Belongs to the sulfatase family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processautophagy

Inferred from electronic annotation. Source: Ensembl

binding of sperm to zona pellucida

Inferred from mutant phenotype PubMed 12080020. Source: MGI

central nervous system development

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to methylmercury

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to pH

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: Ensembl

extrinsic component of external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from direct assay PubMed 12080020. Source: MGI

lysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 12080020. Source: MGI

   Molecular_functionarylsulfatase activity

Inferred from electronic annotation. Source: Ensembl

calcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

cerebroside-sulfatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

sulfuric ester hydrolase activity

Inferred from sequence orthology PubMed 15962010. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 506489Arylsulfatase A
PRO_0000033420

Sites

Active site1241 By similarity
Metal binding281Calcium By similarity
Metal binding291Calcium By similarity
Metal binding681Calcium; via 3-oxoalanine By similarity
Metal binding2801Calcium By similarity
Metal binding2811Calcium By similarity
Binding site1221Substrate By similarity
Binding site1491Substrate By similarity
Binding site2281Substrate By similarity
Binding site3011Substrate By similarity

Amino acid modifications

Modified residue6813-oxoalanine (Cys) By similarity
Glycosylation1571N-linked (GlcNAc...) Potential
Glycosylation1831N-linked (GlcNAc...) Potential
Glycosylation3491N-linked (GlcNAc...) Potential
Disulfide bond155 ↔ 171 By similarity
Disulfide bond160 ↔ 167 By similarity
Disulfide bond299 ↔ 413 By similarity
Disulfide bond487 ↔ 499 By similarity
Disulfide bond488 ↔ 501 By similarity
Disulfide bond492 ↔ 498 By similarity

Experimental info

Sequence conflict851G → A in CAA51702. Ref.1
Sequence conflict851G → A in CAA51703. Ref.1
Sequence conflict1041V → L in CAA51702. Ref.1
Sequence conflict1041V → L in CAA51703. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P50428 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: A12DFA369D65B1AD

FASTA50653,748
        10         20         30         40         50         60 
MALGTLFLAL AAGLSTASPP NILLIFADDL GYGDLGSYGH PSSTTPNLDQ LAEGGLRFTD 

        70         80         90        100        110        120 
FYVPVSLCTP SRAALLTGRL PVRSGMYPGV LGPSSQGGLP LEEVTLAEVL AARGYLTGMA 

       130        140        150        160        170        180 
GKWHLGVGPE GAFLPPHQGF HRFLGIPYSH DQGPCQNLTC FPPDIPCKGG CDQGLVPIPL 

       190        200        210        220        230        240 
LANLTVEAQP PWLPGLEARY VSFSRDLMAD AQRQGRPFFL YYASHHTHYP QFSGQSFTKR 

       250        260        270        280        290        300 
SGRGPFGDSL MELDGAVGAL MTTVGDLGLL EETLVIFTAD NGPELMRMSN GGCSGLLRCG 

       310        320        330        340        350        360 
KGTTFEGGVR EPALVYWPGH ITPGVTHELA SSLDLLPTLA ALTGAPLPNV TLDGVDISPL 

       370        380        390        400        410        420 
LLGTGKSPRK SVFFYPPYPD EIHGVFAVRN GKYKAHFFTQ GSAHSDTTSD PACHAANRLT 

       430        440        450        460        470        480 
AHEPPLLYDL SQDPGENYNV LESIEGVSPE ALQALKHIQL LKAQYDAAMT FGPSQIAKGE 

       490        500 
DPALQICCQP SCTPHPVCCH CPGSQS 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the mouse arylsulfatase A gene and cDNA."
Kreysing J., Polten A., Hess B., von Figura K., Menz K., Steiner F., Gieselmann V.
Genomics 19:249-256(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/Sv and C57BL/6J.
[2]"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. expand/collapse author list , 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].
Strain: C57BL/6J.
Tissue: Lung and Skin.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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].
Tissue: Mammary tumor and Trophoblast stem cell.
[5]"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 32-66.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73230 mRNA. Translation: CAA51702.1.
X73231 Genomic DNA. Translation: CAA51703.1.
AK004540 mRNA. Translation: BAB23356.1.
AK132501 mRNA. Translation: BAE21207.1.
CH466550 Genomic DNA. Translation: EDL04336.1.
BC011284 mRNA. Translation: AAH11284.1.
BC098075 mRNA. Translation: AAH98075.1.
M82876 mRNA. Translation: AAA37260.1.
PIRA54190.
RefSeqNP_033843.2. NM_009713.4.
UniGeneMm.620.

3D structure databases

ProteinModelPortalP50428.
SMRP50428. Positions 19-502.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP50428. 2 interactions.
MINTMINT-4128568.
STRING10090.ENSMUSP00000023292.

Proteomic databases

PaxDbP50428.
PRIDEP50428.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000165199; ENSMUSP00000127646; ENSMUSG00000022620.
GeneID11883.
KEGGmmu:11883.
UCSCuc007xgy.2. mouse.

Organism-specific databases

CTD410.
MGIMGI:88077. Arsa.

Phylogenomic databases

eggNOGCOG3119.
GeneTreeENSGT00560000076940.
HOGENOMHOG000135352.
HOVERGENHBG004283.
InParanoidQ9DC66.
KOK01134.
OMASCCHCPE.
OrthoDBEOG7QZG9J.
PhylomeDBP50428.
TreeFamTF314186.

Enzyme and pathway databases

SABIO-RKP50428.

Gene expression databases

BgeeP50428.
CleanExMM_ARSA.
GenevestigatorP50428.

Family and domain databases

Gene3D3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMSSF53649. SSF53649. 1 hit.
PROSITEPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279915.
PROP50428.
SOURCESearch...

Entry information

Entry nameARSA_MOUSE
AccessionPrimary (citable) accession number: P50428
Secondary accession number(s): Q9DC66
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot