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Arylsulfatase E (ASE) (EC 3.1.6.-)

 ARSE_HUMAN              Reviewed;         589 AA.
P51690; Q53FT2; Q53FU8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 2.
20-JUN-2018, entry version 153.
RecName: Full=Arylsulfatase E;
Short=ASE;
EC=3.1.6.-;
Flags: Precursor;
Name=ARSE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS CDPX1 SER-12; PRO-111;
ARG-117; VAL-137 AND ARG-245.
TISSUE=Kidney;
PubMed=7720070; DOI=10.1016/0092-8674(95)90367-4;
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.;
"A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia
punctata (CDPX) and implications for warfarin embryopathy.";
Cell 81:15-25(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-424.
TISSUE=Kidney proximal tubule, and Pancreas;
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.
[3]
CHARACTERIZATION.
PubMed=9497243; DOI=10.1086/301746;
Daniele A., Parenti G., D'Addio M., Andria G., Ballabio A., Meroni G.;
"Biochemical characterization of arylsulfatase E and functional
analysis of mutations found in patients with X-linked chondrodysplasia
punctata.";
Am. J. Hum. Genet. 62:562-572(1998).
[4]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[5]
VARIANT CDPX1 TYR-492.
PubMed=9409863;
DOI=10.1002/(SICI)1096-8628(19971212)73:2<139::AID-AJMG7>3.0.CO;2-P;
Parenti G., Buttitta P., Meroni G., Franco B., Bernard L.,
Rizzolo M.G., Brunetti-Pierri N., Ballabio A., Andria G.;
"X-linked recessive chondrodysplasia punctata due to a new point
mutation of the ARSE gene.";
Am. J. Med. Genet. 73:139-143(1997).
[6]
VARIANTS CDPX1 ASN-80; MET-481 AND SER-578.
PubMed=12567415; DOI=10.1002/ajmg.a.10950;
Brunetti-Pierri N., Andreucci M.V., Tuzzi R., Vega G.R., Gray G.,
McKeown C., Ballabio A., Andria G., Meroni G., Parenti G.;
"X-linked recessive chondrodysplasia punctata: spectrum of
arylsulfatase E gene mutations and expanded clinical variability.";
Am. J. Med. Genet. A 117:164-168(2003).
-!- FUNCTION: May be essential for the correct composition of
cartilage and bone matrix during development. Has no activity
toward steroid sulfates.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by millimolar concentrations of
warfarin.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.;
Temperature dependence:
Almost completely inactivated after 10 minutes at 50 degrees
Celsius.;
-!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack.
-!- TISSUE SPECIFICITY: Expressed in the pancreas, liver and kidney.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:19159218}.
-!- PTM: 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. {ECO:0000250}.
-!- DISEASE: Chondrodysplasia punctata 1, X-linked recessive (CDPX1)
[MIM:302950]: 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.
{ECO:0000269|PubMed:12567415, ECO:0000269|PubMed:7720070,
ECO:0000269|PubMed:9409863}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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EMBL; X83573; CAA58556.1; -; mRNA.
EMBL; AK223183; BAD96903.1; -; mRNA.
EMBL; AK223199; BAD96919.1; -; mRNA.
CCDS; CCDS14122.1; -.
PIR; I37187; I37187.
RefSeq; NP_000038.2; NM_000047.2.
RefSeq; XP_005274576.1; XM_005274519.4.
UniGene; Hs.386975; -.
ProteinModelPortal; P51690; -.
SMR; P51690; -.
BioGrid; 106908; 26.
IntAct; P51690; 4.
STRING; 9606.ENSP00000370526; -.
iPTMnet; P51690; -.
PhosphoSitePlus; P51690; -.
BioMuta; ARSE; -.
DMDM; 77416850; -.
MaxQB; P51690; -.
PaxDb; P51690; -.
PeptideAtlas; P51690; -.
PRIDE; P51690; -.
ProteomicsDB; 56377; -.
DNASU; 415; -.
Ensembl; ENST00000381134; ENSP00000370526; ENSG00000157399.
GeneID; 415; -.
KEGG; hsa:415; -.
UCSC; uc004crc.5; human.
CTD; 415; -.
DisGeNET; 415; -.
EuPathDB; HostDB:ENSG00000157399.14; -.
GeneCards; ARSE; -.
GeneReviews; ARSE; -.
HGNC; HGNC:719; ARSE.
HPA; HPA060518; -.
HPA; HPA070651; -.
MalaCards; ARSE; -.
MIM; 300180; gene.
MIM; 302950; phenotype.
neXtProt; NX_P51690; -.
OpenTargets; ENSG00000157399; -.
Orphanet; 79345; Brachytelephalangic chondrodysplasia punctata.
PharmGKB; PA25010; -.
eggNOG; KOG3867; Eukaryota.
eggNOG; COG3119; LUCA.
GeneTree; ENSGT00760000119062; -.
HOVERGEN; HBG004283; -.
InParanoid; P51690; -.
KO; K18222; -.
PhylomeDB; P51690; -.
TreeFam; TF314186; -.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
Reactome; R-HSA-1663150; The activation of arylsulfatases.
ChiTaRS; ARSE; human.
GeneWiki; Arylsulfatase_E; -.
GenomeRNAi; 415; -.
PRO; PR:P51690; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000157399; -.
CleanEx; HS_ARSE; -.
ExpressionAtlas; P51690; baseline and differential.
Genevisible; P51690; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
GO; GO:0004065; F:arylsulfatase activity; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008152; P:metabolic process; IEA:InterPro.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
Gene3D; 3.40.720.10; -; 3.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR024607; Sulfatase_CS.
InterPro; IPR000917; Sulfatase_N.
Pfam; PF00884; Sulfatase; 1.
SUPFAM; SSF53649; SSF53649; 1.
PROSITE; PS00523; SULFATASE_1; 1.
PROSITE; PS00149; SULFATASE_2; 1.
1: Evidence at protein level;
Calcium; Complete proteome; Disease mutation; Glycoprotein;
Golgi apparatus; Hydrolase; Metal-binding; Reference proteome; Signal.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 589 Arylsulfatase E.
/FTId=PRO_0000033425.
ACT_SITE 86 86 Nucleophile.
{ECO:0000250|UniProtKB:P15289}.
ACT_SITE 147 147 {ECO:0000250|UniProtKB:P15289}.
METAL 46 46 Calcium. {ECO:0000250}.
METAL 47 47 Calcium. {ECO:0000250}.
METAL 86 86 Calcium; via 3-oxoalanine. {ECO:0000250}.
METAL 353 353 Calcium. {ECO:0000250}.
METAL 354 354 Calcium. {ECO:0000250}.
BINDING 145 145 Substrate. {ECO:0000250}.
BINDING 301 301 Substrate. {ECO:0000250}.
BINDING 378 378 Substrate. {ECO:0000250}.
MOD_RES 86 86 3-oxoalanine (Cys).
{ECO:0000250|UniProtKB:P15289}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 344 344 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 12 12 R -> S (in CDPX1; dbSNP:rs122460151).
{ECO:0000269|PubMed:7720070}.
/FTId=VAR_007307.
VARIANT 80 80 I -> N (in CDPX1).
{ECO:0000269|PubMed:12567415}.
/FTId=VAR_023570.
VARIANT 111 111 R -> P (in CDPX1; dbSNP:rs122460153).
{ECO:0000269|PubMed:7720070}.
/FTId=VAR_007308.
VARIANT 117 117 G -> R (in CDPX1; dbSNP:rs122460152).
{ECO:0000269|PubMed:7720070}.
/FTId=VAR_007309.
VARIANT 137 137 G -> V (in CDPX1; dbSNP:rs80338711).
{ECO:0000269|PubMed:7720070}.
/FTId=VAR_007310.
VARIANT 183 183 R -> H (in dbSNP:rs34412194).
/FTId=VAR_037974.
VARIANT 245 245 G -> R (in CDPX1; dbSNP:rs122460154).
{ECO:0000269|PubMed:7720070}.
/FTId=VAR_007311.
VARIANT 424 424 G -> S (in dbSNP:rs35143646).
{ECO:0000269|Ref.2}.
/FTId=VAR_037975.
VARIANT 481 481 T -> M (in CDPX1; dbSNP:rs80338713).
{ECO:0000269|PubMed:12567415}.
/FTId=VAR_023571.
VARIANT 492 492 C -> Y (in CDPX1; dbSNP:rs122460155).
{ECO:0000269|PubMed:9409863}.
/FTId=VAR_007312.
VARIANT 578 578 P -> S (in CDPX1; dbSNP:rs28935474).
{ECO:0000269|PubMed:12567415}.
/FTId=VAR_023572.
CONFLICT 168 168 D -> E (in Ref. 1; CAA58556).
{ECO:0000305}.
SEQUENCE 589 AA; 65669 MW; 37A941EF4A44027A CRC64;
MLHLHHSCLC FRSWLPAMLA VLLSLAPSAS SDISASRPNI LLLMADDLGI GDIGCYGNNT
MRTPNIDRLA EDGVKLTQHI SAASLCTPSR AAFLTGRYPV RSGMVSSIGY RVLQWTGASG
GLPTNETTFA KILKEKGYAT GLIGKWHLGL NCESASDHCH HPLHHGFDHF YGMPFSLMGD
CARWELSEKR VNLEQKLNFL FQVLALVALT LVAGKLTHLI PVSWMPVIWS ALSAVLLLAS
SYFVGALIVH ADCFLMRNHT ITEQPMCFQR TTPLILQEVA SFLKRNKHGP FLLFVSFLHV
HIPLITMENF LGKSLHGLYG DNVEEMDWMV GRILDTLDVE GLSNSTLIYF TSDHGGSLEN
QLGNTQYGGW NGIYKGGKGM GGWEGGIRVP GIFRWPGVLP AGRVIGEPTS LMDVFPTVVR
LAGGEVPQDR VIDGQDLLPL LLGTAQHSDH EFLMHYCERF LHAARWHQRD RGTMWKVHFV
TPVFQPEGAG ACYGRKVCPC FGEKVVHHDP PLLFDLSRDP SETHILTPAS EPVFYQVMER
VQQAVWEHQR TLSPVPLQLD RLGNIWRPWL QPCCGPFPLC WCLREDDPQ


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