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Protein

Arylsulfatase F

Gene

ARSF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ 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
Complete GO annotation...

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 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:721. ARSF.

Subcellular locationi

  1. Secreted Curated

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25012.

Polymorphism and mutation databases

BioMutaiARSF.
DMDMi259016386.

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. 2 interactions.
IntActiP54793. 1 interaction.
STRINGi9606.ENSP00000352319.

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00760000119062.
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

        10         20         30         40         50
MRPRRPLVFM SLVCALLNTC QAHRVHDDKP NIVLIMVDDL GIGDLGCYGN
60 70 80 90 100
DTMRTPHIDR LAREGVRLTQ HISAASLCSP SRSAFLTGRY PIRSGMVSSG
110 120 130 140 150
NRRVIQNLAV PAGLPLNETT LAALLKKQGY STGLIGKWHQ GLNCDSRSDQ
160 170 180 190 200
CHHPYNYGFD YYYGMPFTLV DSCWPDPSRN TELAFESQLW LCVQLVAIAI
210 220 230 240 250
LTLTFGKLSG WVSVPWLLIF SMILFIFLLG YAWFSSHTSP LYWDCLLMRG
260 270 280 290 300
HEITEQPMKA ERAGSIMVKE AISFLERHSK ETFLLFFSFL HVHTPLPTTD
310 320 330 340 350
DFTGTSKHGL YGDNVEEMDS MVGKILDAID DFGLRNNTLV YFTSDHGGHL
360 370 380 390 400
EARRGHAQLG GWNGIYKGGK GMGGWEGGIR VPGIVRWPGK VPAGRLIKEP
410 420 430 440 450
TSLMDILPTV ASVSGGSLPQ DRVIDGRDLM PLLQGNVRHS EHEFLFHYCG
460 470 480 490 500
SYLHAVRWIP KDDSGSVWKA HYVTPVFQPP ASGGCYVTSL CRCFGEQVTY
510 520 530 540 550
HNPPLLFDLS RDPSESTPLT PATEPLHDFV IKKVANALKE HQETIVPVTY
560 570 580 590
QLSELNQGRT WLKPCCGVFP FCLCDKEEEV SQPRGPNEKR
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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiARSF.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi106909. 2 interactions.
IntActiP54793. 1 interaction.
STRINGi9606.ENSP00000352319.

PTM databases

PhosphoSiteiP54793.

Polymorphism and mutation databases

BioMutaiARSF.
DMDMi259016386.

Proteomic databases

PaxDbiP54793.
PRIDEiP54793.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi416.
GeneCardsiGC0XP002978.
H-InvDBHIX0016636.
HGNCiHGNC:721. ARSF.
HPAiHPA000549.
MIMi300003. gene.
neXtProtiNX_P54793.
PharmGKBiPA25012.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135352.
HOVERGENiHBG004283.
InParanoidiP54793.
KOiK12374.
OMAiFIGTSKH.
OrthoDBiEOG7QZG9J.
PhylomeDBiP54793.
TreeFamiTF314186.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii416.
NextBioi1759.
PROiP54793.
SOURCEiSearch...

Gene expression databases

BgeeiP54793.
CleanExiHS_ARSF.
GenevestigatoriP54793.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 121 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.