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P54793 (ARSF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 F

Short name=ASF
EC=3.1.6.-
Gene names
Name:ARSF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length590 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Cofactor

Binds 1 calcium ion per subunit By similarity.

Enzyme regulation

Not inhibited by DHEAS or warfarin.

Subcellular location

Secreted Potential.

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.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 590568Arylsulfatase F
PRO_0000033427

Sites

Active site1391 By similarity
Metal binding381Calcium By similarity
Metal binding391Calcium By similarity
Metal binding781Calcium; via 3-oxoalanine By similarity
Metal binding3451Calcium By similarity
Metal binding3461Calcium By similarity
Binding site1371Substrate By similarity
Binding site2931Substrate By similarity
Binding site3701Substrate By similarity

Amino acid modifications

Modified residue7813-oxoalanine (Cys) By similarity
Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential

Natural variations

Natural variant5271H → Y. Ref.1 Ref.3
Corresponds to variant rs1052638 [ dbSNP | Ensembl ].
VAR_058846

Experimental info

Sequence conflict20 – 2910CQAHRVHDDK → WPGHTGCMTTR in CAA66462. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54793 [UniParc].

Last modified September 22, 2009. Version 4.
Checksum: EA9B7289040AE79A

FASTA59065,940
        10         20         30         40         50         60 
MRPRRPLVFM SLVCALLNTC QAHRVHDDKP NIVLIMVDDL GIGDLGCYGN DTMRTPHIDR 

        70         80         90        100        110        120 
LAREGVRLTQ HISAASLCSP SRSAFLTGRY PIRSGMVSSG NRRVIQNLAV PAGLPLNETT 

       130        140        150        160        170        180 
LAALLKKQGY STGLIGKWHQ GLNCDSRSDQ CHHPYNYGFD YYYGMPFTLV DSCWPDPSRN 

       190        200        210        220        230        240 
TELAFESQLW LCVQLVAIAI LTLTFGKLSG WVSVPWLLIF SMILFIFLLG YAWFSSHTSP 

       250        260        270        280        290        300 
LYWDCLLMRG HEITEQPMKA ERAGSIMVKE AISFLERHSK ETFLLFFSFL HVHTPLPTTD 

       310        320        330        340        350        360 
DFTGTSKHGL YGDNVEEMDS MVGKILDAID DFGLRNNTLV YFTSDHGGHL EARRGHAQLG 

       370        380        390        400        410        420 
GWNGIYKGGK GMGGWEGGIR VPGIVRWPGK VPAGRLIKEP TSLMDILPTV ASVSGGSLPQ 

       430        440        450        460        470        480 
DRVIDGRDLM PLLQGNVRHS EHEFLFHYCG SYLHAVRWIP KDDSGSVWKA HYVTPVFQPP 

       490        500        510        520        530        540 
ASGGCYVTSL CRCFGEQVTY HNPPLLFDLS RDPSESTPLT PATEPLHDFV IKKVANALKE 

       550        560        570        580        590 
HQETIVPVTY QLSELNQGRT WLKPCCGVFP FCLCDKEEEV SQPRGPNEKR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X97868 mRNA. Translation: CAA66462.1.
AC112653 Genomic DNA. No translation available.
BC022389 mRNA. Translation: AAH22389.1.
PIRA56217.
RefSeqNP_001188467.1. NM_001201538.1.
NP_001188468.1. NM_001201539.1.
NP_004033.2. NM_004042.4.
UniGeneHs.101674.

3D structure databases

ProteinModelPortalP54793.
SMRP54793. Positions 26-577.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106909. 1 interaction.
IntActP54793. 1 interaction.
STRING9606.ENSP00000352319.

PTM databases

PhosphoSiteP54793.

Polymorphism databases

DMDM259016386.

Proteomic databases

PaxDbP54793.
PRIDEP54793.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359361; ENSP00000352319; ENSG00000062096.
ENST00000381127; ENSP00000370519; ENSG00000062096.
ENST00000537104; ENSP00000445594; ENSG00000062096.
GeneID416.
KEGGhsa:416.
UCSCuc004cre.2. human.

Organism-specific databases

CTD416.
GeneCardsGC0XP002978.
H-InvDBHIX0016636.
HGNCHGNC:721. ARSF.
HPAHPA000549.
MIM300003. gene.
neXtProtNX_P54793.
PharmGKBPA25012.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3119.
HOGENOMHOG000135352.
HOVERGENHBG004283.
InParanoidP54793.
KOK12374.
OMAFIGTSKH.
OrthoDBEOG7QZG9J.
PhylomeDBP54793.
TreeFamTF314186.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.

Gene expression databases

BgeeP54793.
CleanExHS_ARSF.
GenevestigatorP54793.

Family and domain databases

Gene3D3.40.720.10. 2 hits.
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

GenomeRNAi416.
NextBio1759.
PROP54793.
SOURCESearch...

Entry information

Entry nameARSF_HUMAN
AccessionPrimary (citable) accession number: P54793
Secondary accession number(s): Q8TCC5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 22, 2009
Last modified: April 16, 2014
This is version 112 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM