P54793 (ARSF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arylsulfatase F
Short name=ASF
EC=3.1.6.-

Gene names

Name:

ARSF

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	590 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)

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.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycosphingolipid metabolic process Traceable author statement. Source: Reactome phospholipid metabolic process Traceable author statement. Source: Reactome post-translational protein modification Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum lumen Traceable author statement. Source: Reactome extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	arylsulfatase activity Traceable author statement Ref.1. Source: ProtInc metal ion binding Inferred 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 – 22	22	Potential
	Chain	23 – 590	568	Arylsulfatase F		PRO_0000033427
Sites
	Active site	139	1	By similarity
	Metal binding	38	1	Calcium By similarity
	Metal binding	39	1	Calcium By similarity
	Metal binding	78	1	Calcium; via 3-oxoalanine By similarity
	Metal binding	345	1	Calcium By similarity
	Metal binding	346	1	Calcium By similarity
	Binding site	137	1	Substrate By similarity
	Binding site	293	1	Substrate By similarity
	Binding site	370	1	Substrate By similarity
Amino acid modifications
	Modified residue	78	1	3-oxoalanine (Cys) By similarity
	Glycosylation	50	1	N-linked (GlcNAc...) Potential
	Glycosylation	117	1	N-linked (GlcNAc...) Potential
	Glycosylation	336	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	527	1	H → Y. Ref.1 Ref.3 Corresponds to variant rs1052638 [ dbSNP | Ensembl ].		VAR_058846
Experimental info
	Sequence conflict	20 – 29	10	CQAHRVHDDK → WPGHTGCMTTR in CAA66462. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P54793 [UniParc]. Last modified September 22, 2009. Version 4. Checksum: EA9B7289040AE79A	FASTA	590	65,940
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00008405.
PIR	A56217.
RefSeq	NP_001188467.1. NM_001201538.1. NP_001188468.1. NM_001201539.1. NP_004033.2. NM_004042.4.
UniGene	Hs.101674.
3D structure databases
ProteinModelPortal	P54793.
ModBase	Search...
Protein-protein interaction databases
IntAct	P54793. 1 interaction.
STRING	9606.ENSP00000352319.
PTM databases
PhosphoSite	P54793.
Polymorphism databases
DMDM	259016386.
Proteomic databases
PaxDb	P54793.
PRIDE	P54793.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000359361; ENSP00000352319; ENSG00000062096. ENST00000381127; ENSP00000370519; ENSG00000062096. ENST00000537104; ENSP00000445594; ENSG00000062096.
GeneID	416.
KEGG	hsa:416.
UCSC	uc004cre.2. human.
Organism-specific databases
CTD	416.
GeneCards	GC0XP002978.
H-InvDB	HIX0016636.
HGNC	HGNC:721. ARSF.
HPA	HPA000549.
MIM	300003. gene.
neXtProt	NX_P54793.
PharmGKB	PA25012.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3119.
HOGENOM	HOG000135352.
HOVERGEN	HBG004283.
InParanoid	P54793.
KO	K12374.
OMA	LKPCCGV.
OrthoDB	EOG4V4379.
PhylomeDB	P54793.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_17015. Metabolism of proteins.
Gene expression databases
Bgee	P54793.
CleanEx	HS_ARSF.
Genevestigator	P54793.
GermOnline	ENSG00000062096. Homo sapiens.
Family and domain databases
Gene3D	3.40.720.10. 2 hits.
InterPro	IPR017849. Alkaline_Pase-like_a/b/a. IPR017850. Alkaline_phosphatase_core. IPR000917. Sulfatase. IPR024607. Sulfatase_CS. [Graphical view]
Pfam	PF00884. Sulfatase. 1 hit. [Graphical view]
SUPFAM	SSF53649. Alkaline_phosphatase_core. 1 hit.
PROSITE	PS00523. SULFATASE_1. 1 hit. PS00149. SULFATASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	416.
NextBio	1759.
SOURCE	Search...

Entry information

Entry name

ARSF_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 104 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.