Reviewed, UniProtKB/Swiss-Prot P51690 (ARSE_HUMAN)

Names and origin

Protein names

Recommended name:
    Arylsulfatase E
      Short name(s)=ASE
    EC=3.1.6.-

Gene names

Name:

ARSE

Organism

Homo sapiens (Human)

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	Golgi apparatus › Golgi stack.
Tissue specificity	Expressed in the pancreas, liver and kidney.
Post-translational modification	N-glycosylated.
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.
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
Gene Ontology (GO)
Biological process	skeletal development Ref.1 Traceable author statement. Source: ProtInc
Molecular function	arylsulfatase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Signal peptide	1 – 31	31	Potential
	Chain	32 – 589	558	Arylsulfatase E
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
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...) Potential
	Glycosylation	258	1	N-linked (GlcNAc...) Potential
	Glycosylation	344	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	12	1	R → S in CDPX1.
	Natural variant	80	1	I → N in CDPX1.
	Natural variant	111	1	R → P in CDPX1.
	Natural variant	117	1	G → R in CDPX1.
	Natural variant	137	1	G → V in CDPX1.
	Natural variant	183	1	R → H: dbSNP rs34412194.
	Natural variant	245	1	G → R in CDPX1.
	Natural variant	424	1	G → S: dbSNP rs35143646.
	Natural variant	481	1	T → M in CDPX1.
	Natural variant	492	1	C → Y in CDPX1.
	Natural variant	578	1	P → S in CDPX1. dbSNP rs28935474.
Experimental info
	Sequence conflict	168	1	D → E in CAA58556. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P51690-1 [UniParc]. Last modified October 11, 2005. Version 2. Checksum: 37A941EF4A44027A	FASTA	589	65,669
	10 20 30 40 50 60 MLHLHHSCLC FRSWLPAMLA VLLSLAPSAS SDISASRPNI LLLMADDLGI GDIGCYGNNT 70 80 90 100 110 120 MRTPNIDRLA EDGVKLTQHI SAASLCTPSR AAFLTGRYPV RSGMVSSIGY RVLQWTGASG 130 140 150 160 170 180 GLPTNETTFA KILKEKGYAT GLIGKWHLGL NCESASDHCH HPLHHGFDHF YGMPFSLMGD 190 200 210 220 230 240 CARWELSEKR VNLEQKLNFL FQVLALVALT LVAGKLTHLI PVSWMPVIWS ALSAVLLLAS 250 260 270 280 290 300 SYFVGALIVH ADCFLMRNHT ITEQPMCFQR TTPLILQEVA SFLKRNKHGP FLLFVSFLHV 310 320 330 340 350 360 HIPLITMENF LGKSLHGLYG DNVEEMDWMV GRILDTLDVE GLSNSTLIYF TSDHGGSLEN 370 380 390 400 410 420 QLGNTQYGGW NGIYKGGKGM GGWEGGIRVP GIFRWPGVLP AGRVIGEPTS LMDVFPTVVR 430 440 450 460 470 480 LAGGEVPQDR VIDGQDLLPL LLGTAQHSDH EFLMHYCERF LHAARWHQRD RGTMWKVHFV 490 500 510 520 530 540 TPVFQPEGAG ACYGRKVCPC FGEKVVHHDP PLLFDLSRDP SETHILTPAS EPVFYQVMER 550 560 570 580 VQQAVWEHQR TLSPVPLQLD RLGNIWRPWL QPCCGPFPLC WCLREDDPQ

References

	« Hide 'large scale' referencesShow '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]	"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.
[5]	"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.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	X83573 mRNA. Translation: CAA58556.1. AK223183 mRNA. Translation: BAD96903.1. AK223199 mRNA. Translation: BAD96919.1.
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...
Genome annotation databases
Ensembl	ENSG00000157399. Homo sapiens. [Contig view]
GeneID	415.
KEGG	hsa:415.
Organism-specific databases
HGNC	HGNC:719. ARSE.
MIM	300180. gene. 302950. phenotype.
Orphanet	176. Chondrodysplasia punctata, non rhizomelic type.
PharmGKB	PA25010.
GenAtlas	Search...
GeneCards	Search...
GeneLynx	Search...
Phylogenomic databases
HOVERGEN	P51690.
Gene expression databases
ArrayExpress	P51690.
CleanEx	HS_ARSE.
GermOnline	ENSG00000157399. Homo sapiens.
Family and domain databases
InterPro	IPR017849. Alkaline_Pase-like_a/b/a. IPR000917. Sulphatase. [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]
ProDom	P51690. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
LinkHub	P51690.
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

ARSE_HUMAN

Accession

Primary (citable) accession number: P51690
Secondary accession number(s): Q53FT2, Q53FU8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 11, 2005
Last modified:	July 22, 2008
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)